Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 123 (08 May 2019)
Sequence version 3 (23 Jan 2002)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Cobyrinate a,c-diamide synthase

Gene

cbiA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Is able to use other nucleotide triphosphates as substrate, such as GTP or UTP, although less efficiently than ATP.UniRule annotation1 Publication

Miscellaneous

The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.16 sec(-1).1 Publication
  1. KM=0.74 µM for cobyrinate1 Publication
  2. KM=2.7 µM for ATP1 Publication
  3. KM=53 µM for glutamine1 Publication
  4. KM=26200 µM for ammonia1 Publication

    pH dependencei

    The catalytic activity is essentially constant between pH 6.8 and 8.0.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: adenosylcobalamin biosynthesis

    This protein is involved in step 10 of the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route).1 PublicationUniRule annotation
    Proteins known to be involved in the 10 steps of the subpathway in this organism are:
    1. Sirohydrochlorin cobaltochelatase (cbiK)
    2. Cobalt-precorrin-2 C(20)-methyltransferase (cbiL)
    3. Probable cobalt-factor III C(17)-methyltransferase (cbiH)
    4. Cobalt-precorrin-4 C(11)-methyltransferase (cbiF)
    5. Cobalt-precorrin-5A hydrolase (cbiG)
    6. Cobalt-precorrin-5B C(1)-methyltransferase (cbiD)
    7. Cobalt-precorrin-6A reductase (cbiJ)
    8. Cobalt-precorrin-7 C(5)-methyltransferase (cbiE), Cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (cbiT)
    9. Cobalt-precorrin-8 methylmutase (cbiC)
    10. Cobyrinate a,c-diamide synthase (cbiA)
    This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route), the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei334NucleophileUniRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei438Increases nucleophilicity of active site CysUniRule annotation1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLigase
    Biological processCobalamin biosynthesis
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-13217
    SENT99287:STM2035-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.3.5.11 5542

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P29946

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00148;UER00231

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Cobyrinate a,c-diamide synthaseUniRule annotationCurated (EC:6.3.5.11UniRule annotation)
    Alternative name(s):
    Cobyrinic acid a,c-diamide synthetase1 PublicationUniRule annotation
    Cleaved into the following chain:
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:cbiA1 PublicationUniRule annotation
    Ordered Locus Names:STM2035
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri99287 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001014 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi45D → N: Loss of amidation activity when glutamine is used as substrate, and 750-fold reduction in amidation activity whith ammonia as substrate. 1 Publication1
    Mutagenesisi46Y → A: 26-fold reduction in amidation activity with glutamine as substrate. The affinity for cobyrinate is nearly not affected whereas that for the c-monoamide intermediate decreases by 27-fold. 1 Publication1
    Mutagenesisi47L → A: 10-fold reduction in amidation activity with glutamine as substrate. The affinity for cobyrinate is nearly not affected whereas that for the c-monoamide intermediate decreases by 6-fold. 1 Publication1
    Mutagenesisi48D → N: 500-fold reduction in amidation activity with either glutamine or ammonia as substrate. 1 Publication1
    Mutagenesisi90E → Q: Loss of amidation activity with either glutamine or ammonia as substrate. 1 Publication1
    Mutagenesisi97D → N: 3-fold reduction in amidation activity with glutamine as substrate. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001412691 – 459Cobyrinate a,c-diamide synthaseAdd BLAST459
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternate1 Publication
    ChainiPRO_00004308052 – 459Cobyrinate a,c-diamide synthase, N-terminally processedAdd BLAST458

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P29946

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P29946

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    1 Publication

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini252 – 446GATase cobBQ-typeUniRule annotationAdd BLAST195

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.1 PublicationUniRule annotation

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the CobB/CbiA family.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C0Y Bacteria
    COG1797 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000289958

    KEGG Orthology (KO)

    More...
    KOi
    K02224

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    MYLTNSI

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P29946

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.880, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00027 CobB_CbiA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004484 CbiA_synth
    IPR029062 Class_I_gatase-like
    IPR017929 CobB/CobQ_GATase
    IPR002586 CobQ/CobB/MinD/ParA_Nub-bd_dom
    IPR011698 GATase_3
    IPR027417 P-loop_NTPase

