Reviewed, UniProtKB/Swiss-Prot Q9Z4Y5 (FABH2_STRCO)

Names and origin

Protein names

Recommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2
    EC=2.3.1.180
Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase III protein 2
    Beta-ketoacyl-ACP synthase III 2
      Short name=KAS III 2

Gene names

Name:	fabH2
Ordered Locus Names:	SCO3246
ORF Names:	SCE29.15c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity.
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
Sequence similarities	Belongs to the fabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: HAMAP beta-ketoacyl-acyl-carrier-protein synthase III 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 – 330	330	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815		PRO_0000110484
Regions
	Region	247 – 251	5	ACP-binding By similarity
Sites
	Active site	118	1	By similarity
	Active site	246	1	By similarity
	Active site	276	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z4Y5-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 18E520075B8CE00A	FASTA	330	33,703
	10 20 30 40 50 60 MSAARGGRAG AVVTGVGTCL PETVVDNDEV SRHLDTDHAW IHSRTGIERR RRVSPGTTTG 70 80 90 100 110 120 DLAVTAGAAA LKSAGRDDCD LVLLATTTPD RRCPATAPRV ASRLGLRAAA AFDLSAVCSG 130 140 150 160 170 180 FVYGLSVASA MITAGTCDRA LVIGADVYSS IVDPDDRGTA VVFGDGAGAV LLERGDTGDP 190 200 210 220 230 240 GAVLHTELGS DGTGDELITI PPDGAYLTMR GSDVYTRAVT TMAESARSTA AHAGWDLADV 250 260 270 280 290 300 DAFVGHQANL RILTSVAKRL RLPPERVVSN IADVANTAAA SIPLALADAA AQGRIGSGDR 310 320 330 LLLTAFGGGL TWGSAAVVWS GAEPVQDQRS

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939115 Genomic DNA. Translation: CAB38890.1.
PIR	T36194.
RefSeq	NP_627458.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBase	Search...
Genome annotation databases
GeneID	1098680.
GenomeReviews	Gene locus SCO3246 in contig AL645882_GR.
KEGG	sco:SCO3246.
NMPDR	fig|100226.1.peg.3206.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9Z4Y5.
OMA	QDRTTAV.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO3246-MON.
BRENDA	2.3.1.180. 1084.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00747. fabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH2_STRCO

Accession

Primary (citable) accession number: Q9Z4Y5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 52 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)