ID K9F3G6_9ACTO Unreviewed; 917 AA.
AC K9F3G6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HMPREF9233_00088 {ECO:0000313|EMBL:EKU96000.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU96000.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU96000.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) 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:EKU96000.1}.
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DR EMBL; AGWL01000001; EKU96000.1; -; Genomic_DNA.
DR RefSeq; WP_007000306.1; NZ_JH992955.1.
DR AlphaFoldDB; K9F3G6; -.
DR STRING; 202789.GCA_001457435_00159; -.
DR PATRIC; fig|883066.3.peg.91; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_11; -.
DR Proteomes; UP000009888; 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:EKU96000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 149..309
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 496..721
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
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"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 917 AA; 102377 MW; 7926C3886B5629A8 CRC64;
MSEQPHSAHL VNGQLSQIPD SDPEETREWL DSVGDLIETN GTDRARFVLN SMEEYARGKG
VGISPELSTP YINTIPASAE PEYPGDEEIE RQFRMWTRWN AAVMVTRAQR PGVGVGGHIS
SYAAQATLYE VGLNHFFRGP DAPGGGDQVY FQGHSSPGNY SRAYLEGRLT EADLDNFRQE
ASRPSGGRGL PSYPHPHQMP DFWQFPSVSL GIGPANSIYQ AWFNRYLAER GIQDTSDQHV
WAFIGDGEMD EPESRGMLQL AAYQKLDNLT WVINCNLQRL DGPVRGNGSI VQELEAFFKG
AGWNVIKVLW GREWDPLLAN DQDHALVDLM SSTLDGDYQG YKANDGAYVR NNFFGRDPRT
KALVQDMSDD QIWALRRGGH DPRKIYAAYR NALATKGQPT VILAQTVKGY DLGTSFAGRN
SNHQMKKLNS ADLKLLRDTT GVPIEDSQLE NPYEAPYYKP PEDHPAMQYM REHRNQLGGY
IPQRRIFEGG IEMPKEKPFE SMKKGSGKQK VATTMALVRL LKDLVRDKKF GYRLVPIVPD
EARTFGMDSM FPSQKIFNTL GQNYTAVDHD MLLSYKESTQ GQLLHTGITE AGSVAAYTAA
ATSYAIHNQP MIPFYIFYSM FGFQRTGDQL WAATDALARG FIVGATAGRT TLTGEGSQHM
DGHSPVIAST NPGVIHYDPA YAYEIGHIFK DGIVRMYGDG SDGRNQNVQY YLTVYNEPIH
QPAEPENVDV DGIIKGIYKL DEADGQGGPR VNLLASGVGV PWAREAKKML RRDWGVDATV
WSVTSWYELR RDGMETNEYN YLHPTEAPRE AYVTAKLKNE QGPFIATSDF EHQVQDSIRE
WVPGRYETLG ADGIGISDTR PAARRYFKID DATMVVRALH ALALEGQMDA SVVQEAIDKY
DINNPQAAEP VPDNDPE
//
