A0A4P6UWI0 · A0A4P6UWI0_9HYPH

  • Protein
    O-succinylhomoserine sulfhydrylase
  • Gene
    metZ
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the formation of L-homocysteine from O-succinyl-L-homoserine (OSHS) and hydrogen sulfide.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-succinyl-L-homoserine: step 1/1.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functioncarbon-sulfur lyase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process'de novo' L-methionine biosynthetic process
Biological Processhomocysteine biosynthetic process
Biological Processtranssulfuration

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    O-succinylhomoserine sulfhydrylase
  • EC number
  • Short names
    OSH sulfhydrylase
    ; OSHS sulfhydrylase

Gene names

    • Name
      metZ
    • ORF names
      E0E05_01925

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MA7-20
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Ahrensiaceae > Roseitalea

Accessions

  • Primary accession
    A0A4P6UWI0

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue210N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homotetramer.

Family & Domains

Sequence similarities

Belongs to the trans-sulfuration enzymes family. MetZ subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    42,520
  • Last updated
    2019-07-31 v1
  • Checksum
    B1253A30C7049048
MGDGRDGWGPSTAMVHAGTMRSGFGETSEALFLTQGFVYESAEAAEARFKGDEPGFVYSRYANPTVEMFERRMCALEGAEAARATASGMAAVASALMCQLSAGDHVVAARALFGSCRWIVEKLLPRYGVATTLVDGTDPAAWERAVRPNTKLFFFESPTNPTLEVIDIAHVVSVARSCGARTVIDNVFATPLHQKPIELGVDIVVYSTTKHIDGQGRCLGGVVLGRQDWIDEHLHDFFRHTGPSMSPFNAWVMLKGLETLPLRVARQAGSARAVADFLADHGGVSRVVYPGRPDHPQANIIPRQMSGGSTLVAFDVAGGKKAAFAFENALEIIGISNNLGDAKSLITHPATTTHKNLSDEDRAELSIGGGTLRLSVGLEDTEDLIADLDRALAVGGRP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036532
EMBL· GenBank· DDBJ
QBK29461.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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.
FeedbackHelp