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43873 PTHR43873, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01656 CbiA, 1 hit
    PF07685 GATase_3, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52317 SSF52317, 1 hit
    SSF52540 SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00379 cobB, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51274 GATASE_COBBQ, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P29946-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAARHHAFIL AGTGSGCGKT TVTLGLLRLL QKRALRVQPF KVGPDYLDTG
    60 70 80 90 100
    WHTAICGVAS RNLDSFMLPP PVLNALFCEQ MRQADIAVIE GVMGLYDGYG
    110 120 130 140 150
    VDPNYCSTAA MAKQLGCPVI LLVDGKAVST SLAATVMGFQ HFDPTLNLAG
    160 170 180 190 200
    VIVNRVTSDA HYQLLKNAIE HYCSLPVLGY VPPCDGVALP ERHLGLITAR
    210 220 230 240 250
    ESLVNQQSWH DFAATLEQTV DVDALLSLSV LSALPAGMWP ERPDNTAGAG
    260 270 280 290 300
    LTLALADDEA FNFYYPDNID LLERAGVNIV RFSPLHDRAL PDCQMIWLGG
    310 320 330 340 350
    GYPELYAADL AANTVMLKHL RAAHQRGVAI YAECGGLMYL GSTLEDSGGE
    360 370 380 390 400
    IHQMANIIPG HSKMGKRLTR FGYCEAQAMQ PTLLAAPGEI VRGHEFHYSD
    410 420 430 440 450
    FIPETPAVMA CRKVRDGRVL QEWTGGWQTG NTFASYLHVH FAQRPEMLQH

    WLAAARRVL
    Length:459
    Mass (Da):50,037
    Last modified:January 23, 2002 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE1FEF1B5A37F5C14
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti36R → P in AAA27252 (PubMed:8501034).Curated1
    Sequence conflicti111M → I in AAA27252 (PubMed:8501034).Curated1
    Sequence conflicti128V → I in AAA27252 (PubMed:8501034).Curated1
    Sequence conflicti133A → T in AAA27252 (PubMed:8501034).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    L12006 Genomic DNA Translation: AAA27252.1
    AE006468 Genomic DNA Translation: AAL20939.1
    X63012 Genomic DNA Translation: CAA44740.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S20553

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_460980.1, NC_003197.2
    WP_000741259.1, NC_003197.2

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAL20939; AAL20939; STM2035

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1253556

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    stm:STM2035

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|99287.12.peg.2157

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12006 Genomic DNA Translation: AAA27252.1
    AE006468 Genomic DNA Translation: AAL20939.1
    X63012 Genomic DNA Translation: CAA44740.1
    PIRiS20553
    RefSeqiNP_460980.1, NC_003197.2
    WP_000741259.1, NC_003197.2

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Proteomic databases

    PaxDbiP29946
    PRIDEiP29946

    Genome annotation databases

    EnsemblBacteriaiAAL20939; AAL20939; STM2035
    GeneIDi1253556
    KEGGistm:STM2035
    PATRICifig|99287.12.peg.2157

    Phylogenomic databases

    eggNOGiENOG4105C0Y Bacteria
    COG1797 LUCA
    HOGENOMiHOG000289958
    KOiK02224
    OMAiMYLTNSI
    PhylomeDBiP29946

    Enzyme and pathway databases

    UniPathwayiUPA00148;UER00231
    BioCyciMetaCyc:MONOMER-13217
    SENT99287:STM2035-MONOMER
    BRENDAi6.3.5.11 5542
    SABIO-RKiP29946

    Family and domain databases

    Gene3Di3.40.50.880, 1 hit
    HAMAPiMF_00027 CobB_CbiA, 1 hit
    InterProiView protein in InterPro
    IPR004484 CbiA_synth
    IPR029062 Class_I_gatase-like
    IPR017929 CobB/CobQ_GATase
    IPR002586 CobQ/CobB/MinD/ParA_Nub-bd_dom
    IPR011698 GATase_3
    IPR027417 P-loop_NTPase
    PANTHERiPTHR43873 PTHR43873, 1 hit
    PfamiView protein in Pfam
    PF01656 CbiA, 1 hit
    PF07685 GATase_3, 1 hit
    SUPFAMiSSF52317 SSF52317, 1 hit
    SSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR00379 cobB, 1 hit
    PROSITEiView protein in PROSITE
    PS51274 GATASE_COBBQ, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCBIA_SALTY
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29946
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2002
    Last modified: May 8, 2019
    This is version 123 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again