ID A0A089YVP4_9PSED Unreviewed; 572 AA.
AC A0A089YVP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:AIS17805.1};
GN ORFNames=LT40_10545 {ECO:0000313|EMBL:AIS17805.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS17805.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS17805.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS17805.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP009533; AIS17805.1; -; Genomic_DNA.
DR RefSeq; WP_043189666.1; NZ_CP009533.1.
DR AlphaFoldDB; A0A089YVP4; -.
DR STRING; 216142.LT40_10545; -.
DR KEGG; prh:LT40_10545; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000029499; Chromosome.
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:AIS17805.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 572 AA; 62418 MW; AC90B83285AF8125 CRC64;
MASKKVADIV IQTLQEAGVR NCYGIVGDTL NHVTDAISRS EIEWVHVRHE EAAAFAAGAE
SFISGRLTAC AGSCGPGGLH FINGIFEAQR NSAPMVLIAS QIVTSELGMD FPQEVDFKAI
YGSCTVFCEQ VYTPEQARRV TTLAAQTALN EGGVAVIILP SDISSAEVKN DRPFSVHQPR
PVLQPSPDEL AGIADMLAQG KKIAIYAGFG CEGAHDELIE LAQRLKAPIA HTSRAKDFVE
YDNPYNMGMT GVFGVESGYH AMMECDTLLL LGADFAWGQF YPQNAKVIQV DRKGAHLGRR
HPIDLGVVGD VLPTLQALLP LVAERTEHSF LEDCLKVRQK TLKTLAHDQR HTDGHLIHPQ
YLTHLLDKHA TEDALFTADG GSPMVWILRH INTNGQRRTL TSLRHGTMAN AMPQALGLQK
AYPQRQVISL SGDGGLAMLM GDLLTAVQEK LPIKVVVFNN SSLNFVQIEQ KVEGLLDNFT
SLHNPDFAKL AEVMGFYGEQ VSDGASLERA VQRFLNHPGP ALLDVKVNPE ELVMPPKIEF
SQVSNMALYS AKAMLNGRAD DVAHMLVDNF IK
//
