ID   B0CEP5_ACAM1            Unreviewed;       258 AA.
AC   B0CEP5;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   OrderedLocusNames=AM1_3154 {ECO:0000313|EMBL:ABW28150.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Acaryochloridaceae; Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW28150.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW28150.1, ECO:0000313|Proteomes:UP000000268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC         NADH + H(+); 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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FabI subfamily. {ECO:0000256|ARBA:ARBA00009233,
CC       ECO:0000256|PIRNR:PIRNR000094}.
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DR   EMBL; CP000828; ABW28150.1; -; Genomic_DNA.
DR   RefSeq; WP_010468727.1; NC_009925.1.
DR   AlphaFoldDB; B0CEP5; -.
DR   STRING; 329726.AM1_3154; -.
DR   KEGG; amr:AM1_3154; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_3; -.
DR   OrthoDB; 9803628at2; -.
DR   Proteomes; UP000000268; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05372; ENR_SDR; 1.
DR   FunFam; 1.10.8.400:FF:000001; Enoyl-[acyl-carrier-protein] reductase [NADH]; 1.
DR   FunFam; 3.40.50.720:FF:000169; Enoyl-[acyl-carrier-protein] reductase [NADH]; 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   NCBIfam; NF005615; PRK07370.1; 1.
DR   PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH], CHLOROPLASTIC; 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|ARBA:ARBA00023160,
KW   ECO:0000256|PIRNR:PIRNR000094};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR000094};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000094};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT   ACT_SITE        158
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         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-2"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         194..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ   SEQUENCE   258 AA;  27365 MW;  2D64EBF5678DAF08 CRC64;
     MLDLTGKNAL VTGIANNRSI AWGIAQQLHS AGANLGITYL PDEKGRNESK VKKLVEPLAP
     SLFLPCNVQD QAQVDATFSS IQQQWGKLDI LIHCLAFANR EDLGGDFSAV QQDNFNLALD
     VSAYSLVQLS AAAKPLMTEG GSIVTLTYLG GARVVPNYNV MGIAKAALEM NVRYLAAEMG
     PQNVRVNGIS AGPIRTLASS AVGGILDMIH HVEEVAPLKR TVTQTEVGNT AAFLCSDLST
     GITGQILYVD SGYSIMGM
//