ID Q8CV98_OCEIH Unreviewed; 447 AA.
AC Q8CV98;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:BAC12815.1};
GN OrderedLocusNames=OB0859 {ECO:0000313|EMBL:BAC12815.1};
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109 {ECO:0000313|EMBL:BAC12815.1, ECO:0000313|Proteomes:UP000000822};
RN [1] {ECO:0000313|EMBL:BAC12815.1, ECO:0000313|Proteomes:UP000000822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831
RC {ECO:0000313|Proteomes:UP000000822};
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12815.1; -; Genomic_DNA.
DR RefSeq; WP_011065265.1; NC_004193.1.
DR AlphaFoldDB; Q8CV98; -.
DR STRING; 221109.gene:10733080; -.
DR KEGG; oih:OB0859; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9792592at2; -.
DR PhylomeDB; Q8CV98; -.
DR Proteomes; UP000000822; 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; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000000822}.
FT DOMAIN 4..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 447 AA; 48785 MW; 0388A6FEB4647773 CRC64;
MSKKIIIVGG VGGGATVAAQ IRRTNKTAEI LVLERNGYVS FANCGMPYYL GGTITDRQKL
IYPEEKFAQK YDLTVQTHAN VTKINREQKS VVYEKYKTEH KADYDILILS PGASPVLPDI
AGLQQSNTFP LRTIEDMDNI EQFIQSNNPQ SAAIIGGGFI GLEMAESLCH RGFSCSLVDR
SEHVLKRIDK EMAIHIDEHL QEKGIALYVN DGLKSFSDNG TTLHLSSDKT IQADMTIMAI
GIKPNTELAI DAGLEIGETG GIKVNQYMQT TDPTIFALGD AVEVTDFITR EPAHIALAWP
AHRQAFIISS FLSGNPISDD GIIGSSILRV FDLTVAATGQ NKQTLIDNEI AFEETIMKGY
SHAAYYPGSK ELWMQIVYDK NTGQLFGGSV IGFDGADKRM AVLATAIKGK LTVADLASLE
LGYSPIYSGA KDPLNILGYK AMEQLED
//
