ID A0A1E7N996_KITAU Unreviewed; 575 AA.
AC A0A1E7N996; A0A8H9I0N9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:GGU93456.1};
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OEV37214.1};
GN ORFNames=GCM10010502_53610 {ECO:0000313|EMBL:GGU93456.1}, HS99_0005260
GN {ECO:0000313|EMBL:OEV37214.1};
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV37214.1, ECO:0000313|Proteomes:UP000037395};
RN [1] {ECO:0000313|EMBL:OEV37214.1, ECO:0000313|Proteomes:UP000037395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV37214.1}, and ATCC 10762 / DSM
RC 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843 / NCIMB 8234 /
RC A-377 {ECO:0000313|Proteomes:UP000037395};
RA Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OEV37214.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV37214.1};
RA Gradnigo J.S., Johnson N., Somerville G.A.;
RT "Sequencing, Assembly and Comparative Genomics of S. aureofaciens ATCC
RT 10762.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000037395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC 12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA Gradnigo J.S., Johnson N., Somerville G.A.;
RT "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT 10762.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:GGU93456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU93456.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [5] {ECO:0000313|EMBL:GGU93456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU93456.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) 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:OEV37214.1}.
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DR EMBL; BMUB01000015; GGU93456.1; -; Genomic_DNA.
DR EMBL; JPRF03000021; OEV37214.1; -; Genomic_DNA.
DR RefSeq; WP_030558185.1; NZ_LBHA01000051.1.
DR AlphaFoldDB; A0A1E7N996; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000037395; Unassembled WGS sequence.
DR Proteomes; UP000610124; 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; 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 Pyruvate {ECO:0000313|EMBL:GGU93456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037395};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 61964 MW; DF71330ACD2890BB CRC64;
MARTVARVIV DALQELGVRH VFGVVGDALN PLTEAIRTTE GVDWIGCRHE EAAAFAAGAQ
SQLSGTLGVC MGTVGPGSVH LLNGLYDAAK SRTPLLAIAG QVPSAELGSD YFQEVDNDLL
FRDVAVFRAT VTSPDQLPRM LETAVRCAIS ERGVAVLTVP GDLGDRELTD DRPARFPRVR
PVTRADDAGI REAADLVNAA DRVTLLVGRG ARDARGEVLE LAERLSAPMV LTLKAKEGFE
ADNPYQVGQT GLIGNPAAAA ALDACDTLIM LGTDFPYRDW YPTGRKVVQI DLLERNLGRR
VPVDVGLAGD TAATLRALLP HLRPTADRAH LEAARERFEQ WTAGQRRLAD PEHDHHLLGR
LRSALDNRAH DVRPEALAAA VNDCASDDAV FTSDTGMATV WLSRFVTMHG RRRLLGSYNL
GSMANAMPQA LGAQLWAPDR QVVAFCGDGG LSMLLGDLMT IRTHRLPVKL VVFDNRRLGM
VKLEQEQAGL PEFGTELDNP DFAAVATALG LTGIRVTRPS ELLDGVRRAF ETPGPVVLDV
LTNPRELAVP GKPTVEQGWG FAIAKVKETL RSHDG
//
