ID R5SKK7_9FIRM Unreviewed; 289 AA.
AC R5SKK7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase family protein {ECO:0000313|EMBL:CCZ53648.1};
GN ORFNames=BN540_00180 {ECO:0000313|EMBL:CCZ53648.1};
OS Dialister invisus CAG:218.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=1263072 {ECO:0000313|EMBL:CCZ53648.1, ECO:0000313|Proteomes:UP000017966};
RN [1] {ECO:0000313|EMBL:CCZ53648.1, ECO:0000313|Proteomes:UP000017966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:218 {ECO:0000313|Proteomes:UP000017966};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CCZ53648.1}.
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DR EMBL; CBAF010000052; CCZ53648.1; -; Genomic_DNA.
DR AlphaFoldDB; R5SKK7; -.
DR Proteomes; UP000017966; 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; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017966}.
FT DOMAIN 3..151
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 180..284
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 289 AA; 31600 MW; 8A6DAE863CE84B66 CRC64;
MMENETLPRR LTIIGGGYIG LEFASMYARF GSKVTILQNG SVFLPKEDRD MAEAVENVLK
SYGVSVITGA GLKEIKEGTA VYTKNGEEDT LDGDAILLAT GRGPNTEGLH AERAGVELTK
RGAVVTDKHL RTTAENIWAA GDVCGNLQFT YISLDDSRII LSDMQGDGSR TTENRGAFAY
SVFMEPSFSR AGLSEKEAAD KGLNYRVVRM NTDMIPKAKV LRKTAGMLKA VIDKDSGKIL
GAALFCPESY EIINMVKLAM DHDLDYTVLR DFIYTHPTMS EGLNDLFAL
//
