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Database: UniProt
Entry: D8GQ32_CLOLD
LinkDB: D8GQ32_CLOLD
Original site: D8GQ32_CLOLD 
ID   D8GQ32_CLOLD            Unreviewed;       657 AA.
AC   D8GQ32;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Enoate reductase {ECO:0000313|EMBL:ADK16123.1};
DE            EC=1.3.1.31 {ECO:0000313|EMBL:ADK16123.1};
GN   OrderedLocusNames=CLJU_c30750 {ECO:0000313|EMBL:ADK16123.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK16123.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK16123.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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}.
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DR   EMBL; CP001666; ADK16123.1; -; Genomic_DNA.
DR   RefSeq; WP_013239712.1; NZ_LITS01000027.1.
DR   AlphaFoldDB; D8GQ32; -.
DR   STRING; 748727.CLJU_c30750; -.
DR   KEGG; clj:CLJU_c30750; -.
DR   PATRIC; fig|748727.19.peg.2240; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_1_9; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000001656; Chromosome.
DR   GO; GO:0047540; F:2-enoate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   CDD; cd02803; OYE_like_FMN_family; 1.
DR   CDD; cd01029; TOPRIM_primases; 1.
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   InterPro; IPR034154; TOPRIM_DnaG/twinkle.
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; PR00469; PNDRDTASEII.
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   Oxidoreductase {ECO:0000313|EMBL:ADK16123.1}.
FT   DOMAIN          4..343
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          396..628
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   657 AA;  71573 MW;  DBCFC60BEF82F937 CRC64;
     MYQKLFSSKN IGSMTVRNRI VMTAMGNHLA EADGSVSESD IAFYGERAKG GVGLVITECA
     CINLKIGKGN CHQIAVDDDK YIEGLKRMAD EIHKYGSVIA VQIYHPGRQG IAVINGNTSM
     QAPSVTECQV VHQPTHEMTK EEIKDTIHRF IQGAKRLQKA GIDAVELHGA HGYMIGQFLS
     PYTNKRTDEY GGSFENRMRF LDEIIAGVRK ECGSSYPIIV RYSADECMGY AGYPELGIHL
     DEGVKIAKHL EAQGVDALDV SCGIYETMNT SWEPVGFDQG WKINIPAKIK ESVSIPVIGV
     SVIREPEFAE KVLEEEKVDF IGSARQFFAD PEWGNKAQEG KEKSIRKCIS CLYCMETLMS
     ADMGAAPMAC AINYQGGREN QYGDDCLKKD GKGRVVVVIG AGPSGMEAAR ILAKRKFKPI
     VFEKNSKVGG QIVYASKPPK KEKTAWLIDY QKGQLDELGV EVKTNHAPTI DEIKALNPYA
     VFVAQGSNPI MPKAIPGLDG EKVYTPVDIL SGKVTLKGKK VGVIGSGMTG IETAELLGSQ
     GNKVTVFEMA DEIGPGIFFQ NLIDVMGRIA EHEIKLYPKH KLVKIDGTTV TVETTNTNET
     KNFDFDAVVV SLGTASNKEL VEEIKTAFDK VVLLGDAAKA GRIEAAVGSG YKAAFEL
//
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