ID A0A263DJ07_9PSEU Unreviewed; 767 AA.
AC A0A263DJ07;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172};
GN ORFNames=CFP66_32595 {ECO:0000313|EMBL:OZM78171.1};
OS Pseudonocardia sp. MH-G8.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM78171.1, ECO:0000313|Proteomes:UP000216936};
RN [1] {ECO:0000313|EMBL:OZM78171.1, ECO:0000313|Proteomes:UP000216936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-G8 {ECO:0000313|EMBL:OZM78171.1,
RC ECO:0000313|Proteomes:UP000216936};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Non-contiguous finished genome sequence and description of Pseudonocardia
RT marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT phycosphere.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:OZM78171.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKYF01000020; OZM78171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263DJ07; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000216936; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR004660; PDH_E1.
DR InterPro; IPR041621; PDH_E1_M.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF4; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 2.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Pyruvate {ECO:0000313|EMBL:OZM78171.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216936}.
FT DOMAIN 403..607
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 767 AA; 81773 MW; 5AD968271E1D547A CRC64;
MSTRPTESDA LAVLREVEQR VLWLSAAVVH HANRVRPNTT GLKVGGHQAS SASMVTIMTA
LWFEHLRAGD RVSVKPHASP VLHAINYLLG ELDQRYLTTL REFGGLQSYP SRSKDPDPVD
YSTGSVGIGA TAPIWGALAR RYVDAKGAGT GAGRQYSLVG DAELDEGAVW EAVLDPMVAE
LGELVWIVDV NRQSLDRVVP NIGVTRLQGM FAAAGWQVLT VKYGRVLQEL FERPGGDALR
RRIDEMTNPE YQRLLRCSPE QLRERLPAGD AALQRLVAGL DDDTLHTCVR NLGGHDLDAL
GEAFGAIDDT RPTVVFAYTV KGYGLASEGH PQNHSSLLTD EQFGELAARV GAAVDAPWER
FAPGSAPARL CAAVAERLRR DPVVPTPVPE IPADIGRTPS GTATTQAALG RALLDLTRSA
PEAAARVVTL CPDVSSSTNL GGWVNKVGVW SAAERPDWFD DDPETILHWR ERPEGQHVEL
GIAETNLVGL LGELGATWSR WGEPLLPIGV LYDPFVERAL EPWSFGIYAG GQSILVGTPS
GVTLAPEGGA HQSITTPSVG LEQPGCTSYE PAFAIDVEWT LLAALARLGR PDGTSAYLRL
STRPVDQSLA AVPGDPAARE RRRRQVVAGA YPLVRASGTP AVTVAAMGAC VPEALAAAAR
LEALGHPADV VCVTSPGLLF EAVQARAGQG SSESWVLDAA FPARRAAPMV TLLDGHPHTL
AFLAGIHRVR AAHLGVTRFG QSGDLDAVQS HHGLDADTVV RAALDLM
//
