Reviewed, UniProtKB/Swiss-Prot P45855 (THL_BACSU)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase

Gene names

Name:	mmgA
Synonyms:	yqiL
Ordered Locus Names:	BSU24170

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Subcellular location	Cytoplasm.
Developmental stage	Expressed in the mother cell at intermediate stages of sporulation under the control of the sigma-E factor. Ref.1
Induction	Subject to catabolite repression. Ref.1
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Sporulation
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-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 – 393	393	Acetyl-CoA acetyltransferase		PRO_0000206402
Sites
	Active site	88	1	Acyl-thioester intermediate By similarity
	Active site	349	1	Proton acceptor By similarity
	Active site	379	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	68	1	Q → L in AAB09613. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P45855-1 [UniParc]. Last modified August 4, 2003. Version 2. Checksum: E2D52259679E50F7	FASTA	393	41,179
	10 20 30 40 50 60 MRKTVIVSAA RTPFGKFGGV LKEVKAAELG GIVMKEALQQ AGVSGDDVEG NVMGMVVQAG 70 80 90 100 110 120 SGQIPSRQAA RLAGMPWSVP SETLNKVCAS GLRAVTLCDQ MIRAQDADIL VAGGMESMSN 130 140 150 160 170 180 IPYAVPAGRW GARMGDGELR DLMVYDGLTC AFDEVHMAVH GNTAAKEYAI SRREQDEWAL 190 200 210 220 230 240 RSHARAAKAA DEGKFQDEIV PVNWIGRKGK PNVVDKDEAI RRDTSLDQLA KLAPIYASDG 250 260 270 280 290 300 SITAGNAPGV NDGAGAFVLM SEEKAAELGK RPLATILGFS TTGMPAHELA AAPGFAINKL 310 320 330 340 350 360 LKKNGLTVQD IDLFEVNEAF ASVVLTCEKI VGFDLEKVNV NGGAIALGHP IGASGARILM 370 380 390 TLVYELKRRG GGLGVAAICS GAAQGDAVLV QVH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A sigma E dependent operon subject to catabolite repression during sporulation in Bacillus subtilis." Bryan E.M., Beall B.W., Moran C.P. Jr. J. Bacteriol. 178:4778-4786(1996) [PubMed: 8759838] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, INDUCTION. Strain: 168 / MB24.
[2]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U29084 Genomic DNA. Translation: AAB09613.1. D84432 Genomic DNA. Translation: BAA12587.1. AL009126 Genomic DNA. Translation: CAB14348.1.
PIR	B69658.
RefSeq	NP_390297.1.
3D structure databases
SMR	P45855. Positions 4-391.
ModBase	Search...
Genome annotation databases
GeneID	938662.
GenomeReviews	Gene locus BSU24170 in contig AL009126_GR.
KEGG	bsu:BSU24170.
NMPDR	fig|224308.1.peg.2421.
Organism-specific databases
SubtiList	BG11319. mmgA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	APEQVEY.
PhylomeDB	P45855.
Enzyme and pathway databases
BRENDA	2.3.1.9. 150.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THL_BACSU

Accession

Primary (citable) accession number: P45855

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	August 4, 2003
Last modified:	February 9, 2010
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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