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Protein

Serine acetyltransferase

Gene

cysE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.1 Publication

Enzyme regulationi

Inhibited by cysteine.1 Publication

Pathway:iL-cysteine biosynthesis

This protein is involved in step 1 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. Probable cysteine synthase (ytkP), Cysteine synthase (cysK)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU00930-MONOMER.
UniPathwayiUPA00136; UER00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine acetyltransferase (EC:2.3.1.30)
Short name:
SAT
Gene namesi
Name:cysE
Synonyms:cysA
Ordered Locus Names:BSU00930
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU00930. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Serine acetyltransferasePRO_0000068665Add
BLAST

Proteomic databases

PaxDbiQ06750.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000485.

Structurei

3D structure databases

ProteinModelPortaliQ06750.
SMRiQ06750. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049432.
InParanoidiQ06750.
KOiK00640.
OMAiINPLAHS.
OrthoDBiEOG6HMXK6.
PhylomeDBiQ06750.

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000441. CysE. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01172. cysE. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFFRMLKEDI DTVFDQDPAA RSYFEVILTY SGLHAIWAHR IAHALYKRKF
60 70 80 90 100
YFLARLISQV SRFFTGIEIH PGATIGRRFF IDHGMGVVIG ETCEIGNNVT
110 120 130 140 150
VFQGVTLGGT GKEKGKRHPT IKDDALIATG AKVLGSITVG EGSKIGAGSV
160 170 180 190 200
VLHDVPDFST VVGIPGRVVV QNGKKVRRDL NHQDLPDPVA DRFKSLEQQI
210
LELKAELEDR KERINQK
Length:217
Mass (Da):24,143
Last modified:June 1, 1994 - v1
Checksum:i14EFA32FA1086D9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14580 Genomic DNA. Translation: AAA21797.1.
D26185 Genomic DNA. Translation: BAA05327.1.
AL009126 Genomic DNA. Translation: CAB11869.1.
PIRiB53402.
RefSeqiNP_387974.1. NC_000964.3.
WP_003225749.1. NZ_JNCM01000029.1.

Genome annotation databases

EnsemblBacteriaiCAB11869; CAB11869; BSU00930.
GeneIDi936831.
KEGGibsu:BSU00930.
PATRICi18971695. VBIBacSub10457_0096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14580 Genomic DNA. Translation: AAA21797.1.
D26185 Genomic DNA. Translation: BAA05327.1.
AL009126 Genomic DNA. Translation: CAB11869.1.
PIRiB53402.
RefSeqiNP_387974.1. NC_000964.3.
WP_003225749.1. NZ_JNCM01000029.1.

3D structure databases

ProteinModelPortaliQ06750.
SMRiQ06750. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000485.

Proteomic databases

PaxDbiQ06750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11869; CAB11869; BSU00930.
GeneIDi936831.
KEGGibsu:BSU00930.
PATRICi18971695. VBIBacSub10457_0096.

Organism-specific databases

GenoListiBSU00930. [Micado]

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049432.
InParanoidiQ06750.
KOiK00640.
OMAiINPLAHS.
OrthoDBiEOG6HMXK6.
PhylomeDBiQ06750.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00199.
BioCyciBSUB:BSU00930-MONOMER.

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000441. CysE. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01172. cysE. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCYSE_BACSU
AccessioniPrimary (citable) accession number: Q06750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 22, 2015
This is version 101 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.