ID D7E5U0_METEZ Unreviewed; 467 AA.
AC D7E5U0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADI72962.1};
GN OrderedLocusNames=Metev_0030 {ECO:0000313|EMBL:ADI72962.1};
OS Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS / OCM 161 / Z-7303).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI72962.1, ECO:0000313|Proteomes:UP000000391};
RN [1] {ECO:0000313|EMBL:ADI72962.1, ECO:0000313|Proteomes:UP000000391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC {ECO:0000313|Proteomes:UP000000391};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA Woyke T.;
RT "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002069; ADI72962.1; -; Genomic_DNA.
DR RefSeq; WP_013193530.1; NC_014253.1.
DR AlphaFoldDB; D7E5U0; -.
DR STRING; 644295.Metev_0030; -.
DR GeneID; 9345636; -.
DR KEGG; mev:Metev_0030; -.
DR HOGENOM; CLU_003291_1_3_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000000391; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF3; NADH OXIDASE-RELATED; 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:UP000000391}.
FT DOMAIN 14..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 347..447
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 467 AA; 50585 MW; 146FADC7B7751A53 CRC64;
MVGNTSENNT KKQDLVIIGG GAVGMAVATH VQRHGNYNIK VLSKDSHTAY SQCGMPFVLA
GDIPDFNKLI VKNLQFFKDM GIDVRLNTQV NSIDLENHTV HTQIDTVRYD KLVIATGSSP
SIPEPLKEFI KMDNVFTLRT LSDGIKIQNN LEKSKNLVVI GAGGIGVEIA VAGVKRGIST
TLINRSKNVL SHNLDSDMSQ ILQNHLDSKG INLLTGHTPV SINGSDTAES VTIKENITGK
IKNISVDTIV ISTGVNPEVS LAKNAGISVG ESGGLLVNNK LQVKYDNKYL DDVFAGGECA
QVYDFVTGNP FVSQLASTAR RMASVIAENL LEKTSTFTPI TNPWIGVIGD YQVGNVGLTE
KTAYKNKINT VTGSSTGFTR AGYYPGGEKI YIKLLFSNRC LSGAQIIGRK GVKERIDGLS
LAIRKKASID DMLKMETCYT PPVSELVDPI TYAVKDAYKN MDNQKYD
//
