ID A0A1G2AS71_9BACT Unreviewed; 343 AA.
AC A0A1G2AS71;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=A3B74_00875 {ECO:0000313|EMBL:OGY79379.1};
OS Candidatus Kerfeldbacteria bacterium RIFCSPHIGHO2_02_FULL_42_14.
OC Bacteria; Candidatus Kerfeldbacteria.
OX NCBI_TaxID=1798540 {ECO:0000313|EMBL:OGY79379.1, ECO:0000313|Proteomes:UP000177165};
RN [1] {ECO:0000313|EMBL:OGY79379.1, ECO:0000313|Proteomes:UP000177165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:OGY79379.1}.
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DR EMBL; MHKB01000009; OGY79379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2AS71; -.
DR STRING; 1798540.A3B74_00875; -.
DR Proteomes; UP000177165; Unassembled WGS sequence.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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 PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 7..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 343 AA; 36589 MW; A633722FF8E941C1 CRC64;
MNVSHPYDLI IIGAGPGGCA AAVYAGRKQL KTLVITESFG GQSIVSNSIE NWIGEKTISG
VELAKKLEAH VRAQETVTVK TGEKVIVVRE VGDMCISTLD WKKLSSVAAS ANAACEYEVT
TDKGGVFRAK ALLVASGGRR RRLDVLGEAQ FDGKGVSYCS TCDAPLFRGK DVAVVGGGNA
GLEACVDLFP YAKKIYLLNI GDKLGGDPIT QKQVFDSSRV TVIHHAQTME IFGETLVTGL
KYQDTVSGVE KKLAAQGVFV EIGSIPNSEF VKDLVQMNKY NEIIVDHKTL ATSRPGIFAA
GDVTDEIYKQ NNTSVGDAVS ATLSAYNYLL NISKQTPAAQ ETV
//
