ID Q7UU96_RHOBA Unreviewed; 910 AA.
AC Q7UU96;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 OrderedLocusNames=RB3424 {ECO:0000313|EMBL:CAD73186.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD73186.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD73186.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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};
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DR EMBL; BX294138; CAD73186.1; -; Genomic_DNA.
DR RefSeq; NP_865502.1; NC_005027.1.
DR RefSeq; WP_011119356.1; NC_005027.1.
DR AlphaFoldDB; Q7UU96; -.
DR STRING; 243090.RB3424; -.
DR EnsemblBacteria; CAD73186; CAD73186; RB3424.
DR KEGG; rba:RB3424; -.
DR PATRIC; fig|243090.15.peg.1580; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_0; -.
DR InParanoid; Q7UU96; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000001025; Chromosome.
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:CAD73186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 156..315
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..720
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..90
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 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 910 AA; 101493 MW; A8A04C003CD8D7F8 CRC64;
MSESKSVAQA EISQNLGELQ HSPDVDVDSA ETQEWISSLE YVLQSKGPER VKFLIDQLRD
RAAEEGVPLS SDTSTPYVNT IPPHEQPAYP GNRELERRIK SIIRWNAMAM VVRANKRPGG
VGGHISTFAS SATLYEVAFN HFFQGRGEDG YSGDSIYFQG HASPGMYSRA YLEGRLSDEN
LDNFRRELAP GGGLSSYPHP WLMPGFWEYP TVSMGLGPIM AIYQARFNEY LNDRGIKDTK
GQKVWAFLGD GECDEPETLG AIGLASREKL DNLIFVINCN LQRLDGPVRG NSKIIQELES
IFHGAGWNVI KVVWGGEWDE LLARDTTGLL AKRMNEVVDG QYQKYTSMPG SYIREHFFGK
YPELLELVKH LSDEKLEKIR RGGHDPEKVY AAYHRATTLN NGKPTVILAK TVKGYGLGEA
GEGRNVAHNQ KKMNEAELLE FRTRFGIPIS DEKVGEAPFY KPPANSTEIK YLKTRRETLG
GPVPSRPTEH PKLEIPALDV FQKFVAKRTD NKEVSTTFAA VQMLISMCRD KSIGKYVVPI
VPDESRTFGM EGMFKQFGIY AHAGQLYEPT DSDQVAYYKE AQDGQILEEG ITECGSMSSF
NAAGTAYSCH GVNMIPFYIY YSMFGFQRIG DSIWAAADMR AKGFLVGGTA GRTTLNGEGL
QHQDGHSLLN AIAFPTVRAY DPAFAYEVTV IVHEGLKRMY EEGEECLYYI TAENEAYVQP
EIPEGCEEGI IKGMYKFNSR EVDGAKARVQ LFGSGAILNS ALKAQEILAE KYNIASDVWS
VTSYTLLRRD AHSVERWNRL HPTETPRKSY LEEVLEGVEG PFISASDYVR ALGEQLTPWI
PGDYYVLGTD GMGRSETREA LRRHFEVDAE SITIAALGRL AKAGTFEAAD VAQAIKDLDY
DPDKVDPYFA
//
