ID A0A1Q7LVZ7_9CREN Unreviewed; 465 AA.
AC A0A1Q7LVZ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=NADH oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ07_03570 {ECO:0000313|EMBL:OLD04596.1};
OS Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD04596.1, ECO:0000313|Proteomes:UP000186658};
RN [1] {ECO:0000313|EMBL:OLD04596.1, ECO:0000313|Proteomes:UP000186658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD04596.1}.
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DR EMBL; MNGL01000024; OLD04596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7LVZ7; -.
DR STRING; 1805098.AUJ07_03570; -.
DR Proteomes; UP000186658; 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; 3.50.50.60; 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:SF3; NITRITE REDUCTASE [NAD(P)H]; 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;
FT DOMAIN 4..311
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 332..434
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 465 AA; 49741 MW; D2D362FD0CCBFE3B CRC64;
MVRRIIVVGC GVAGTTAAFH ARKTDRTAQI TIVGDEDLPE YSRCGLPYAF SRVVPETHSL
LGYDEVFYEQ TNRVVLQLGW KVNRIKTDFQ QVEISKVSDG TKQTLEYDSL ILGTGARPGK
LSIPGAELDG VFTIRTIDDI EGLANHLSTV SAKKAAIIGA GLTGSEMAEA LLLRRVSVIE
AEIAPEILPV ILDPDMASLV RARAQEHGVE YYLASSLDKI LGEKGKVSAV QISGKNHEVQ
AVIVAVRVRP NTETAKEGGL LLGEFGGIRT DERMQTSAKN VYAAGDCVET YDRMTRRHVL
FQLSTTAVRQ AAVAGTNAGG GNARYPGSTG VTTVKLFDLE VASFGPTTAL AEKLGLHPVS
VRITGSTRLP YYPGGKDLTV KLLAEPQSGR LLGAQLVGEE GATLRANFAS MAGHLGLTVE
AFSDIETCYS PPLAPVWDPV TIAAQALVRK LSSTRKPSEL QAPRS
//