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Database: UniProt
Entry: D9PZ19_ACIS3
LinkDB: D9PZ19_ACIS3
Original site: D9PZ19_ACIS3 
ID   D9PZ19_ACIS3            Unreviewed;       437 AA.
AC   D9PZ19;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:ADL19806.1};
GN   OrderedLocusNames=ASAC_1401 {ECO:0000313|EMBL:ADL19806.1};
OS   Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS   345-15).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19806.1, ECO:0000313|Proteomes:UP000000346};
RN   [1] {ECO:0000313|EMBL:ADL19806.1, ECO:0000313|Proteomes:UP000000346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC   {ECO:0000313|Proteomes:UP000000346};
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT   a new order, Acidilobales, and suggests an important ecological role in
RT   terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
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}.
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DR   EMBL; CP001742; ADL19806.1; -; Genomic_DNA.
DR   RefSeq; WP_013267318.1; NC_014374.1.
DR   AlphaFoldDB; D9PZ19; -.
DR   STRING; 666510.ASAC_1401; -.
DR   GeneID; 9499658; -.
DR   KEGG; asc:ASAC_1401; -.
DR   eggNOG; arCOG01069; Archaea.
DR   HOGENOM; CLU_003291_1_3_2; -.
DR   InParanoid; D9PZ19; -.
DR   OMA; DKNHTNY; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000000346; Chromosome.
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:SF1; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 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; PR00469; PNDRDTASEII.
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:UP000000346}.
FT   DOMAIN          2..275
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          325..423
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   437 AA;  47270 MW;  A4EDB05EEACBCA63 CRC64;
     MEILVIGGGA AGMSAASWAR RRAPDARITV LERTNIISHA PCGVPYYIGG LFKDYWLLQA
     YDVKFFRERR NIEVITNAEA EELDVKSRVA VARMGGQRVK LEFDRLVIAT GARPRRLNNV
     DDAKVIYVHH PADAETARRA AEAAREVTVV GGGVLGVEMA EQLRNMGKVI HLVHRGPYLM
     SRDLDEELGS GLTEMARRAG VDLRLGVTVA EASGDRVRLS DGSELRSDLV VAAVGVEPDV
     DLVRGQLRLG PHGAIAVDDR LQATYDYAFA AGDAMEHRNM VTGQPDWRPL APIANKSGLV
     AGVNAAGGDK RFPGVLGDIV TRFEGVAFGR VGLNEAEARR ANIRYVTSII TTRSRARYYP
     GGGDVTVKLL AEESSGVIIG GQVAGPEEVI GRLGVIAAAI MKRMTAEELF FVEIGYHPSS
     GRAWDPVVLA ARQLMRI
//
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