FABI_HELPY
ID FABI_HELPY Reviewed; 275 AA.
AC O24990;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
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; OrderedLocusNames=HP_0195;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITORS,
RP AND SUBUNIT.
RX PubMed=17879346; DOI=10.1002/prot.21586;
RA Lee H.H., Moon J., Suh S.W.;
RT "Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein
RT reductase in complex with hydroxydiphenyl ether compounds, triclosan and
RT diclosan.";
RL Proteins 69:691-694(2007).
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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17879346}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; AE000511; AAD07262.1; -; Genomic_DNA.
DR PIR; C64544; C64544.
DR RefSeq; NP_206994.1; NC_000915.1.
DR RefSeq; WP_000506216.1; NC_018939.1.
DR PDB; 2PD3; X-ray; 2.50 A; A/B/C/D=1-275.
DR PDB; 2PD4; X-ray; 2.30 A; A/B/C/D=1-275.
DR PDBsum; 2PD3; -.
DR PDBsum; 2PD4; -.
DR AlphaFoldDB; O24990; -.
DR SMR; O24990; -.
DR IntAct; O24990; 1.
DR STRING; 85962.C694_00970; -.
DR DrugBank; DB04393; Soneclosan.
DR DrugBank; DB08604; Triclosan.
DR PaxDb; O24990; -.
DR EnsemblBacteria; AAD07262; AAD07262; HP_0195.
DR KEGG; hpy:HP_0195; -.
DR PATRIC; fig|85962.47.peg.210; -.
DR eggNOG; COG0623; Bacteria.
DR OMA; GILDMIH; -.
DR PhylomeDB; O24990; -.
DR BRENDA; 1.3.1.9; 2604.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; O24990; -.
DR Proteomes; UP000000429; 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 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..275
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT /id="PRO_0000054902"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT BINDING 19..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT BINDING 95
FT /ligand="substrate"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT BINDING 191..195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17879346"
FT SITE 203
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2PD4"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2PD4"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 156..177
FT /evidence="ECO:0007829|PDB:2PD4"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2PD4"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2PD4"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:2PD4"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2PD4"
SQ SEQUENCE 275 AA; 29981 MW; 1894A5AA2105895A CRC64;
MGFLKGKKGL IVGVANNKSI AYGIAQSCFN QGATLAFTYL NESLEKRVRP IAQELNSPYV
YELDVSKEEH FKSLYNSVKK DLGSLDFIVH SVAFAPKEAL EGSLLETSKS AFNTAMEISV
YSLIELTNTL KPLLNNGASV LTLSYLGSTK YMAHYNVMGL AKAALESAVR YLAVDLGKHH
IRVNALSAGP IRTLASSGIA DFRMILKWNE INAPLRKNVS LEEVGNAGMY LLSSLSSGVS
GEVHFVDAGY HVMGMGAVEE KDNKATLLWD LHKEQ
