Reviewed, UniProtKB/Swiss-Prot Q9PIH1 (FABH_CAMJE)

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:	Cj0328c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: HAMAP beta-ketoacyl-acyl-carrier-protein synthase III activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
flaG	Q0PAW9	1	EBI-1194759,EBI-1191365

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 324	324	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110409
Regions
	Region	247 – 251	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	246	1	By similarity
	Active site	276	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PIH1-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: B1DE49F008016D9E	FASTA	324	35,165
	10 20 30 40 50 60 MLKASLKSIA SYIPEKILSN ADLEKMVDTT DEWITRRTGI KERRIASENE NTSDLGTKAA 70 80 90 100 110 120 LKAIERANLK PEDIDAILVA TLSPDYFTMP STACKIASNL GLVNISAFDI SAACSGFIYL 130 140 150 160 170 180 LEQAKALVES GLKKNVLIIG AEKTSSIMDY NDRSICILFG DGAGAGVVSL DNENHILDVH 190 200 210 220 230 240 TASNGNYGDL LMTQRSQKSS LCQTLSMQMK GNEVFKIAVN TLSNDVVEIL AKNNILAQEI 250 260 270 280 290 300 DLFIPHQANL RIIKAVQEKL NLSDEKCVIT VQKYGNTSAA SIPMAMNDAY EEGRLKKGNL 310 320 ILLDAFGGGF TWGSALLKFG GENF

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL34479.1.
PIR	D81452.
RefSeq	YP_002343766.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PIH1. 36 interactions.
Genome annotation databases
GeneID	904652.
GenomeReviews	Gene locus Cj0328c in contig AL111168_GR.
KEGG	cje:Cj0328c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PIH1. YSRITGT.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0328C-MON.
BRENDA	2.3.1.180. 255835.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. [Graphical view]
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00747. fabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH_CAMJE

Accession

Primary (citable) accession number: Q9PIH1
Secondary accession number(s): Q0PBI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)