ID A0A0Q5BBB5_9MICO Unreviewed; 583 AA.
AC A0A0Q5BBB5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KQQ09973.1};
GN ORFNames=ASF46_02380 {ECO:0000313|EMBL:KQQ09973.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ09973.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ09973.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ09973.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ09973.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ09973.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQQ09973.1}.
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DR EMBL; LMNR01000001; KQQ09973.1; -; Genomic_DNA.
DR RefSeq; WP_056866265.1; NZ_LMNR01000001.1.
DR AlphaFoldDB; A0A0Q5BBB5; -.
DR STRING; 1736327.ASF46_02380; -.
DR Proteomes; UP000050868; 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:KQQ09973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 583 AA; 61050 MW; C5CEA52C1FECF6F7 CRC64;
MAQKTVADQL IAQLIDAGVS RIYGIVGDSL NPIVDAVRRS GGSAKGGIDW IHVRNEEAAA
FAAGAEAQLT GRLAVCAGSC GPGNLHLING LYDAHRSGAP VLAIASHIPG NEIGSSYFQE
THPDRLFVEC SNYRELVSTA AQAPRVVNAA MRSAVALGGV AVVTLPGDVA EFEAVGEFPA
FVLPAPAVLV PDDGDVRALA AAIDSAKTVA IFAGAGVRNA HDEVVAFAEL VGAPVGHSLR
GKEWIQYDNP YDVGMTGLLG YGAAHAGIHD ADLLILLGTD FPYEQFLPDA SEVVIAQVDT
DASKLGRRVS VAHPVHGDVG ATLRALTPLV QRKSHRFLEK TLKKHEKLVT GVVGKYTEVE
KRRPIHPELV ASTLDGLLSE DAIVTADTGM GNVWQARYIT PNGRRRLIGS YLHGSMANAL
PQAVGAQLSH PGRQVVSLSG DGGLSMLMGE LVTVAAYRLP VTIVVFNNST LGLVKVEMLV
DGFPDFAVDV PMVDYAKVAE AIGIRGIRVE DPKDVEGALR EALAQDGPVL VDVVTDPLAL
SLPPTITGAQ VKGFALAMSK IVMNGGTGEA IALARSNVKH ALP
//
