A9NFF0 (FABH_ACHLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	fabH
Ordered Locus Names:	ACL_0461

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	310 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
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 – 310	310	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000088304
Regions
	Region	240 – 244	5	ACP-binding By similarity
Sites
	Active site	116	1	By similarity
	Active site	239	1	By similarity
	Active site	269	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NFF0 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: ABDA336628042842	FASTA	310	34,122
	10 20 30 40 50 60 MKNLPIKIVS TGRYAPDNIM TNDDFSKILD TNDEWITTRT GIKRRHIAQG ETAIDMAYKA 70 80 90 100 110 120 ALKAVENKNY DKEKIDLIIV ASITSPVKTP SIANLIQAKL GLNHKNIVAF DINAACSGFV 130 140 150 160 170 180 YAVEIAASMI SSGNYKSALV IGSEHMSSIL DWEDRSTAIL FGDAAGAAII EVSDNPKDNA 190 200 210 220 230 240 YFWNGSRGDD TGILWIDPKV KMAGREVYKF AVDIMPKAIH KVLEKAGLTI DDIDYIIPHQ 250 260 270 280 290 300 ANYRIIQSVA KDMNLPIERF LMNLEEYGNT SAASIPFLLD EHKTNNPEVK RVILVGFGGG 310 FTWGAAILNV

References

[1]

"Complete genome and proteome of Acholeplasma laidlawii." Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I. , Alexeev D.G., Ladygina V.G., Govorun V.M. J. Bacteriol. 193:4943-4953(2011) [PubMed: 21784942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PG-8A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000896 Genomic DNA. Translation: ABX81080.1.
RefSeq	YP_001620456.1. NC_010163.1.
3D structure databases
ProteinModelPortal	A9NFF0.
ModBase	Search...
Protein-protein interaction databases
STRING	A9NFF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5803120.
GenomeReviews	Gene locus ACL_0461 in contig CP000896_GR.
KEGG	acl:ACL_0461.
PATRIC	20637642. VBIAchLai134690_0442.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	VPNEVIL.
Enzyme and pathway databases
BioCyc	ALAI441768:ACL_0461-MONOMER.
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

FABH_ACHLI

Accession

Primary (citable) accession number: A9NFF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program