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Database: UniProt
Entry: E0NIK1_PEDAC
LinkDB: E0NIK1_PEDAC
Original site: E0NIK1_PEDAC 
ID   E0NIK1_PEDAC            Unreviewed;       397 AA.
AC   E0NIK1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=trans-2-enoyl-CoA reductase (NAD(+)) {ECO:0000256|ARBA:ARBA00011983};
DE            EC=1.3.1.44 {ECO:0000256|ARBA:ARBA00011983};
GN   Name=xcc {ECO:0000313|EMBL:EFL94964.1};
GN   ORFNames=HMPREF0623_1832 {ECO:0000313|EMBL:EFL94964.1};
OS   Pediococcus acidilactici DSM 20284.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus; Pediococcus acidilactici group.
OX   NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL94964.1, ECO:0000313|Proteomes:UP000004470};
RN   [1] {ECO:0000313|EMBL:EFL94964.1, ECO:0000313|Proteomes:UP000004470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL94964.1,
RC   ECO:0000313|Proteomes:UP000004470};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00001615};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EFL94964.1}.
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DR   EMBL; AEEG01000009; EFL94964.1; -; Genomic_DNA.
DR   RefSeq; WP_004166781.1; NZ_GL397067.1.
DR   AlphaFoldDB; E0NIK1; -.
DR   eggNOG; COG3007; Bacteria.
DR   HOGENOM; CLU_057698_1_0_9; -.
DR   Proteomes; UP000004470; Unassembled WGS sequence.
DR   GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR   InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR   InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR   PANTHER; PTHR37480; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 1.
DR   PANTHER; PTHR37480:SF1; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 1.
DR   Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR   Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR   Pfam; PF12241; Enoyl_reductase; 1.
PE   4: Predicted;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EFL94964.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004470}.
FT   DOMAIN          83..318
FT                   /note="Trans-2-enoyl-CoA reductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF12241"
FT   DOMAIN          325..383
FT                   /note="Enoyl reductase FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF07055"
SQ   SEQUENCE   397 AA;  44594 MW;  5F7E14D98C426B78 CRC64;
     MKVKPKIVGN VIKSVNPYGC RQAVLNQINY VKSKGKYAGP KKVLILGGSS SYGLATRITT
     AFGSGADTIN VAYERGPKSP EQLGSAGWYN SIFFKQFAEQ AGLIAQNFIG DAYSDTMKQR
     VIEYIKNEFG GKIDLLVYSL AAPKRNDPRS EKVWRSVLKP IDQSMTGENI DLEHERLFTE
     TIAPATPEEI QGTAKVMGGE DWEWWIQALK EAHVLADDFK TVLYSYIGPQ MTYPFYHEGT
     LGVAKTQAER SAERINQELK PLQGRALVCV STVVTTKASV VIPIMPKYMI ALYKVMTDEA
     THETPIMHKD RVYREMIYGK HPIYDPKGRL RADHYELRPS TQAKTAALYQ QINADNFKSP
     MTGYAQFRKE FLNTAGFAVD GLENDEFEFS DLLNLKP
//
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