ID A0A1X7GTH2_9ACTN Unreviewed; 601 AA.
AC A0A1X7GTH2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SMF74506.1};
GN ORFNames=SAMN02745830_05753 {ECO:0000313|EMBL:SMF74506.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF74506.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF74506.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF74506.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWZW01000014; SMF74506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7GTH2; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000192930; Unassembled WGS sequence.
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:SMF74506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192930};
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..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 601 AA; 65197 MW; B1AF8908694820B5 CRC64;
MSTKVSDHIL RRLREWGVEH VFAYPGDGIN GLLAAWGRAD DDPRFIQSRH EEMSAFQAVG
YAKFSGRVGV CAATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTDRSAMGG SYQQEVDLLS
LYKDVASDFC EMVTVPEQLP NVLDRALRTA IARRTVTAVI VPADVQQLDH SPPEHAFKMV
PSSLGMPHYA PMPDDEDLRR AADVLNSCGK IALLIGQGAR HARTEVMAVA DRLGAGVAKA
LLGKDALDDD LPYVTGAIGL LGTRPSYEMM RECDGLLVIG SSFPYSQFLP EFGQARAVQI
DIDPHMVGLR YPFEVNLVGD AARTLRRLLP LLDQVEDPAW RTKIEDNVTR WWEVMDRRAA
VGADPINPEQ VAHALNDVLP ENVILSADSG SAANWYARHL KLRGAMRGSL SGTLATMGPG
VPYAIGAKFA HGDRPAIALV GDGAMQMNGM AELITVAKYW REWEDPRLIV AVFNNQDLNQ
VTWEMRAMSG APQFLPSQSI PDVGYADFAR SLGLAGVRVE KPEQVAGAWE TALAADRPCV
LDFVTDPAVP PIPPHATLEQ IEAAVASVLK GDSDRGAMVR QGFKAKIQDF LPGNRHGESG
R
//
