A1STW1 (FABH_PSYIN) 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:	Ping_1087

Organism

Psychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]

Taxonomic identifier

357804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Psychromonadaceae › Psychromonas

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_1000056394
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)
	A1STW1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 871D398C04259058	FASTA	319	33,841
	10 20 30 40 50 60 MNSKIIGTGG YLPVTVRSND DLEKMVDTSD EWITTRTGIK ERRIANQQET IAFMGKEAAL 70 80 90 100 110 120 QALEAANLTA EDLDLIIVGT TSNHNAFPSA ACEIQNLLGI YDIPAFDISA ACAGFTYALS 130 140 150 160 170 180 AADNFIKAGS AKKVLVIGAD TLAATCDSTD RSTIILFGDG AGAVVISATE DEGILSTHIN 190 200 210 220 230 240 ADGRFGELLK LPNPQRGNAQ TVHEAYLSMS GNDVFKVAVK KLSQVVVDTL AANNIEKEQL 250 260 270 280 290 300 DWLVPHQANK RIITATAKKL GMSMDQVILT LENQGNTSAA SVPLALDEGV RSGKIKPGQL 310 ILLEAFGGGF TWGSALVRM

References

[1]

"Complete sequence of Psychromonas ingrahamii 37." 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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000510 Genomic DNA. Translation: ABM02926.1.
RefSeq	YP_942525.1. NC_008709.1.
3D structure databases
ProteinModelPortal	A1STW1.
SMR	A1STW1. Positions 1-318.
ModBase	Search...
Protein-protein interaction databases
STRING	A1STW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4625381.
GenomeReviews	Gene locus Ping_1087 in contig CP000510_GR.
KEGG	pin:Ping_1087.
PATRIC	23067137. VBIPsyIng103130_1190.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	RILNFLA.
PhylomeDB	A1STW1.
Enzyme and pathway databases
BioCyc	PING357804:PING_1087-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_PSYIN

Accession

Primary (citable) accession number: A1STW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program