ID E6MYR1_NEIMH Unreviewed; 261 AA.
AC E6MYR1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN ORFNames=NMH_1909 {ECO:0000313|EMBL:EFV63313.1};
OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=909420 {ECO:0000313|EMBL:EFV63313.1, ECO:0000313|Proteomes:UP000032707};
RN [1] {ECO:0000313|EMBL:EFV63313.1, ECO:0000313|Proteomes:UP000032707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76 {ECO:0000313|EMBL:EFV63313.1,
RC ECO:0000313|Proteomes:UP000032707};
RX PubMed=21378179; DOI=10.1128/JB.01331-10;
RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA van de Beek D., Pannekoek Y., van der Ende A.;
RT "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL J. Bacteriol. 193:2371-2372(2011).
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 Evidence={ECO:0000256|PIRNR:PIRNR000094};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000256|ARBA:ARBA00009233,
CC ECO:0000256|PIRNR:PIRNR000094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV63313.1}.
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DR EMBL; AEQZ01000038; EFV63313.1; -; Genomic_DNA.
DR RefSeq; WP_002223367.1; NZ_AEQZ01000038.1.
DR AlphaFoldDB; E6MYR1; -.
DR SMR; E6MYR1; -.
DR GeneID; 83615070; -.
DR PATRIC; fig|909420.3.peg.437; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000032707; Unassembled WGS sequence.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 {ECO:0000256|PIRNR:PIRNR000094};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000094};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000094}.
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 19..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-2"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 193..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ SEQUENCE 261 AA; 27691 MW; AF2D0C70F550253D CRC64;
MGFLQGKKIL ITGMISERSI AYGIAKACRE QGAELAFTYV VDKLEERVRK MAAELDSELV
FRCDVASDDE INQVFADLGK HWDGLDGLVH SIGFAPKEAL SGDFLDSISR EAFNTAHEIS
AYSLPALAKA ARPMMRGRNS AIVALSYLGA VRAIPNYNVM GMAKASLEAG IRFTAACLGK
EGIRCNGISA GPIKTLAASG IADFGKLLGH VAAHNPLRRN VTIEEVGNTA AFLLSDLSSG
ITGEITYVDG GYSINALSTE G
//
