ID B9Y3W8_9FIRM Unreviewed; 630 AA.
AC B9Y3W8;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EEF69312.1};
GN ORFNames=HOLDEFILI_00498 {ECO:0000313|EMBL:EEF69312.1};
OS Holdemania filiformis DSM 12042.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemania.
OX NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF69312.1, ECO:0000313|Proteomes:UP000005950};
RN [1] {ECO:0000313|EMBL:EEF69312.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69312.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF69312.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69312.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL Submitted (FEB-2009) 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:EEF69312.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCF01000032; EEF69312.1; -; Genomic_DNA.
DR RefSeq; WP_006057709.1; NZ_GG657552.1.
DR AlphaFoldDB; B9Y3W8; -.
DR STRING; 545696.HOLDEFILI_00498; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000005950; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 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 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;
FT DOMAIN 6..321
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 369..593
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 630 AA; 69306 MW; 447813DEF6FEBD6C CRC64;
MEYPHLFSPI QLNKLTLRNR IVAAPIGELY EPKARGGAGL VVCGHTIVEP GRSSFASGEE
PTAFFKYEVE KTRQKIRACH RYGARASIEI FHAGQYARVK DHAWGPCSLI REDGVEVKAL
DSAEMERIAG LFAEAAQQAK TLGFDAIFLH FGHGWLAAQF LSPLFNHRTD EYGGSLPNRA
RFPLLILRKI REAVGPEFPV DMRISGEECV PGSIPFEDTL AFIQMAEPYI DGVQISAGLD
INHEGNVHMA TTNFKEHMPN LKWARTVKKT CPGLVVSVVG AIMNPSEAEQ ILANGDVDLV
AFGRAFIADP NWPNKAREGR TCDIVPCLRC LQCYHIATNR QNVGCSVNPR YCNETLIPER
MIPAEQAQRV VIIGAGPAGL NAAITASRRG HEVIVLEKST EIGGALNTIA REYYKEDIRS
YRDYLTNQFA QCDIDLRLNT AADRSMIEAL HPQALIIACG AQPVTPPVPG IDQSFVMGFT
EAIHHPERIG KQVVIIGGGT IGAEIGLELA ERKGRQVTIV EMTDTLASQG NLLYRIALRQ
KLDPLTNFTA LTETRCIQIG DHEVEILHQT EQRKLKADTV IIAAGVRTNR AFVNSLYGIC
PQTFEVGDAL QPRKIQEAVF EGTGVALSIE
//
