ID Q9HJX5_THEAC Unreviewed; 435 AA.
AC Q9HJX5;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=NADH peroxidase related protein {ECO:0000313|EMBL:CAC11966.1};
GN OrderedLocusNames=Ta0837 {ECO:0000313|EMBL:CAC11966.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC11966.1, ECO:0000313|Proteomes:UP000001024};
RN [1] {ECO:0000313|EMBL:CAC11966.1, ECO:0000313|Proteomes:UP000001024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC {ECO:0000313|Proteomes:UP000001024};
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445065; CAC11966.1; -; Genomic_DNA.
DR RefSeq; WP_010901248.1; NC_002578.1.
DR AlphaFoldDB; Q9HJX5; -.
DR STRING; 273075.gene:9572051; -.
DR PaxDb; 273075-Ta0837; -.
DR EnsemblBacteria; CAC11966; CAC11966; CAC11966.
DR GeneID; 1456380; -.
DR KEGG; tac:Ta0837; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR InParanoid; Q9HJX5; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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; COENZYME A DISULFIDE REDUCTASE; 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;
KW Oxidoreductase {ECO:0000313|EMBL:CAC11966.1};
KW Peroxidase {ECO:0000313|EMBL:CAC11966.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001024}.
FT DOMAIN 1..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 319..419
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 435 AA; 46232 MW; 5408066E542423D8 CRC64;
MDIVVIGGGA AGMAAASKAK RVNKDANVTV IESGSFVSYA ECGIPYFLQG IVGKAEDLLH
YPLEEFTEKR GIKVITGRVV KKIDTASLSL VLDNGSAVKF DRLIIATGSR PRIPDGIASG
VFGLRSLESA IRLKEAIDGS RTITIIGAGV LGVELASTLT EAGKRVKVIS KYDRVMPQLD
PDMGKILNDY FSSKVEVEFS STPVEIKKGE DGFAVKTTVD DHVSDVVIAA VGIVPNSNIA
VDAGIKVDQR GAIITDEHME TSIPGIYAAG DVATVKNIIT GQDEMMPLAQ IANKAGRVAG
SNAAGSEMRF PGAIGSTLVK VFDMEVGFTG LNEKRASVLG IPYGKTMIKA KSRANYYPGK
EDIFVKILYD SRDKKIIGGQ VIGKDGAAWR LNTLATAIFA GFTVEDLFYD DLGYTPPFGP
VWDPLVVAGS VSMRE
//
