ID B0N8A4_9FIRM Unreviewed; 664 AA.
AC B0N8A4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EDS18043.1};
GN ORFNames=CLORAM_02839 {ECO:0000313|EMBL:EDS18043.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS18043.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS18043.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18043.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS18043.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18043.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:EDS18043.1}.
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DR EMBL; ABFX02000008; EDS18043.1; -; Genomic_DNA.
DR RefSeq; WP_003538936.1; NZ_DS499659.1.
DR AlphaFoldDB; B0N8A4; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR Proteomes; UP000005798; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005798}.
FT DOMAIN 8..357
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 403..628
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 664 AA; 74377 MW; ED16F28670CB274B CRC64;
MNQYYPHLFQ PLRVNTMMLK NRIIASTMGI PKSHELLSTT HYGNVSIIDK SVGGAAMTFV
SIESAANANG EFPKHDRDGI RESISVARQY GAKVGTWCVP RLKQDAANDI RAHYDGKQVL
APSPYLTRSG ARAVELTLED IQGIMKQARN DALAIKRFGF DFIYLYVGYE ELTTQFLSPV
FNKRTDEYGG SLENRMRFTI EHVKTIRNAV GTDFPIVILL GASDYLKGSY QFEEMLELLK
RIEDDVDLIN VSAGMDMIPG YFPEDQIIEP ELGLEAWYSV NGKHCQSIFE PHLTNVHWAK
LVKQNFPNKL VGVIGSIMTP KEAEQLLQEG VVDIISMGRP LVADPFLPRK AMQGQSDDIV
PCIRCLQCYH SATEHTNVQC SVNPRYRREH RVPLKLEKSE IIKKVIVVGG GPAGCKAAIT
AHDRGHQVIL IEQRDKLGGQ LNLAQHEMHK QELKAYRDYL ENQINKRDIQ VMYKTTATKN
LLEQLNGDVV LVAIGASPIR LHFPGEQLEY VDYFENIYPK LDSLKDNVCI VGGGQVGIEL
AVELLERGKL VTVIEMTDQI ASQGHILYRA GLRRLLKRFE KQLTILINSQ CLGFSESGVK
IINKNGESII KCDNAIIAVG MKPNREEAFK LYGIADETMM FGDCEKLGQV VGATNDAYFI
AANI
//
