O54151 (FABH3_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 3
EC=2.3.1.180

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

Gene names

Name:	fabH3
Ordered Locus Names:	SCO5888
ORF Names:	SC3F7.08

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
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. HAMAP MF_01815
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity. HAMAP MF_01815
Subcellular location	Cytoplasm Probable HAMAP MF_01815.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815
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 Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro 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 – 335	335	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 3 HAMAP MF_01815		PRO_0000110485
Regions
	Region	257 – 261	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	256	1	By similarity
	Active site	286	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O54151 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 1629F0EE6FBC6860	FASTA	335	34,697
	10 20 30 40 50 60 MTRASVLTGL GSCLPSRCVT NAELERTMDT SDEWIRARTG IAQRYVAEEG TLTSDLAVGA 70 80 90 100 110 120 AERALKSARL TPDEIDAVIV ATTTPDRPCP ATAPTVAARL GTGPVPAFDV SAVCSGFLYG 130 140 150 160 170 180 LATGSGLIAS GAAERVLVIG AETFSRILNP QDRSTSVIFG DGAGAVVLRA GEPGETGALG 190 200 210 220 230 240 PLRLGSDGTG VDLITVPAGG PPRPGAAAPD DLADRYFTME GKRVFWLAVQ RMGECAESVL 250 260 270 280 290 300 DRAGWRVADV DWLVSHQANH RITARLADEI GIPRERSVSN IAEVGNTAAA SIPLALDHAH 310 320 330 ARGTLRPGDR VLLTAFGGGL TWGAAALTWP AVDPV

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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939125 Genomic DNA. Translation: CAA16179.1.
PIR	T34914.
RefSeq	NP_630009.1. NC_003888.3.
3D structure databases
ProteinModelPortal	O54151.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1101330.
GenomeReviews	Gene locus SCO5888 in contig AL645882_GR.
KEGG	sco:SCO5888.
NMPDR	fig|100226.1.peg.5837.
PATRIC	23741680. VBIStrCoe124346_5987.
Phylogenomic databases
HOGENOM	HBG649927.
OMA	HTIFMEG.
PhylomeDB	O54151.
ProtClustDB	PRK09352.
Family and domain databases
HAMAP	MF_01815. FabH. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KO	K00648.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 1 hit.
TIGRFAMs	TIGR00747. FabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH3_STRCO

Accession

Primary (citable) accession number: O54151

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program