Reviewed, UniProtKB/Swiss-Prot Q5PA98 (FABH_ANAMM)

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:	AM869

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	322 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 – 322	322	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056322
Regions
	Region	250 – 254	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	249	1	By similarity
	Active site	279	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PA98-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: FB8EC850F5AE00E0	FASTA	322	33,876
	10 20 30 40 50 60 MRRSVFCGVG AFLPAKVITN DDLSLMVDTT DEWVFRRTGI KRRHVVEEGD TVSCMATEAA 70 80 90 100 110 120 KIALEDAGVS ATEVDLIIVA TATPDKTMPS CATMVQGSLG CKNAAAFDIN AACSGFLYAL 130 140 150 160 170 180 SIVDSMIKAG QANIALIIGS EAMSKVVDWT DRSTCVLFGD GAGAFVFKGQ DETEKPGAGV 190 200 210 220 230 240 MSTLLCADGS LGNVLYTNGG VASTGKAGYI CMKGTVLFEH AVVKLSSAIS ALLESSALDV 250 260 270 280 290 300 DSIDWFIPHQ ANVRIIDLVI NRLGLSRDKV ILSIDEHANT SSASIPLAMY EAKRAGRIKK 310 320 GNLVLFAAIG AGITWGVSLL RL

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV86782.1.
RefSeq	YP_154037.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PA98.
Genome annotation databases
GeneID	3171592.
GenomeReviews	Gene locus AM869 in contig CP000030_GR.
KEGG	ama:AM869.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PA98.
OMA	ITRGAAF.
Enzyme and pathway databases
BioCyc	AMAR234826:AM869-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_ANAMM

Accession

Primary (citable) accession number: Q5PA98

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 34 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)