A1B364 (FABH_PARDP) 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:	Pden_1861

Organism

Paracoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]

Taxonomic identifier

318586 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	323 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 – 323	323	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000070235
Regions
	Region	251 – 255	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	250	1	By similarity
	Active site	280	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1B364 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: EA39626E1024B673	FASTA	323	34,408
	10 20 30 40 50 60 MRRAIVRGTG HYLPERVVEN SWFEDKLDTS DEWIRARTGI ERRHFAAEDQ RTSDLGILAA 70 80 90 100 110 120 QAALADAGLE AAQIDAVIVA TSTPDLTFPS VATMVQAGLG MRHGFAYDLQ AVCAGFVYAL 130 140 150 160 170 180 ANADALIRAG LADRVLLIGA ETFSRIMDWT DRGTCVLFGD GAGAVVLEAA EGQGSSADRG 190 200 210 220 230 240 ILATDLNSDG QYRDLLYVDG GVASTGTAGH LRMQGNLVFR HAVEKLADTA HRALDRAGLT 250 260 270 280 290 300 PDQVDWLVPH QANLRIIEAT AKRMHLPMEK VVLTVADHGN TSAASIPLAL SVANAEGRFK 310 320 PGDLLVAEAI GGGLAWGSVV LRW

References

[1]

"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222." 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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pd 1222.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000489 Genomic DNA. Translation: ABL69958.1.
RefSeq	YP_915654.1. NC_008686.1.
3D structure databases
ProteinModelPortal	A1B364.
ModBase	Search...
Protein-protein interaction databases
STRING	A1B364.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4579120.
GenomeReviews	Gene locus Pden_1861 in contig CP000489_GR.
KEGG	pde:Pden_1861.
PATRIC	22854827. VBIParDen97112_1796.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	DAYIRGG.
PhylomeDB	A1B364.
ProtClustDB	CLSK933877.
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_PARDP

Accession

Primary (citable) accession number: A1B364

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program