Q9ZFE4 (FABI_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Short name=ENR
EC=1.3.1.9

Alternative name(s):
NADH-dependent enoyl-ACP reductase

Gene names

Name:	fabI
Ordered Locus Names:	PA1806

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 265	265	Enoyl-[acyl-carrier-protein] reductase [NADH] FabI		PRO_0000054904
Regions
	Nucleotide binding	19 – 20	2	NAD By similarity
	Nucleotide binding	66 – 67	2	NAD By similarity
	Nucleotide binding	195 – 199	5	NAD By similarity
Sites
	Active site	149	1	Proton acceptor By similarity
	Active site	159	1	Proton acceptor By similarity
	Binding site	13	1	NAD; via carbonyl oxygen By similarity
	Binding site	40	1	NAD By similarity
	Binding site	94	1	NAD; via carbonyl oxygen By similarity
	Binding site	97	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	166	1	NAD By similarity
	Site	204	1	Involved in acyl-ACP binding By similarity
	Site	207	1	Involved in acyl-ACP binding By similarity
	Site	208	1	Involved in acyl-ACP binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZFE4 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 3E7A946886DFB293	FASTA	265	28,006
	10 20 30 40 50 60 MGFLTGKRAL IVGVASKLSI ASGIAAAMHR EGAELAFTYQ NDKLRGRVEE FASGWGSRPE 70 80 90 100 110 120 LCFPCDVADD SQIEAVFAAL GKHWDGLDII VHSVGFAPGD QLDGDFTAVT TREGFRIAHD 130 140 150 160 170 180 ISAYSFIALA KAGREMMKGR NGSLLTLSYL GAERTMPNYN VMGMAKASLE AGVRYLAGSL 190 200 210 220 230 240 GAEGTRVNAV SAGPIRTLAA SGIKSFRKML AANERQTPLR RNVTIEEVGN AGAFLCSDLA 250 260 SGISGEILYV DGGFNTTAMG PLDDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis." Hoang T.T., Schweizer H.P. J. Bacteriol. 181:5489-5497(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF104262 Genomic DNA. Translation: AAC95362.1. AE004091 Genomic DNA. Translation: AAG05195.1.
PIR	C83419.
RefSeq	NP_250497.1. NC_002516.2.
3D structure databases
ProteinModelPortal	Q9ZFE4.
SMR	Q9ZFE4. Positions 2-259.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA1806.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	878311.
KEGG	pae:PA1806.
PATRIC	19837991. VBIPseAer58763_1876.
Organism-specific databases
PseudoCAP	PA1806.
Phylogenomic databases
eggNOG	COG0623.
KO	K00208.
OMA	WGKLDFI.
ProtClustDB	CLSK866795.
Enzyme and pathway databases
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PIRSF	PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTS	PR00081. GDHRDH.
ProtoNet	Search...

Entry information

Entry name

FABI_PSEAE

Accession

Primary (citable) accession number: Q9ZFE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program