P44432 (FABI_HAEIN) 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
Synonyms:	envM
Ordered Locus Names:	HI_1734

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Enzyme regulation	Inhibited by 1,4-benzodiazepine and naphthyridinone derivatives. Ref.2 Ref.3
Pathway	Lipid metabolism; fatty acid biosynthesis.
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 262	261	Enoyl-[acyl-carrier-protein] reductase [NADH] FabI		PRO_0000054901
Regions
	Nucleotide binding	19 – 20	2	NAD By similarity
	Nucleotide binding	64 – 65	2	NAD By similarity
	Nucleotide binding	192 – 196	5	NAD By similarity
Sites
	Active site	146	1	Proton acceptor By similarity
	Active site	156	1	Proton acceptor By similarity
	Binding site	13	1	NAD; via carbonyl oxygen By similarity
	Binding site	92	1	NAD; via carbonyl oxygen By similarity
	Binding site	95	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	163	1	NAD By similarity
	Site	201	1	Involved in acyl-ACP binding By similarity
	Site	204	1	Involved in acyl-ACP binding By similarity
	Site	205	1	Involved in acyl-ACP binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44432 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 71CEF6189795388E	FASTA	262	28,119
	10 20 30 40 50 60 MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE FAKEFGSDIV 70 80 90 100 110 120 LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL DGDYVNAATR EGYRIAHDIS 130 140 150 160 170 180 AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE RAIPNYNVMC LAKASLEAAT RVMAADLGKE 190 200 210 220 230 240 GIRVNAISAG PIRTLAASGI KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI 250 260 TGEIVHVDAG FSITAMGELG EE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI)." Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., Burgess W.J., Heerding D.A., Yuan C.C., Head M.S., Payne D.J., Rittenhouse S.F., Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., Keller P.M., Polizzi B.J., Qiu X., Janson C.A., Huffman W.F. J. Med. Chem. 45:3246-3256(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[3]	"Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK." Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., DeWolf W.E. Jr., Elkins P.A., Head M.S., Jakas D.R., Janson C.A., Keller P.M., Manley P.J., Moore T.D., Payne D.J., Pearson S., Polizzi B.J., Qiu X., Rittenhouse S.F., Uzinskas I.N., Wallis N.G., Huffman W.F. J. Med. Chem. 46:1627-1635(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23379.1.
PIR	B64139.
RefSeq	NP_439876.2. NC_000907.1.
3D structure databases
ProteinModelPortal	P44432.
SMR	P44432. Positions 2-259.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1734.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC23379; AAC23379; HI_1734.
GeneID	950535.
KEGG	hin:HI1734.
PATRIC	20192225. VBIHaeInf48452_1815.
Phylogenomic databases
eggNOG	COG0623.
KO	K00208.
OMA	LVHCLAF.
ProtClustDB	CLSK918312.
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...
Other
BindingDB	P44432.

Entry information

Entry name

FABI_HAEIN

Accession

Primary (citable) accession number: P44432

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program