ID V1CC72_9FIRM Unreviewed; 452 AA.
AC V1CC72;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:ESE28903.1};
GN ORFNames=HMPREF9089_01304 {ECO:0000313|EMBL:ESE28903.1};
OS Eubacterium brachy ATCC 33089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE28903.1, ECO:0000313|Proteomes:UP000017536};
RN [1] {ECO:0000313|EMBL:ESE28903.1, ECO:0000313|Proteomes:UP000017536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE28903.1,
RC ECO:0000313|Proteomes:UP000017536};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:ESE28903.1}.
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DR EMBL; AXUD01000019; ESE28903.1; -; Genomic_DNA.
DR AlphaFoldDB; V1CC72; -.
DR STRING; 1321814.HMPREF9089_01304; -.
DR PATRIC; fig|1321814.3.peg.1246; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_9; -.
DR Proteomes; UP000017536; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017536}.
FT DOMAIN 11..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 347..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 452 AA; 49937 MW; E71A9C757A8313C4 CRC64;
MWFWRNKKMS KIVVVGANHA GTAAINTMLD NYSGNEVVVL ERNFNTSFLG CGMALWIGDQ
IQGGGEGLFY SSPEQLREKG AKVSINTEVE KIDFDKKIIY YSNKEDGKVE ESYDKLILAT
GSLPIIPPIP GRELENVQQV KLYQDAQAVI EKLKLGGINH VTVVGSGYIG VELAEAFKRK
GKEVALLDIA DGCLTGYYDP EFSNLMKQNL IDNGIDCKFG QALEEIKGDK KVEAVKTSNE
EFATDMVILC VGFRPNTELG KGKLEQFKNG AYIVNKKQET SVKDVYAIGD CATVYDNAVD
GINYIALATN AVRSGIIAAH NACGTAIESI GVQGSNGISI YGLHLISTGL TAEKAAKFGY
EVETTSFEDN QRPEFMKEND IVKIKIVYDK KTRRVLGMQC ASRYDMSMVN HMFSLAIQEH
VTIDRIALLD IFFLPHFNKP YNYITMAALT AK
//
