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
//