Reviewed, UniProtKB/Swiss-Prot Q820T1 (FABH_ENTFA)

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:	EF_2885

Organism

Enterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	321 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	3D-structure 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 321	321	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110427
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)
	Q820T1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 1306C774594D6D9D	FASTA	321	35,182
	10 20 30 40 50 60 MKNYARISCT SRYVPENCVT NHQLSEMMDT SDEWIHSRTG ISERRIVTQE NTSDLCHQVA 70 80 90 100 110 120 KQLLEKSGKQ ASEIDFILVA TVTPDFNMPS VACQVQGAIG ATEAFAFDIS AACSGFVYAL 130 140 150 160 170 180 SMAEKLVLSG RYQTGLVIGG ETFSKMLDWT DRSTAVLFGD GAAGVLIEAA ETPHFLNEKL 190 200 210 220 230 240 QADGQRWAAL TSGYTINESP FYQGHKQASK TLQMEGRSIF DFAIKDVSQN ILSLVTDETV 250 260 270 280 290 300 DYLLLHQANV RIIDKIARKT KISREKFLTN MDKYGNTSAA SIPILLDEAV ENGTLILGSQ 310 320 QRVVLTGFGG GLTWGSLLLT L

References

[1]

"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: V583 / ATCC 700802.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE016830 Genomic DNA. Translation: AAO82575.1.

RefSeq

NP_816505.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IL4	X-ray	3.00	A/B/C/D	2-321	[»]
3IL5	X-ray	2.60	A/B/C/D	1-321	[»]
3IL6	X-ray	2.50	A	1-321	[»]

ModBase

Search...

Genome annotation databases

GeneID

1201733.

GenomeReviews

Gene locus EF_2885 in contig AE016830_GR.

KEGG

efa:EF2885.

NMPDR

fig|226185.1.peg.2690.

TIGR

EF_2885.

Phylogenomic databases

HOGENOM

Q820T1.

OMA

GHRIASS.

Enzyme and pathway databases

BioCyc

EFAE226185:EF_2885-MON.

BRENDA

2.3.1.180. 704.

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...

Other Resources

BindingDB

Q820T1.

Entry information

Entry name

FABH_ENTFA

Accession

Primary (citable) accession number: Q820T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 47 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)