ID A0A0R0D4I6_9GAMM Unreviewed; 572 AA.
AC A0A0R0D4I6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KRG77037.1};
GN ORFNames=ABB28_01270 {ECO:0000313|EMBL:KRG77037.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG77037.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG77037.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG77037.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG77037.1}.
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DR EMBL; LDJK01000005; KRG77037.1; -; Genomic_DNA.
DR RefSeq; WP_057506889.1; NZ_LDJK01000005.1.
DR AlphaFoldDB; A0A0R0D4I6; -.
DR PATRIC; fig|517011.3.peg.2015; -.
DR Proteomes; UP000051386; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:KRG77037.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051386};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 572 AA; 61856 MW; 2FCC0A667DD90DA2 CRC64;
MSKRVADIVV ETLQQAGVRR CYGIVGDTLN HVTTAIHGSD IDWVHVRHEE VAAFAAGADS
LISGQLTACA GSCGPGSLHF INGVFENNRN KAPMVLIASQ VVTSELGMEF PQEVDFKAVY
SSCSVFCEQV YSAEQARRVV TLACQAAISR RGVAVVILPS DISEQVVKHD PPFAVHYTQP
VLRPGDDELL RIAELLGQGK RIGIYAGAGC QGAHAPLLEL ARRLQAPIAH TSRAKDFVEP
DNPFNMGMTG IFGIESGFHA VMECDTLLLL GADFAWGQYY PDKATIIQVD HDGSHLGRRH
PVTLGVVGDI GPTLEALLPM LPPREDTDFL DECIGHREKA LAKRAEEEAP GEGELIHPQY
LTALLDQHAA DDALFTADCG SPMVWVLRHI RVNGRRRTLT SLLHGTMANA MPQALGLQKA
FPGRQVVALC GDGGLSMLMG DLLTAVQENL PIKIVVYNNG SLNFVELEQK VEGLLDYYTE
LKNPDFGKLA EVIGFHGRTV TRSQDLALAV QDLLAQPGPA LLDVHTAPTE LVMPPQVEAG
QVIGTARYMA KAVLAGRIGE VKELLADNFL KR
//
