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Q06750 (CYSE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine acetyltransferase

Short name=SAT
EC=2.3.1.30
Gene names
Name:cysE
Synonyms:cysA
Ordered Locus Names:BSU00930
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS).

Catalytic activity

Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine. Ref.4

Enzyme regulation

Inhibited by cysteine. Ref.4

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the transferase hexapeptide repeat family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcysteine biosynthetic process from serine

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine O-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Serine acetyltransferase
PRO_0000068665

Sequences

Sequence LengthMass (Da)Tools
Q06750 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 14EFA32FA1086D9D

FASTA21724,143
        10         20         30         40         50         60 
MFFRMLKEDI DTVFDQDPAA RSYFEVILTY SGLHAIWAHR IAHALYKRKF YFLARLISQV 

        70         80         90        100        110        120 
SRFFTGIEIH PGATIGRRFF IDHGMGVVIG ETCEIGNNVT VFQGVTLGGT GKEKGKRHPT 

       130        140        150        160        170        180 
IKDDALIATG AKVLGSITVG EGSKIGAGSV VLHDVPDFST VVGIPGRVVV QNGKKVRRDL 

       190        200        210 
NHQDLPDPVA DRFKSLEQQI LELKAELEDR KERINQK 

« Hide

References

« Hide 'large scale' references
[1]"Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis."
Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M., Lapointe J.
J. Biol. Chem. 269:7473-7482(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis."
Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P., Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I.
J. Biol. Chem. 283:35551-35560(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14580 Genomic DNA. Translation: AAA21797.1.
D26185 Genomic DNA. Translation: BAA05327.1.
AL009126 Genomic DNA. Translation: CAB11869.1.
PIRB53402.
RefSeqNP_387974.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ06750.
SMRQ06750. Positions 2-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU00930.

Proteomic databases

PaxDbQ06750.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11869; CAB11869; BSU00930.
GeneID936831.
KEGGbsu:BSU00930.
PATRIC18971695. VBIBacSub10457_0096.

Organism-specific databases

GenoListBSU00930. [Micado]

Phylogenomic databases

eggNOGCOG1045.
HOGENOMHOG000049432.
KOK00640.
OMAKAISCLF.
OrthoDBEOG6HMXK6.
ProtClustDBCLSK872621.

Enzyme and pathway databases

BioCycBSUB:BSU00930-MONOMER.
UniPathwayUPA00136; UER00199.

Family and domain databases

InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000441. CysE. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01172. cysE. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSE_BACSU
AccessionPrimary (citable) accession number: Q06750
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 13, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList