Reviewed, UniProtKB/Swiss-Prot Q06750 (CYSE_BACSU)

Names and origin

Protein names

Recommended name:
    Serine acetyltransferase
      Short name=SAT
    EC=2.3.1.30

Gene names

Name:	cysE
Synonyms:	cysA
Ordered Locus Names:	BSU00930

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	Serine acetyltransferase		PRO_0000068665

Sequences

	Sequence		Length	Mass (Da)
	Q06750-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 14EFA32FA1086D9D	FASTA	217	24,143
	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

References

	« Hide 'large scale' referencesShow '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: 7510287] [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: 7584024] [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: 9384377] [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: 18974048] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L14580 Genomic DNA. Translation: AAA21797.1. D26185 Genomic DNA. Translation: BAA05327.1. AL009126 Genomic DNA. Translation: CAB11869.1.
PIR	B53402.
RefSeq	NP_387974.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	936831.
GenomeReviews	Gene locus BSU00930 in contig AL009126_GR.
KEGG	bsu:BSU00930.
NMPDR	fig|224308.1.peg.93.
Organism-specific databases
SubtiList	BG10155. cysE. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q06750.
OMA	RHPTIKD.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0093-MON.
BRENDA	2.3.1.30. 150.
Family and domain databases
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR005881. Ser_O-AcTrfase. [Graphical view]
Pfam	PF00132. Hexapep. 4 hits. [Graphical view]
TIGRFAMs	TIGR01172. cysE. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSE_BACSU

Accession

Primary (citable) accession number: Q06750

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)