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Protein

O-acetylserine sulfhydrylase

Gene

cysK1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -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

GO - Biological processi

  • cysteine biosynthetic process from serine Source: MTBBASE

Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Cysteine biosynthesis
LigandPyridoxal 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

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
Helixi46 – 57Combined sources12
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
OMAiWDSGERY
PhylomeDBiP9WP55

Family and domain databases

InterProiView protein in InterPro
IPR005856 Cys_synth
IPR005859 CysK
IPR001216 P-phosphate_BS
IPR001926 PLP-dep
IPR036052 Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291 PALP, 1 hit
SUPFAMiSSF53686 SSF53686, 1 hit
TIGRFAMsiTIGR01139 cysK, 1 hit
TIGR01136 cysKM, 1 hit
PROSITEiView protein in PROSITE
PS00901 CYS_SYNTHASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCYSK_MYCTU
AccessioniPrimary (citable) accession number: P9WP55
Secondary accession number(s): L0TC08, P0A534, P95230
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: March 28, 2018
This is version 28 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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