ID   A3PB04_PROM0            Unreviewed;       260 AA.
AC   A3PB04;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   Name=fabI {ECO:0000313|EMBL:ABO16929.1};
GN   OrderedLocusNames=P9301_03061 {ECO:0000313|EMBL:ABO16929.1};
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO16929.1, ECO:0000313|Proteomes:UP000001430};
RN   [1] {ECO:0000313|EMBL:ABO16929.1, ECO:0000313|Proteomes:UP000001430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO16929.1,
RC   ECO:0000313|Proteomes:UP000001430};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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   -!- 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; CP000576; ABO16929.1; -; Genomic_DNA.
DR   RefSeq; WP_011862322.1; NC_009091.1.
DR   AlphaFoldDB; A3PB04; -.
DR   STRING; 167546.P9301_03061; -.
DR   KEGG; pmg:P9301_03061; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_3; -.
DR   OrthoDB; 9803628at2; -.
DR   Proteomes; UP000001430; Chromosome.
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:InterPro.
DR   CDD; cd05372; ENR_SDR; 1.
DR   FunFam; 1.10.8.400:FF:000001; 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|PIRNR:PIRNR000094, ECO:0000256|PIRSR:PIRSR000094-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001430}.
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT   BINDING         14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         20..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         68..69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-2"
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         196..200
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ   SEQUENCE   260 AA;  27759 MW;  DA7B667999C9A946 CRC64;
     MLLNLTGKKI LVTGIANNRS IAWGIAQQLS KAGAELGITY LPDDKGRFES KVRELTEPLN
     PSLFLPLDVQ NPAQIEEIFK NIKDNWGQID GLVHCLAFAG RDELIGDYSA TTSEGFDRAL
     NISAYSLAPL CKAAKPLFSD GAGVVSLTYL GSERAIPNYN VMGVAKAALE ASVRYLSAEL
     GPERQVRVNA ISAGPIRTLA SSAIGGILDM IHNVEEKAPL RRTVTQTEVG NTAAFLLSDL
     SSGISGQTIY VDAGYCINGM
//