ID W0RGK7_9BACT Unreviewed; 326 AA.
AC W0RGK7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138, ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU364074};
GN ORFNames=J421_2667 {ECO:0000313|EMBL:AHG90204.1};
OS Gemmatirosa kalamazoonensis.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG90204.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG90204.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG90204.1,
RC ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO2.
CC {ECO:0000256|RuleBase:RU364074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
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DR EMBL; CP007128; AHG90204.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RGK7; -.
DR STRING; 861299.J421_2667; -.
DR KEGG; gba:J421_2667; -.
DR PATRIC; fig|861299.3.peg.2715; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_0; -.
DR InParanoid; W0RGK7; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000019151; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35891 MW; A3F50455C7498125 CRC64;
MPVITYRDAL NQALREEMQR DDRVFIMGEE VGVYQGAYKV SKGLLQDFGE MRVVDTPITE
LGFAGVGVGA AMVGLRPVIE FMTWNFALLA LDQVVNAAAK MLYMSGGQYN IPIVFRGPNG
AALQLSAQHS QAWESWLAHI PGLKVVAPGT PYDAKGLLKS AIRDDNPVCM LEGEMLYNTK
GEVPEEEYVI PIGKAELKRE GDHATIVTWG KMALVAVNAA DQLAKEGIRV DVVDLRTVRP
MDTEAIYESV RKTNRCVVLE EGWPHSGVGA QVTDSVQREC FDHLDAPVIR VHQEDVPMPY
AKNLEKAAKP DAPKTIAAIK KVLYLE
//
