ID M7MTN8_9MICC Unreviewed; 913 AA.
AC M7MTN8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=ADIAG_02306 {ECO:0000313|EMBL:EMQ98290.1};
OS Paeniglutamicibacter gangotriensis Lz1y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paeniglutamicibacter.
OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ98290.1, ECO:0000313|Proteomes:UP000012015};
RN [1] {ECO:0000313|EMBL:EMQ98290.1, ECO:0000313|Proteomes:UP000012015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ98290.1,
RC ECO:0000313|Proteomes:UP000012015};
RX PubMed=23766407;
RA Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT Station Dakshin Gangotri.";
RL Genome Announc. 1:e00347-e00313(2013).
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:EMQ98290.1}.
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DR EMBL; AOCK01000006; EMQ98290.1; -; Genomic_DNA.
DR AlphaFoldDB; M7MTN8; -.
DR STRING; 1276920.ADIAG_02306; -.
DR PATRIC; fig|1276920.7.peg.2312; -.
DR eggNOG; COG2609; Bacteria.
DR Proteomes; UP000012015; 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}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 149..311
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..719
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 913 AA; 101573 MW; 5D97DCC8D729210A CRC64;
MAVEEHISHI RSGLTSQLPD RDPEETAEWI ESFDDLVETQ GTERAQYIVR SLLQRAGAKS
VGVPMVTTTD YVNTIPVDQE PEFPGDEQIE RRYRAFMRWN AAVMVHRGQR PGVGVGGHIS
TYAGAATLYE VGFNHFFRGK EHSGGGDQVF FQGHASPGMY ARAFLEGRLS EEDLDGFRQE
KSREGHALPS YPHPHSLPDF WEFPTVSMGI GPMNAIYQAQ SNRYLQNRGI KDTSDQQVWA
FLGDGEMDEP ESRGLLQLAA NEKLDNLTFV VNCNLQRLDG PVRGNGKIMQ ELEAFFRGAG
WNVIKVVWGR EWDALLDKDE DNSLVDIMNQ TPDGDYQTYK AENGAFVREH FFGKSPQTKE
MVADLTDEQI WNLKRGGHDY HKVYAAYKAA TEFKGKPTVI LTKTVKGYGL GPHFEARNAT
HQMKKMTLED LKAFRDHLRI PITDEQLEAD PYMPPYYRPE QDSAEYKYMM ERRNELGGSV
PSRRNKSKEI HLPEDKAYET ASRGSGKQQA ATTMAFVRLL KDLMRDKEFG KRVVPIVPDE
SRTFGMDAFF PTAKIYNPAG QNYLSVDREL VLAYKESPAG QLIHPGINEA GAVAAFTAAG
TSYSTHDEPL IPIYVFYSMF GFQRTGDAFW AAGDQMTRGF IMGATAGRTT LTGEGLQHAD
GHSPILASTN PAVITYDPAY GYEIGHIVKA GLERMYGGKH EDPNVMYYIT IYNEPYQQPK
EPEDLDVPGI LGGIYQVSPA TIDGPRAQLL ASGVAVPWTI EAQRMLAEDW GVSADVWSVT
SWNELRRDGL ACEEQSFLDP TAEPRIPFVA QQLAGATGPI VAVSDYMKAV PDQIRQFVPN
EFATLGADGF GFSDTREAAR RFFKIDAHSV VVRTLQMLAK RGEVDASAPA AAFAKYKLDD
VTAEATAIAG ADA
//
