ID A0A1D2WBR5_9EURY Unreviewed; 585 AA.
AC A0A1D2WBR5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 05-FEB-2025, entry version 25.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:OEC87827.1};
GN ORFNames=A9507_06540 {ECO:0000313|EMBL:OEC87827.1};
OS Methanobacterium sp. A39.
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1860100 {ECO:0000313|EMBL:OEC87827.1, ECO:0000313|Proteomes:UP000094736};
RN [1] {ECO:0000313|EMBL:OEC87827.1, ECO:0000313|Proteomes:UP000094736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A39 {ECO:0000313|EMBL:OEC87827.1,
RC ECO:0000313|Proteomes:UP000094736};
RA Woodcroft B.J.;
RT "Validation of picogram- and femtogram-input DNA libraries for microscale
RT metagenomics.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEC87827.1}.
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DR EMBL; LZPM01000009; OEC87827.1; -; Genomic_DNA.
DR RefSeq; WP_069583041.1; NZ_LZPM01000009.1.
DR AlphaFoldDB; A0A1D2WBR5; -.
DR STRING; 1860100.A9507_06540; -.
DR Proteomes; UP000094736; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProtKB-ARBA.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd00730; rubredoxin; 1.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:OEC87827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094736};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..44
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 585 AA; 64802 MW; B93DC797577F0B0A CRC64;
MAKYRCTVCN YVYDEEKEGT KFEDLPENWT CPVCNSPKSE FVLLTEEVKE LKEDESTVSD
VLVEQMAEWG VEYVFGIPGT SSLGIIDAIR KNEKIKYIQV RHEESAAFMA SAHGKLKGHV
SACLTVAGPG ATNLATGLYD AKLDHSPVLA LTGMVKRQLI GPGSFQEIDQ HSFFKPIAIF
DEILMSENQT VTLTTFAMKH AITDRGVAHI GIPNDVQKLP HTEKIISFDG SFPNKAISPP
MFVIMQAAQI INQSKRPVII AGFGAMGQGA NLLELAEKIS APIVSTFRGK GVVDEFNDLY
VGSHGGIGST AATRLVRSAD LLIVVGSSFS DMTQIPEKKT IQIDIDPMMI AKQYPVEVGL
LGSSAEILPK LNDRVKENKK ESYLDEIKKF KSDWLKLLEG EIDSKTTPVR PPYIIKVLND
KLADDAVITL DIGENTWWFG RNFWMKDTQK MILSGYLASM GFGLPAAIAA QLIYPDRQVV
CIAGDGGFSM LMADFVTAIK YELPVKIFIL NNSELGMIRQ EQLMEGYENW QTDLYNFDFA
EYARICGGIG INVEKPEQLE DAVEKALLEN KPVIVDINTD PVRFK
//
