ID A0A1H1TL30_9ACTN Unreviewed; 604 AA.
AC A0A1H1TL30;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SDS60882.1};
GN ORFNames=SAMN04489717_3243 {ECO:0000313|EMBL:SDS60882.1};
OS Actinopolymorpha singaporensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Actinopolymorphaceae; Actinopolymorpha.
OX NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS60882.1, ECO:0000313|Proteomes:UP000198983};
RN [1] {ECO:0000313|EMBL:SDS60882.1, ECO:0000313|Proteomes:UP000198983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS60882.1,
RC ECO:0000313|Proteomes:UP000198983};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; LT629732; SDS60882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1TL30; -.
DR STRING; 117157.SAMN04489717_3243; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000198983; Chromosome i.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:SDS60882.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198983};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 604 AA; 65903 MW; 1C90ECC78EE56FDD CRC64;
MPLTADFILE RLRAWGIHRI YGYPGDGINA FLGALDRADG DPEIIQPRHE EMGAFMATAH
AKFTGGIGCC MATSGGGTIH LLNGLYDAKL DHQPVVAIIG QQKRIALGSG YQQEIDPNSL
YKDVSADFLQ TCMHPAQARQ LVDRACKVAL NNRTVATIIV PEDVAEEEAQ PSPPRQHGAV
YTSVGWTKPR VIPPETEIRV AADILNQGQK VAMLVGQGAS DSADEVVEAA ELLGAGIAKT
SLGRAVLPDD LPYSTGPIGL LGSTASYEMM RDADTLFMIG TSFPYAEWLP QEGQCKGVEI
DLDGKMIGVR YPMDSHLVGD AKSTLKELIP LLRRKEDRSW RKKIEGEVAE WWRVLDDRAH
DKADPLNPEL VVHELSERLP DDTIVTTDAG TAANWWARHL RLREGMMASL AGNLATMGPG
TPYAISARFS YPDRPVIALI GDGVFQMNGM AELITVKRYR DRIGDAPLVF CVFNNQDLNQ
VTWEQRAMAG DPKFEGTQRI PDVPYAEFAK LLGFTGVRCD SPKRIGAAWD EVLSAGGPAV
LEVVVDPEIP PVPPHFMKMQ AKKAAQALRK GDPEAVGIAV KGTKQKGHEF TESIRRHLLP
GGVR
//
