ID L0HDK5_METFS Unreviewed; 443 AA.
AC L0HDK5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component {ECO:0000313|EMBL:AGB01408.1};
DE Flags: Precursor;
GN OrderedLocusNames=Metfor_0331 {ECO:0000313|EMBL:AGB01408.1};
OS Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB01408.1, ECO:0000313|Proteomes:UP000010824};
RN [1] {ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA Liu W.-T., Woyke T.;
RT "Complete sequence of Methanoregula formicicum SMSP.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB01408.1, ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RX PubMed=25189582;
RA Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT Sludge Blanket Reactor.";
RL Genome Announc. 2:e00870-14(2014).
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-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP003167; AGB01408.1; -; Genomic_DNA.
DR RefSeq; WP_015284372.1; NC_019943.1.
DR AlphaFoldDB; L0HDK5; -.
DR STRING; 593750.Metfor_0331; -.
DR GeneID; 14309004; -.
DR KEGG; mfo:Metfor_0331; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_0_2_2; -.
DR InParanoid; L0HDK5; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000010824; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AGB01408.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000010824}.
FT DOMAIN 2..309
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 443 AA; 46662 MW; 3828110FEC643386 CRC64;
MIVVLGGGPA GRLAAIRLAS AGREVTLVEK GGIGGQCLHY GCMPVCAMND VARHIQAAGL
FSKLGILGKV PDLDFEALLR EMAKVQETIT DVLDKETRDA GVEILYGQEG RFDGREVIVG
SESLKSEAVI LSTGSRPALP DIDGIRNEGV FTPHSLKAMK SLPGRLVIIG GGIMAAEFAY
IFSRFGSRVT VLSRSGFLKN LDETIRKRAV RELAGVEIRE GTDVLAVGGS PENLKIPLKN
GGKESVLACD AVLVAAGLTP NSGMLEGIPK RPNGEVIVDE YMQTTISGIY AAGDVTGPPF
LTPVARLQGI VAADNILGAR RKMDYSAIPQ ALNLGYELAF CSDNNPRSKP LVIPGVAGPG
TFWAVPASDT GFAKILVAPD GTLSGMATAS PGGGLIAGYM ALLMKRHFLV HDFSDFIEVH
PSTDGVYGLA KYASGVLKKH EKH
//
