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Protein

O-acetylserine sulfhydrylase

Gene

cysK1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide.1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Competitively inhibited by a four-residue peptide derived from the C-terminus of serine acetyltransferase (CysE). This suggests that CysK1 may associate with CysE in vivo to form a bi-enzyme complex, in which the OASS activity is down-regulated.1 Publication

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Serine acetyltransferase (cysE)
  2. O-acetylserine sulfhydrylase (cysK1)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741Pyridoxal phosphate1 Publication
Binding sitei266 – 2661Pyridoxal phosphate1 Publication

GO - Molecular functioni

  • cysteine synthase activity Source: MTBBASE
  • L-cysteine desulfhydrase activity Source: GO_Central
  • pyridoxal phosphate binding Source: MTBBASE
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • cysteine biosynthetic process from serine Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MTU-936721. Cysteine synthesis from O-acetylserine.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
O-acetylserine sulfhydrylase1 Publication (EC:2.5.1.471 Publication)
Short name:
OAS sulfhydrylase1 Publication
Short name:
OASS1 Publication
Alternative name(s):
Cysteine synthase A
Short name:
CSase A
O-acetylserine (thiol)-lyase A
Short name:
OAS-TL A
O-acetylserine-specific cysteine synthase
Sulfide-dependent cysteine synthase
Gene namesi
Name:cysK1
Synonyms:cysK
Ordered Locus Names:Rv2334
ORF Names:MTCY98.03
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2334.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular region Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2321612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310O-acetylserine sulfhydrylasePRO_0000167094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-(pyridoxal phosphate)lysine1 Publication

Proteomic databases

PaxDbiP9WP55.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2334.

Chemistry

BindingDBiP9WP55.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Beta strandi16 – 183Combined sources
Beta strandi20 – 223Combined sources
Beta strandi28 – 347Combined sources
Helixi35 – 373Combined sources
Helixi44 – 5714Combined sources
Beta strandi66 – 705Combined sources
Helixi74 – 8613Combined sources
Beta strandi89 – 957Combined sources
Helixi100 – 1089Combined sources
Beta strandi112 – 1165Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 13515Combined sources
Turni144 – 1463Combined sources
Helixi149 – 1568Combined sources
Helixi158 – 1658Combined sources
Turni166 – 1683Combined sources
Beta strandi172 – 1765Combined sources
Beta strandi178 – 1803Combined sources
Helixi181 – 19313Combined sources
Beta strandi198 – 2047Combined sources
Turni209 – 2124Combined sources
Helixi234 – 2363Combined sources
Beta strandi239 – 2435Combined sources
Helixi245 – 25915Combined sources
Helixi265 – 27814Combined sources
Helixi281 – 2833Combined sources
Beta strandi287 – 2926Combined sources
Beta strandi294 – 2963Combined sources
Helixi297 – 2993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3BX-ray1.80A1-310[»]
2Q3CX-ray2.10A1-310[»]
2Q3DX-ray2.20A1-310[»]
3ZEIX-ray2.00A1-310[»]
ProteinModelPortaliP9WP55.
SMRiP9WP55. Positions 1-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1825Pyridoxal phosphate binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
KOiK01738.
OMAiVKCRIGS.
PhylomeDBiP9WP55.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WP55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIAEDITQL IGRTPLVRLR RVTDGAVADI VAKLEFFNPA NSVKDRIGVA
60 70 80 90 100
MLQAAEQAGL IKPDTIILEP TSGNTGIALA MVCAARGYRC VLTMPETMSL
110 120 130 140 150
ERRMLLRAYG AELILTPGAD GMSGAIAKAE ELAKTDQRYF VPQQFENPAN
160 170 180 190 200
PAIHRVTTAE EVWRDTDGKV DIVVAGVGTG GTITGVAQVI KERKPSARFV
210 220 230 240 250
AVEPAASPVL SGGQKGPHPI QGIGAGFVPP VLDQDLVDEI ITVGNEDALN
260 270 280 290 300
VARRLAREEG LLVGISSGAA TVAALQVARR PENAGKLIVV VLPDFGERYL
310
STPLFADVAD
Length:310
Mass (Da):32,753
Last modified:April 16, 2014 - v1
Checksum:i597B1106CA6D0B9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45122.1.
PIRiG70660.
RefSeqiWP_003899275.1. NZ_KK339370.1.
YP_177868.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP45122; CCP45122; Rv2334.
GeneIDi886016.
KEGGimtu:Rv2334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45122.1.
PIRiG70660.
RefSeqiWP_003899275.1. NZ_KK339370.1.
YP_177868.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3BX-ray1.80A1-310[»]
2Q3CX-ray2.10A1-310[»]
2Q3DX-ray2.20A1-310[»]
3ZEIX-ray2.00A1-310[»]
ProteinModelPortaliP9WP55.
SMRiP9WP55. Positions 1-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2334.

Chemistry

BindingDBiP9WP55.
ChEMBLiCHEMBL2321612.

Proteomic databases

PaxDbiP9WP55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45122; CCP45122; Rv2334.
GeneIDi886016.
KEGGimtu:Rv2334.

Organism-specific databases

TubercuListiRv2334.

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
KOiK01738.
OMAiVKCRIGS.
PhylomeDBiP9WP55.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
ReactomeiR-MTU-936721. Cysteine synthesis from O-acetylserine.

Miscellaneous databases

PROiP9WP55.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex."
    Schnell R., Oehlmann W., Singh M., Schneider G.
    J. Biol. Chem. 282:23473-23481(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH THE REACTION INTERMEDIATE ALPHA-AMINOACRYLATE OR PEPTIDE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, REACTION MECHANISM.
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiCYSK_MYCTU
AccessioniPrimary (citable) accession number: P9WP55
Secondary accession number(s): L0TC08, P0A534, P95230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.