ID W7IL98_9PSEU Unreviewed; 598 AA.
AC W7IL98; A0A8E3BD57;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:PWW53691.1};
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EWC61123.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:EWC61123.1};
GN ORFNames=DFQ13_11575 {ECO:0000313|EMBL:PWW53691.1}, UO65_3604
GN {ECO:0000313|EMBL:EWC61123.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC61123.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC61123.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC61123.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
RN [2] {ECO:0000313|EMBL:PWW53691.1, ECO:0000313|Proteomes:UP000247287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8578 {ECO:0000313|EMBL:PWW53691.1,
RC ECO:0000313|Proteomes:UP000247287};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAY-2018) 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:EWC61123.1}.
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DR EMBL; AYXG01000130; EWC61123.1; -; Genomic_DNA.
DR EMBL; QHCP01000015; PWW53691.1; -; Genomic_DNA.
DR RefSeq; WP_035283894.1; NZ_QHCP01000015.1.
DR AlphaFoldDB; W7IL98; -.
DR STRING; 909613.UO65_3604; -.
DR PATRIC; fig|909613.9.peg.3605; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR Proteomes; UP000247287; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0047112; F:pyruvate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; 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; 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; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:EWC61123.1};
KW Pyruvate {ECO:0000313|EMBL:EWC61123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 598 AA; 64438 MW; 8DF4E081EAE45A91 CRC64;
MSETVADHLL RRLREWGVDQ VFAYPGDGIN GIVAAFGRAD DRPRFVQVRH EEMAAFAAVG
HAKFSGSVGV CLATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTSRSAMGG SYQQEVDLQA
LFKDVAGDYL VEVNVAEQLP NALDRAIRTA QATRSPTAVI IPADLQELEY TAPRHEFKHV
PSSPPSAAWS TTVAPAEGVA RAAELINAGS KVAILIGQGA RGAAEQVREL AEVTGAGVAK
ALLGKDVLSD ELPWVTGAIG LLGTRPSYEM MRDCDTLVIV GSNFPYSQFL PEFGQARAVQ
IDVDGRHIGL RYPTEVNLVG DSAHTLDSLI PLLVPKTDRS WRTTIEGNVA SWWDTMDRQA
ALEAKPVNPM RIVSELSARI PLDAIVTADS GSSTNWYARH LKIRGDIRAS LSGTLASMGP
AVPYAIGAKF AHPDRPVVAL VGDGAMQMNG LAELITIARY RHRWSDQRLV VCVFHNNDLN
QVTWELRAMG GAPKFEESQS LPEVDYAGFA RSLGLAAITV EHPDQLGPAW DKAFAADSPM
VLDVHCDPEV PPIPPHATFE QVRSVTEAVL KGDPAALHLI TQGAKTKLQE FLPDRDRD
//
