A4G6T2 (FABH_HERAR) 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:	HEAR2077

Organism

Herminiimonas arsenicoxydans [Complete proteome] [HAMAP]

Taxonomic identifier

204773 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Oxalobacteraceae › Herminiimonas

Protein attributes

Sequence length	328 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 – 328	328	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000070232
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	122	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4G6T2 [UniParc]. Last modified April 17, 2007. Version 1. Checksum: 2282F7F29E006EE1	FASTA	328	34,698
	10 20 30 40 50 60 MTLYSKIIGT GSYLPPNRVT NQDLIERLAL DGIETSDEWI VSRSGISARH YADADMQSSD 70 80 90 100 110 120 LAVEAAKRAL DMAKLAANDI DLIILATSTP DFFGGFPSTA CVVQRKLGVT NGCAAVDVQA 130 140 150 160 170 180 VCSGFVYALA TADKFIKSGS HKNVLVIGAE VFSRIIDFKD RTTCVLFGDG SGAVVMTASE 190 200 210 220 230 240 EPGVLATKLH ADGSYGDILC GPGRISNGVL EGSAFMYMDG QAVFKLAIGL LDKVANEVLQ 250 260 270 280 290 300 LAKMDASEVD WIVPHQANIR IMQGTAKKLG LSMDKMIVTV DQHGNTSAAS IPMALDVGVR 310 320 DGRIKPGQNV MMEGVGGGFT WGAVLARM

References

[1]

"A tale of two oxidation states: bacterial colonization of arsenic-rich environments." Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E., Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M., Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E., Lieutaud A. , Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J., Lett M.-C., Danchin A., Bertin P.N. PLoS Genet. 3:518-530(2007) [PubMed: 17432936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ULPAs1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU207211 Genomic DNA. Translation: CAL62219.1.
RefSeq	YP_001100342.1. NC_009138.1.
3D structure databases
ProteinModelPortal	A4G6T2.
SMR	A4G6T2. Positions 3-327.
ModBase	Search...
Protein-protein interaction databases
STRING	A4G6T2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4930873.
GenomeReviews	Gene locus HEAR2077 in contig CU207211_GR.
KEGG	har:HEAR2077.
NMPDR	fig|204773.3.peg.1973.
PATRIC	22114200. VBIHerArs17568_1965.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	VIGSEVY.
PhylomeDB	A4G6T2.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	HARS204773:HEAR2077-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_HERAR

Accession

Primary (citable) accession number: A4G6T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 17, 2007
Last modified:	December 14, 2011
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