ID A0A0N0XUA0_9ACTN Unreviewed; 891 AA.
AC A0A0N0XUA0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=ADL29_28795 {ECO:0000313|EMBL:KPC60598.1};
OS Streptomyces chattanoogensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC60598.1, ECO:0000313|Proteomes:UP000037982};
RN [1] {ECO:0000313|Proteomes:UP000037982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|PIRNR:PIRNR000156}.
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 ECO:0000256|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|PIRNR:PIRNR000156};
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:KPC60598.1}.
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DR EMBL; LGKG01000159; KPC60598.1; -; Genomic_DNA.
DR RefSeq; WP_053926482.1; NZ_LGKG01000159.1.
DR AlphaFoldDB; A0A0N0XUA0; -.
DR PATRIC; fig|66876.3.peg.6313; -.
DR Proteomes; UP000037982; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR035807; PDC_E1_N.
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; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:KPC60598.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037982};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 144..296
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 482..709
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 891 AA; 98073 MW; 4052120C56C1ACD7 CRC64;
MPEPVRLPYS QLDQLPDRDP EETAEWRASL DAVTRAAGPH RATYLMRRAL EHNGAPGLAP
LETDYVNTIP TSAEPAFPGD PAMEARITAW NRWNAAAMVT RGSRFGVGGH IATFASAAWL
YETGFNHFFR GKEGDGSGDQ LYIQGHASPG IYARAFLDGR LTEDHLDHFR QESGGKGLPS
YPHPRRLPWL WEFPTVSMGL GPLSAIYQAR FNRYLQGRGI KDTANSHVWA FLGDGEMDEP
ESTAALALAG REGLDNLTFV INCNLQRLDG PVRANFKIVQ ELESQFRAAG WNVVKSLWGS
AWDELFQLDT TGALVRRLRQ VPDAQFQTYA TRDVAYVREH FFGAEPALAE MAKVLTDAKI
AECFHTSRGG HEARKVYAAY KAAVGFKGAP TVILAQTVKG YTLGPGFESK NANHQMKKLS
GKEFRAMRDL LDLPIPDSRL DEDLVPYGHP GADSPEVRYL QERRAALGGP APARRLHASA
ALPQPEERAF KALHKGSGKQ EMATTMAFVR LAKDLMRDKE TGRRWVPIVP DEARTFGMES
LFPSAGIYSP KGQTYEPVDR DQLMYYKEAT DGQILNEGIT EAGAMADFIA AATSYATHGE
PMIPFYIFYS MFGWQRTADQ MWQLADQLGK GFIVGATAGR TTLTGEGLQH ADGHSHLIAS
TNPASLNYDP AFAYEIAVIV KDGLRRMYGE TAPGEDSNVF YYLTVYNEPK VQPAMPEGVE
EGILKGLYRF KEAAGATSET PRTQLLASGT AIHWALEAQE LLAADWGVAA DVWSATSWGE
LRRDALACDA ARLDGEDRIP YVTRALAGAP GPVVAVSDWM RAVPDQIAPW VEQDWVSIGT
DGFGLSDTRE AARRHFGVDA QSVVVQTLAA LARRGEVKPE TVKEARQRYG L
//
