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Q06750

- CYSE_BACSU

UniProt

Q06750 - CYSE_BACSU

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Protein

Serine acetyltransferase

Gene

cysE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Pathwayi

GO - Molecular functioni

  1. serine O-acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cysteine biosynthetic process from serine Source: InterPro
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: Chromosome

Organism-specific databases

GenoListiBSU00930. [Micado]

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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.BSU00930.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1045.
HOGENOMiHOG000049432.
InParanoidiQ06750.
KOiK00640.
OMAiDNVTVYQ.
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.

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 .
PIRi B53402.
RefSeqi NP_387974.1. NC_000964.3.

3D structure databases

ProteinModelPortali Q06750.
SMRi Q06750. Positions 2-215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU00930.

Proteomic databases

PaxDbi Q06750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB11869 ; CAB11869 ; BSU00930 .
GeneIDi 936831.
KEGGi bsu:BSU00930.
PATRICi 18971695. VBIBacSub10457_0096.

Organism-specific databases

GenoListi BSU00930. [Micado ]

Phylogenomic databases

eggNOGi COG1045.
HOGENOMi HOG000049432.
InParanoidi Q06750.
KOi K00640.
OMAi DNVTVYQ.
OrthoDBi EOG6HMXK6.
PhylomeDBi Q06750.

Enzyme and pathway databases

UniPathwayi UPA00136 ; UER00199 .
BioCyci BSUB:BSU00930-MONOMER.

Family and domain databases

InterProi IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000441. CysE. 1 hit.
SUPFAMi SSF51161. SSF51161. 1 hit.
TIGRFAMsi TIGR01172. cysE. 1 hit.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 97 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