ID A0A1I0XIE3_9RHOB Unreviewed; 885 AA.
AC A0A1I0XIE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05421688_2215 {ECO:0000313|EMBL:SFA99723.1};
OS Poseidonocella pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871651 {ECO:0000313|EMBL:SFA99723.1, ECO:0000313|Proteomes:UP000198796};
RN [1] {ECO:0000313|EMBL:SFA99723.1, ECO:0000313|Proteomes:UP000198796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29316 {ECO:0000313|EMBL:SFA99723.1,
RC ECO:0000313|Proteomes:UP000198796};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00003157, 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};
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DR EMBL; FOJU01000003; SFA99723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XIE3; -.
DR STRING; 871651.SAMN05421688_2215; -.
DR OrthoDB; 9773339at2; -.
DR Proteomes; UP000198796; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SFA99723.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198796};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 199..290
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 470..696
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 885 AA; 99635 MW; 2B3DF7E3FBC2A97D CRC64;
MTDTPEDIDP IESQEWQDAI EDVIQRDGAN RAHFLLDKAV QQARANGATL PFSATTPYLN
TIPPDDEFDF PGDYEMEGRI RAITRWNAMA TVVRRNKESS EYGGHIASFA SSAALYDVGL
NHFWRSKSAI HGGDLVFFQG HVVPGIYARS FMEGRISQET LEKFRSEVDG GGLSSYPHPW
LMPDYWQFPT VSMGLGPLMA IYQARFMKYL HNRGLIDAAD RKVWVFLGDG EMDEPESLGA
ISLAAREKLD NLIFVINCNL QRLDGPVRGN GKIVQELEGE FRGAGWDVIK LLWGRGWDDL
LEKDTSGMLR KLMDETVDGD YQTYKSKDGG FIREHFFGRY PETAALVEDW SDEEIWNLRR
GGHDTRKVYT AFKRASESKG QPTCLLVKTV KGYGMGTAGE GQNTTHQQKK MHEDQLRAMR
DRFQIPVSDE DLPKAPFVTL NNAQKAYLAE RRKELGGEFP KRHWRDAPKL EIPALEKFKG
QLESTGDREI STTMAFVRIL TTLLRDKAVG KHVVPIVPDE SRTFGMEGLF RSVGIYNPLG
QKYTPEDKDQ MMYYKESESG QVLQEGINEA GAMADWIAAA TSYSTHGVPM IPFFIYYSMF
GFQRIGDLAW AAGDSRARGF MLGGTAGRTT LNGEGLQHED GHSHILASTI PNCISYDPTF
SYEVAVIVQH GLKRMYQDQE DVYFYLTLMN ENYQHPEMPM GAEEGIIRGL YRMRKTSRPG
KKHVNLMGSG TILVQAIKAA EMLKEDFGVT ADIWSATSFN ELARDCQDTA RWNRLNPLAE
PRTSYLYQTL QGAKGPFIAA TDYMKNFAEQ VRSCVPGRYT VLGTDGYGRS DSRVNLRRFF
EVDANHIAAA AMVDLHREGA VSDKDLKAAL VKYDIDGDKP NPRLV
//
