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Database: UniProt
Entry: A0A1Y4RS12_9FIRM
LinkDB: A0A1Y4RS12_9FIRM
Original site: A0A1Y4RS12_9FIRM 
ID   A0A1Y4RS12_9FIRM        Unreviewed;       663 AA.
AC   A0A1Y4RS12;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=2-enoate reductase {ECO:0000313|EMBL:OUQ19413.1};
GN   ORFNames=B5E84_06500 {ECO:0000313|EMBL:OUQ19413.1};
OS   Lachnoclostridium sp. An14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965562 {ECO:0000313|EMBL:OUQ19413.1, ECO:0000313|Proteomes:UP000196089};
RN   [1] {ECO:0000313|Proteomes:UP000196089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An14 {ECO:0000313|Proteomes:UP000196089};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC       oxidoreductase/NADH oxidase family. {ECO:0000256|ARBA:ARBA00011048}.
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:OUQ19413.1}.
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DR   EMBL; NFLE01000008; OUQ19413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4RS12; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000196089; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023014};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196089}.
FT   DOMAIN          5..359
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          403..632
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   663 AA;  73069 MW;  48D785D983A8FF6B CRC64;
     MKYKNLFTPV KIGSVTIKNR FAMAPMGPLG LADAQGGFNQ RGIDYYTERA KGGTGLIITG
     VTFSDCKVET QSMPNCPNST YNPVHFIRTS KEMTERVHAY GSKIFLMMSA GFGRVTIPTN
     LGEFPPVAPS AIPHRWLDKI CRPLTVEEIR SIVKSFGDGA YNAKRGGFDG VEIHAVHEGY
     LLDQFAISMF NLRNDEYGGS LENRLRFAKE VVEEIKSRCG DDFPVALRFS VKSMIKDWRE
     GALPGEEFEE KGRDIEEGLE AAKLLVEYGY DALDTDVGTY DAWWWNHPPM YQEKGLFRPY
     CKMVKDVVDV PVLCAGRMDN PDMASAAVEN GECDIVSLGR PLLADPDYVN KLRCGRYDEV
     RPCISCQEGC MGRIQEYSMI NCAVNPQAAR ERAMAYEPVL KSKKVMVVGG GVAGCEAARV
     LAIRGHRPEL FEKGTRLGGN LIPGGAPEFK EDDIALADWY ATMLNRLEVP VHLNHEVTKE
     EVLAGGYDAV IIATGSKPKT FSLGDDSRVY TAAQVLLKEK DCGDATVVVG GGLVGCETAL
     WLAQHGRKVT IVEALDKLLA VNGPLCHANK DMLERLVPYH GVDVITGARV KGYENGVLTA
     ETAEGEKKIP CDSVILAVGY QEENSLYHQL EFDVPELYLL GDAKKVSNIM YGIWDAFEVA
     NHI
//
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