Reviewed, UniProtKB/Swiss-Prot Q5HAV9 (FABH_EHRRW)

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:	Erum5720, ERWE_CDS_06010

Organism

Ehrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]

Taxonomic identifier

254945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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
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_1000056360
Regions
	Region	247 – 251	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	246	1	By similarity
	Active site	276	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HAV9-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 19E1CE594DE5BD0E	FASTA	319	34,267
	10 20 30 40 50 60 MRSSRILGIG SYLPKSLVTN DDLACTVATS DEWIVKRTGI RQRYIAADDQ MTSDMAVEAA 70 80 90 100 110 120 KLALNDSGIN KQDVDLIVVA TTTPDRTFPS CATIVQSKLE CKNAFAFDIQ AVCSGFIYAM 130 140 150 160 170 180 AIADNFIKSG QVNVSLVIGA EVMSRILDWK DRSTCVLFGD GAGAVVLSNN SARNTGVIST 190 200 210 220 230 240 ILYSDGTLHN LLYTSGGTAY NGVAGTICMN GTVVFEHAIE KLSASIVEIL NKNNLSIDEV 250 260 270 280 290 300 NWFVLHQANI RIIELVARRL KIPSEKMVIS INQHANTSAA SIPLALSYAK NSGKLKQDDL 310 VVLAAIGAGI TWGVCLVRM

References

[1]

"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number." Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A. Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed: 15637156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity." Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D. J. Bacteriol. 188:2533-2542(2006) [PubMed: 16547041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR767821 Genomic DNA. Translation: CAH58302.1. CR925678 Genomic DNA. Translation: CAI27095.1.
RefSeq	YP_180435.1. YP_197477.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HAV9.
Genome annotation databases
GeneID	3233317. 3261079.
GenomeReviews	Gene locus Erum5720 in contig CR767821_GR. Gene locus ERWE_CDS_06010 in contig CR925678_GR.
KEGG	eru:Erum5720. erw:ERWE_CDS_06010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5HAV9.
OMA	FKSAVTS.
Enzyme and pathway databases
BioCyc	ERUM254945:ERWE_CDS_06010-MON.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
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_EHRRW

Accession

Primary (citable) accession number: Q5HAV9
Secondary accession number(s): Q5FD52

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 15, 2005
Last modified:	November 3, 2009
This is version 38 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)