ID E3DQZ4_HALPG Unreviewed; 494 AA.
AC E3DQZ4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADO77983.1};
GN OrderedLocusNames=Hprae_1858 {ECO:0000313|EMBL:ADO77983.1};
OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77983.1, ECO:0000313|Proteomes:UP000006866};
RN [1] {ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Halanaerobium praevalens DSM 2228.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO77983.1, ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RX PubMed=21886858;
RA Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the extremely halophilic Halanaerobium
RT praevalens type strain (GSL).";
RL Stand. Genomic Sci. 4:312-321(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP002175; ADO77983.1; -; Genomic_DNA.
DR RefSeq; WP_014554000.1; NC_017455.1.
DR AlphaFoldDB; E3DQZ4; -.
DR STRING; 572479.Hprae_1858; -.
DR KEGG; hpk:Hprae_1858; -.
DR PATRIC; fig|572479.3.peg.1891; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_9; -.
DR Proteomes; UP000006866; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006866}.
FT DOMAIN 7..341
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 378..484
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 494 AA; 54570 MW; 067A3BBFD12C29F5 CRC64;
MKQKLNYDLL VIGAGAAGFY AAREAARAGL KTAIVEKNEL GGTAFYWGSL PVKMIADKIK
AYQKTKKMLP EFKLDLKKTD FLLQAADFKK IEAKIKKDLS QAGADLFYGE GHFNSAHEFE
LKEKLIKAER VILASGSQVK TNAGLELEQE PIISHKEAVS FKKLPESMLI IGMNIEGAEF
ASIFSFLGVK VYILDQKDSL LPGIDQDLTK VLKQELEKNG VEIMTSTTLK KAEITELKNQ
KVVKVEVESN LNSKQTKTTR AVQVETAQGA SSTGTKTLIV DKILFTAGRE ANFPAGIEKM
QLAFNKQGLQ VNSKLQTTNP AVYALGDLNG NFGIASTAIN DALIAVNELK QLDIFKNKLK
AHYKKPVTHL KTAAAQTIPL NIFTLPEIGG FGLSETQLKA KNIAYRVQKY YFKDCWRSLI
SQKKGFVKIM LAAESEKILG VYFVGDQLSE IVSSLSLTAD LELKDLLENI YIQPTRTEIL
REAALMEPKL GSSF
//
