Q15TZ6 (FABH_PSEA6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.41

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:	Patl_2124

Organism

Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP]

Taxonomic identifier

342610 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	319 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	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056392
Regions
	Region	247 – 251	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	246	1	By similarity
	Active site	276	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q15TZ6 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: C9215B490FAF408E	FASTA	319	34,309
	10 20 30 40 50 60 MNSRIIGTGS YYPSDVRTNA DLSLMVDTSD EWITDRTGIK ERRIIGEHET AATMGFEASK 70 80 90 100 110 120 KALEAAGIDA KSLDMIVCAT TSGRYSLPST ACEIQKALDV DGIPAFDVAA ACAGYCYALS 130 140 150 160 170 180 VADQYIKSGM AKRILVVGTD CLSRMISPED RTMVILFGDA AGATIIEASE EPGILSTHIH 190 200 210 220 230 240 AAGSYGDLLA IGNPTRGDES SIHENWGSMK GNEVFRVAVT KLSEIVEETL AANNMQKSDL 250 260 270 280 290 300 DWLVPHQANF RIIKATAKKL DMSLDQVVIT LERYGNTSAA TVPTALDEAI RDGRIKRGQN 310 LLLEAFGGGF AWASALVRY

References

[1]

"Complete sequence of Pseudoalteromonas atlantica T6c." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000388 Genomic DNA. Translation: ABG40642.1.
RefSeq	YP_661696.1. NC_008228.1.
3D structure databases
ProteinModelPortal	Q15TZ6.
SMR	Q15TZ6. Positions 1-319.
ModBase	Search...
Protein-protein interaction databases
STRING	Q15TZ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4173379.
GenomeReviews	Gene locus Patl_2124 in contig CP000388_GR.
KEGG	pat:Patl_2124.
NMPDR	fig|342610.3.peg.3320.
PATRIC	23049370. VBIPseAtl25434_2273.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	RILNFLA.
PhylomeDB	Q15TZ6.
Enzyme and pathway databases
BioCyc	PATL342610:PATL_2124-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_PSEA6

Accession

Primary (citable) accession number: Q15TZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 25, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program