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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)DescriptionActionsGraphical viewLength
Binding sitei74Pyridoxal phosphate1 Publication1
Binding sitei266Pyridoxal phosphate1 Publication1

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

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6559-MONOMER.
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 databases

ChEMBLiCHEMBL2321612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001670941 – 310O-acetylserine sulfhydrylaseAdd BLAST310

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

PaxDbiP9WP55.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2334.

Chemistry databases

BindingDBiP9WP55.

Structurei

Secondary structure

1310
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 10Combined sources4
Beta strandi16 – 18Combined sources3
Beta strandi20 – 22Combined sources3
Beta strandi28 – 34Combined sources7
Helixi35 – 37Combined sources3
Helixi44 – 57Combined sources14
Beta strandi66 – 70Combined sources5
Helixi74 – 86Combined sources13
Beta strandi89 – 95Combined sources7
Helixi100 – 108Combined sources9
Beta strandi112 – 116Combined sources5
Helixi118 – 120Combined sources3
Helixi121 – 135Combined sources15
Turni144 – 146Combined sources3
Helixi149 – 156Combined sources8
Helixi158 – 165Combined sources8
Turni166 – 168Combined sources3
Beta strandi172 – 176Combined sources5
Beta strandi178 – 180Combined sources3
Helixi181 – 193Combined sources13
Beta strandi198 – 204Combined sources7
Turni209 – 212Combined sources4
Helixi234 – 236Combined sources3
Beta strandi239 – 243Combined sources5
Helixi245 – 259Combined sources15
Helixi265 – 278Combined sources14
Helixi281 – 283Combined sources3
Beta strandi287 – 292Combined sources6
Beta strandi294 – 296Combined sources3
Helixi297 – 299Combined sources3

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni178 – 182Pyridoxal phosphate binding1 Publication5

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q3BX-ray1.80A1-310[»]
2Q3CX-ray2.10A1-310[»]
2Q3DX-ray2.20A1-310[»]
3ZEIX-ray2.00A1-310[»]
ProteinModelPortaliP9WP55.
SMRiP9WP55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2334.

Chemistry databases

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.
BioCyciMTBH37RV:G185E-6559-MONOMER.
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...

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: November 2, 2016
This is version 23 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.