FABI_HAEIN
ID FABI_HAEIN Reviewed; 262 AA.
AC P44432;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI;
DE Short=ENR;
DE EC=1.3.1.9;
DE AltName: Full=NADH-dependent enoyl-ACP reductase;
GN Name=fabI; Synonyms=envM; OrderedLocusNames=HI_1734;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP ACTIVITY REGULATION.
RX PubMed=12109908; DOI=10.1021/jm020050+;
RA Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., Burgess W.J.,
RA Heerding D.A., Yuan C.C., Head M.S., Payne D.J., Rittenhouse S.F.,
RA Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., Keller P.M.,
RA Polizzi B.J., Qiu X., Janson C.A., Huffman W.F.;
RT "Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP
RT reductase (FabI).";
RL J. Med. Chem. 45:3246-3256(2002).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=12699381; DOI=10.1021/jm0204035;
RA Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., DeWolf W.E. Jr.,
RA Elkins P.A., Head M.S., Jakas D.R., Janson C.A., Keller P.M., Manley P.J.,
RA Moore T.D., Payne D.J., Pearson S., Polizzi B.J., Qiu X., Rittenhouse S.F.,
RA Uzinskas I.N., Wallis N.G., Huffman W.F.;
RT "Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases
RT FabI and FabK.";
RL J. Med. Chem. 46:1627-1635(2003).
CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an
CC enoyl moiety that is covalently linked to an acyl carrier protein
CC (ACP). Involved in the elongation cycle of fatty acid which are used in
CC the lipid metabolism (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC -!- ACTIVITY REGULATION: Inhibited by 1,4-benzodiazepine and
CC naphthyridinone derivatives. {ECO:0000269|PubMed:12109908,
CC ECO:0000269|PubMed:12699381}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC23379.1; -; Genomic_DNA.
DR PIR; B64139; B64139.
DR RefSeq; NP_439876.2; NC_000907.1.
DR RefSeq; WP_005649928.1; NC_000907.1.
DR AlphaFoldDB; P44432; -.
DR SMR; P44432; -.
DR STRING; 71421.HI_1734; -.
DR BindingDB; P44432; -.
DR PRIDE; P44432; -.
DR EnsemblBacteria; AAC23379; AAC23379; HI_1734.
DR KEGG; hin:HI_1734; -.
DR PATRIC; fig|71421.8.peg.1815; -.
DR eggNOG; COG0623; Bacteria.
DR HOGENOM; CLU_010194_10_1_6; -.
DR PhylomeDB; P44432; -.
DR BioCyc; HINF71421:G1GJ1-1750-MON; -.
DR SABIO-RK; P44432; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..262
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT /id="PRO_0000054901"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 19..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 192..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 201
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT SITE 204
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT SITE 205
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 28119 MW; 71CEF6189795388E CRC64;
MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE FAKEFGSDIV
LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL DGDYVNAATR EGYRIAHDIS
AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE RAIPNYNVMC LAKASLEAAT RVMAADLGKE
GIRVNAISAG PIRTLAASGI KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI
TGEIVHVDAG FSITAMGELG EE
