ID   FABI_HELPJ              Reviewed;         275 AA.
AC   Q9ZMN7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 136.
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=jhp_0181;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FabI subfamily. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05765.1; -; Genomic_DNA.
DR   PIR; B71964; B71964.
DR   RefSeq; WP_000506206.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMN7; -.
DR   SMR; Q9ZMN7; -.
DR   KEGG; hpj:jhp_0181; -.
DR   PATRIC; fig|85963.30.peg.840; -.
DR   eggNOG; COG0623; Bacteria.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
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   Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..275
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000054903"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
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         162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            203
FT                   /note="Involved in acyl-ACP binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  30026 MW;  E44EA1A482A0341B CRC64;
     MGFLKGKKGL IVGVANNKSI AYGIAQSCFN QGATLAFTYL NESLEKRVRP IAQELNSPYV
     YELDVSKEEH FKSLYNNIKQ DLGSLDFIVH SVAFAPKEAL EGSLLETSKS AFNTAMEISV
     YSLIELTNTL KPLLNNGASV LTLSYLGSTK YMAHYNVMGL AKAALESAVR YLAVDLGKHN
     IRVNALSAGP IRTLASSGIA DFRMILKWNE INAPLRKNVS LEEVGNAGMY LLSSLSNGVS
     GEVHFVDAGY HVMGMGAVEE KDNKATLLWD LHKEQ
//