ID A0A0R0MFQ2_9BURK Unreviewed; 907 AA.
AC A0A0R0MFQ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=aceE {ECO:0000313|EMBL:KRI00733.1};
GN ORFNames=AO057_12780 {ECO:0000313|EMBL:KRI00733.1};
OS Curvibacter sp. PAE-UM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRI00733.1, ECO:0000313|Proteomes:UP000051912};
RN [1] {ECO:0000313|EMBL:KRI00733.1, ECO:0000313|Proteomes:UP000051912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAE-UM {ECO:0000313|EMBL:KRI00733.1,
RC ECO:0000313|Proteomes:UP000051912};
RA Ma D.;
RT "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT river sediment.";
RL Submitted (SEP-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|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};
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:KRI00733.1}.
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DR EMBL; LKCX01000017; KRI00733.1; -; Genomic_DNA.
DR RefSeq; WP_057676309.1; NZ_KQ483358.1.
DR AlphaFoldDB; A0A0R0MFQ2; -.
DR STRING; 1714344.AO057_12780; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000051912; 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; 2.
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:KRI00733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051912};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 115..310
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 376..441
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 503..715
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 907 AA; 101469 MW; CE49C132A1E2D08F CRC64;
MSALPQNLSG IEAQDIDSQE TLEWKHALEA VIAQEGPERA HFLLEQLLEH AREHSIDLPF
SATTGYTNTI EPDQEAHSPG NLDLEGRLRA YMRWNAMAMV VKANRLDPAD GGDLGGHISS
FQSLAHMFAA GFNHFWHADN TDEGGTHGGD LLYIQGHSSP GIYARAFLEG RISEEQMLNF
RQEVDGKGLS SYPHPKLMPG FWQFPTVSMG LGPIMSIYQA RFLKYLHARG LADTSQRKVW
VFCGDGEMDE PESLGAIGLA AREKLDNLVF VVNCNLQRLD GPVRGNGKII QELEGEFRGA
GWNVIKLIWG KEWDGLLARD KDGALRKIMM DTLDGDYQAF KANDGAFVRK NFFGRDPRTL
EMVSKMSDQE VWGLRRGGHD AQKVYAAFHK AHNSQGGPTV LLVKTVKGWG MGKAGEGKNT
AHQTKKLGDD DIRYMRDRFN IPIPDSELPK IPFYKPADDT PEMKYLHERR QALGGYLPKR
RTVSSESFTV PSLETFKSVL EPTAEGREIS TTQAYVRFLT QLLRDQALGP RVVPILVDEA
RTFGMEGLFR QIGIYNPEGQ KYTPVDKDQV MYYKEDKAGQ ILQEGINEAG GICSWIAAAT
SYSTNNRIMI PFYIYYSMFG LQRVGDLAWA AGDMQARGFL LGGTSGRTTL NGEGLQHEDG
HSQVLASTIP NCVSYDPTFA HEVGIILHHG LKRMVEKQDN VFFYLTLLNE NYAMPGLKAG
TEEQIIKGMY LLQEAKAGKK TPQVNLLGSG TILRESMFAK ELLEKDWGVT ANVWSCPSFN
ELARDGQDVE RWNLLHPTAK QRVAFVTQQL EPHAGPVIAS TDYVKTFSEQ IRPYIPKGRT
YKVLGTDGFG RSDFRSKLRE HFEVNRHYIV VAALRSLVEE GTVPMEKVAE AIAKYKIKTD
KVNPLYA
//
