ID A0A1X4NBI7_9PROT Unreviewed; 252 AA.
AC A0A1X4NBI7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=THS27_08750 {ECO:0000313|EMBL:OSQ43902.1};
OS Thalassospira sp. MCCC 1A01428.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ43902.1, ECO:0000313|Proteomes:UP000193740};
RN [1] {ECO:0000313|EMBL:OSQ43902.1, ECO:0000313|Proteomes:UP000193740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ43902.1,
RC ECO:0000313|Proteomes:UP000193740};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000175,
CC 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:OSQ43902.1}.
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DR EMBL; JFJZ01000008; OSQ43902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NBI7; -.
DR STRING; 1470575.THS27_08750; -.
DR OrthoDB; 9803628at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000193740; 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; 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 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 17..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 62..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-2"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ SEQUENCE 252 AA; 27001 MW; 5668C2046947FA8F CRC64;
MLAGKKGLVI GIANDKSIAY GCAQAFRRDG ADLAVTYLNQ KAEKYVRPLA ENVDASIIAP
LDVCDEAQAD ALFADIGEKW GKLDFVLHCI AFAPADDLHG RVVDCSRDGF LTAMDISCHS
FQRIAKRAEP LMADGGALLT VSYMGSERVI DHYGIMGPVK AALESATRYM AAELGPQGIR
VHAISPGPLL TRAASGIAEF DNLMTQARAR SPEHRLVTID EIGDLASFLA SDRSRAITGD
VIHIDGGYHI MG
//