Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O33194 (G3PP_MYCTU)

Entry version 132 (26 Feb 2020)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

D,L-glycerol 3-phosphate phosphatase

Gene

Rv1692

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Glycerol-phosphate phosphatase with a preference for D-glycerol 3-phosphate (sn-glycerol 1-phosphate) over L-glycerol 3-phosphate (sn-glycerol 3-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+1 Publication, Co2+1 Publication, Mn2+1 PublicationNote: Although Co2+ and Mn2+ support eight- and fourfold higher catalytic efficiency than Mg2+, respectively, Mg2+ is likely the physiologically relevant catalytic divalent metal ion.1 Publication

<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 0.77 sec(-1) with D,L-glycerol 3-phosphate as substrate. kcat is 0.18 sec(-1) with D-ribulose 5-phosphate as substrate. kcat is 0.18 sec(-1) with glycerol 2-phosphate as substrate. kcat is 1.00 sec(-1) with p-nitrophenyl 3-phosphate as substrate. kcat is 0.02 sec(-1) with L-glycerol 3-phosphate as substrate.1 Publication
  1. KM=0.89 mM for D,L-glycerol 3-phosphate1 Publication
  2. KM=1.30 mM for D-ribulose 5-phosphate1 Publication
  3. KM=2.01 mM for glycerol 2-phosphate1 Publication
  4. KM=19.30 mM for p-nitrophenyl 3-phosphate1 Publication
  5. KM=1.10 mM for L-glycerol 3-phosphate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Glycerolipid metabolism

    This protein is involved in Glycerolipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in Glycerolipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei14NucleophileBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi14MagnesiumCombined sources1 Publication1
    Active sitei16Proton donorBy similarity1
    Metal bindingi16Magnesium; via carbonyl oxygenCombined sources1 Publication1
    Metal bindingi209MagnesiumCombined sources1 Publication1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • glycerol metabolic process Source: UniProtKB-KW
    • glycerophospholipid catabolic process Source: UniProtKB
    Complete GO annotation on QuickGO ...

    <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 functionHydrolase
    Biological processGlycerol metabolism
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MTBH37RV:G185E-5883-MONOMER

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000001039

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    D,L-glycerol 3-phosphate phosphatase1 Publication (EC:3.1.3.211 Publication)
    Short name:
    G3P phosphatase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    Ordered Locus Names:Rv1692Imported, LH57_09220Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83332 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...    TubercuListi    		Rv1692

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Deletion of this gene results in an accumulation of G3P and G3P-containing lipid polar heads.1 Publication

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004359011 – 353D,L-glycerol 3-phosphate phosphataseAdd BLAST353

    Proteomic databases

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

    More...    PaxDbi    		O33194

    PRoteomics IDEntifications database

    More...    PRIDEi    		O33194

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		83332.Rv1692

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1353
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		O33194

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <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

    <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

    Crystal structures of Rv1692 reveal a unique architecture, a fusion of a predicted haloacid dehalogenase fold with a previously unidentified GCN5-related N-acetyltransferase (GNAT) region. Although not directly involved in acetyl transfer, or regulation of enzymatic activity in vitro, the GNAT region is critical for the solubility of the phosphatase.1 Publication

    <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 HAD-like hydrolase superfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105DSU Bacteria
    COG0647 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_043473_1_0_11

    KEGG Orthology (KO)

    More...    KOi    		K06117

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		PPMHRET

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		O33194

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.1000, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR041065 GNAT-like
    IPR036412 HAD-like_sf
    IPR006357 HAD-SF_hydro_IIA
    IPR023214 HAD_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF18407 GNAT_like, 1 hit
    PF13344 Hydrolase_6, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000915 PGP-type_phosphatase, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF56784 SSF56784, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01460 HAD-SF-IIA, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    O33194-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKSIAQEHDC LLIDLDGTVF CGRQPTGGAV QSLSQVRSRK LFVTNNASRS 
            60         70         80         90        100
    ADEVAAHLCE LGFTATGEDV VTSAQSAAHL LAGQLAPGAR VLIVGTEALA 
           110        120        130        140        150
    NEVAAVGLRP VRRFEDRPDA VVQGLSMTTG WSDLAEAALA IRAGALWVAA 
           160        170        180        190        200
    NVDPTLPTER GLLPGNGSMV AALRTATGMD PRVAGKPAPA LMTEAVARGD 
           210        220        230        240        250
    FRAALVVGDR LDTDIEGANA AGLPSLMVLT GVNSAWDAVY AEPVRRPTYI 
           260        270        280        290        300
    GHDLRSLHQD SKLLAVAPQP GWQIDVGGGA VTVCANGDVD DLEFIDDGLS 
           310        320        330        340        350
    IVRAVASAVW EARAADLHQR PLRIEAGDER ARAALQRWSL MRSDHPVTSV 

    GTQ
    Length:353
    Mass (Da):37,011
    Last modified:January 1, 1998 - v1
    <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:i5DBE79E0040B5849
    GO

    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
    		AL123456 Genomic DNA Translation: CCP44457.1
    CP009480 Genomic DNA Translation: AIR14443.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_216208.1, NC_000962.3
    WP_003408380.1, NZ_NVQJ01000010.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AIR14443; AIR14443; LH57_09220
    CCP44457; CCP44457; Rv1692

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		885241

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mtu:Rv1692
    mtv:RVBD_1692

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|83332.111.peg.1880

    <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
    		AL123456 Genomic DNA Translation: CCP44457.1
    CP009480 Genomic DNA Translation: AIR14443.1
    RefSeqiNP_216208.1, NC_000962.3
    WP_003408380.1, NZ_NVQJ01000010.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4I9GX-ray3.25A/B1-353[»]
    SMRiO33194
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv1692

    Chemistry databases

    SwissLipidsiSLP:000001039

    Proteomic databases

    PaxDbiO33194
    PRIDEiO33194

    Genome annotation databases

    EnsemblBacteriaiAIR14443; AIR14443; LH57_09220
    CCP44457; CCP44457; Rv1692
    GeneIDi885241
    KEGGimtu:Rv1692
    mtv:RVBD_1692
    PATRICifig|83332.111.peg.1880

    Organism-specific databases

    TubercuListiRv1692

    Phylogenomic databases

    eggNOGiENOG4105DSU Bacteria
    COG0647 LUCA
    HOGENOMiCLU_043473_1_0_11
    KOiK06117
    OMAiPPMHRET
    PhylomeDBiO33194

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-5883-MONOMER

    Family and domain databases

    Gene3Di3.40.50.1000, 2 hits
    InterProiView protein in InterPro
    IPR041065 GNAT-like
    IPR036412 HAD-like_sf
    IPR006357 HAD-SF_hydro_IIA
    IPR023214 HAD_sf
    PfamiView protein in Pfam
    PF18407 GNAT_like, 1 hit
    PF13344 Hydrolase_6, 1 hit
    PIRSFiPIRSF000915 PGP-type_phosphatase, 1 hit
    SUPFAMiSSF56784 SSF56784, 1 hit
    TIGRFAMsiTIGR01460 HAD-SF-IIA, 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 nameiG3PP_MYCTU
    <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: O33194
    Secondary accession number(s): F2GK45, I6XYN9, Q7D849
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2016
    Last sequence update: January 1, 1998
    Last modified: February 26, 2020
    This is version 132 of the entry and version 1 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

    3D-structure, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    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