ID B8CZZ3_HALOH Unreviewed; 449 AA.
AC B8CZZ3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACL70845.1};
GN OrderedLocusNames=Hore_21000 {ECO:0000313|EMBL:ACL70845.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70845.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL70845.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL70845.1; -; Genomic_DNA.
DR RefSeq; WP_015923814.1; NC_011899.1.
DR AlphaFoldDB; B8CZZ3; -.
DR STRING; 373903.Hore_21000; -.
DR KEGG; hor:Hore_21000; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000000719; 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; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000719}.
FT DOMAIN 1..290
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..431
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 449 AA; 48445 MW; 8E035CD5E1C8D000 CRC64;
MKIAIIGGVA AGTSAAAKAH RENPEAEIIL FEKDENISYA GCGLPYYISG VTDSRQKVVI
NTPEAFTKKY KVEVRTGHRV DEIIPDKKLI RYRNLKNNRD GEYRYDKLII TTGASPVIPP
IPGIKLNNIL TLRTINHADM IKNILNKNKP ERVSIIGAGL IGLEMAESFS KLGLKVTVIE
KLPQVLPQFS PEMAQIVGAH LKENGVDLLL KDGVVKFTGD NSVEKVITES GQEIKTDLVL
VSVGIRPNVE LARKAGIKIG PTGAIAVNNK MQTSLSDIYA AGDCAESTDL VSGKSIWAPL
GSTANKQGRV AGENAAGGNN RHDGVLKTAI TKVFDLTVAR TGLSEKEASE AGFDPIGVKI
KAVNHAGYYP GLDKLHIKGV FDKKTKRIIG AEVIGKNGAD KRIDVLSTAI YSKLTTHDLF
QLDLAYAPPY STPKDAVARL GMVSQKKFK
//
