ODP2_AZOVI
ID ODP2_AZOVI Reviewed; 638 AA.
AC P10802;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE AltName: Full=E2;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX PubMed=3292237; DOI=10.1111/j.1432-1033.1988.tb14140.x;
RA Hanemaaijer R., Janssen A., de Kok A., Veeger C.;
RT "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase
RT complex from Azotobacter vinelandii. Molecular cloning and sequence
RT analysis.";
RL Eur. J. Biochem. 174:593-599(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-16 AND 381-416.
RX PubMed=3691494; DOI=10.1111/j.1432-1033.1987.tb13604.x;
RA Hanemaaijer R., de Kok A., Jolles J., Veeger C.;
RT "The domain structure of the dihydrolipoyl transacetylase component of the
RT pyruvate dehydrogenase complex from Azotobacter vinelandii.";
RL Eur. J. Biochem. 169:245-252(1987).
RN [3]
RP LIPOYL DOMAIN CONFORMATION.
RX PubMed=3191993; DOI=10.1016/0014-5793(88)80369-7;
RA Hanemaaijer R., Vervoort J., Westphal A.H., de Kok A., Veeger C.;
RT "Mobile sequences in the pyruvate dehydrogenase complex, the E2 component,
RT the catalytic domain and the 2-oxoglutarate dehydrogenase complex of
RT Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy.";
RL FEBS Lett. 240:205-210(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 382-638.
RX PubMed=1549782; DOI=10.1126/science.1549782;
RA Mattevi A., Obmolova G., Schulze E., Kalk K.H., Westphal A.H., de Kok A.,
RA Hol W.G.J.;
RT "Atomic structure of the cubic core of the pyruvate dehydrogenase
RT multienzyme complex.";
RL Science 255:1544-1550(1992).
RN [5]
RP STRUCTURE BY NMR OF 1-79.
RX PubMed=8068086; DOI=10.1111/j.1432-1033.1994.tb18717.x;
RA Berg A., de Kok A., Vervoort J.;
RT "Sequential 1H and 15N nuclear magnetic resonance assignments and secondary
RT structure of the N-terminal lipoyl domain of the dihydrolipoyl
RT transacetylase component of the pyruvate dehydrogenase complex from
RT Azotobacter vinelandii.";
RL Eur. J. Biochem. 221:87-100(1994).
RN [6]
RP STRUCTURE BY NMR OF 1-79.
RX PubMed=9119000; DOI=10.1111/j.1432-1033.1997.00352.x;
RA Berg A., Vervoort J., de Kok A.;
RT "Three-dimensional structure in solution of the N-terminal lipoyl domain of
RT the pyruvate dehydrogenase complex from Azotobacter vinelandii.";
RL Eur. J. Biochem. 244:352-360(1997).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 3 lipoyl cofactors covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X12455; CAA30987.1; ALT_INIT; Genomic_DNA.
DR PIR; S01017; XXAV.
DR PDB; 1DPB; X-ray; 2.50 A; A=396-638.
DR PDB; 1DPC; X-ray; 2.60 A; A=396-638.
DR PDB; 1DPD; X-ray; 2.70 A; A=396-638.
DR PDB; 1EAA; X-ray; 2.60 A; A=396-638.
DR PDB; 1EAB; X-ray; 2.60 A; A=396-638.
DR PDB; 1EAC; X-ray; 2.60 A; A=396-638.
DR PDB; 1EAD; X-ray; 2.60 A; A=396-638.
DR PDB; 1EAE; X-ray; 2.60 A; A=396-638.
DR PDB; 1EAF; X-ray; 2.60 A; A=396-638.
DR PDB; 1IYU; NMR; -; A=2-79.
DR PDB; 1IYV; NMR; -; A=2-79.
DR PDBsum; 1DPB; -.
DR PDBsum; 1DPC; -.
DR PDBsum; 1DPD; -.
DR PDBsum; 1EAA; -.
DR PDBsum; 1EAB; -.
DR PDBsum; 1EAC; -.
DR PDBsum; 1EAD; -.
DR PDBsum; 1EAE; -.
DR PDBsum; 1EAF; -.
DR PDBsum; 1IYU; -.
DR PDBsum; 1IYV; -.
DR AlphaFoldDB; P10802; -.
DR SMR; P10802; -.
DR DrugBank; DB08120; 6,8-DIMERCAPTO-OCTANOIC ACID AMIDE.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB01846; Oxidized coenzyme A.
DR PRIDE; P10802; -.
DR EvolutionaryTrace; P10802; -.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178:SF2; PTHR43178:SF2; 4.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 3.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Glycolysis;
KW Lipoyl; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3691494"
FT CHAIN 2..638
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162272"
FT DOMAIN 2..74
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 117..191
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 222..296
FT /note="Lipoyl-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 338..375
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 90..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..638
FT /note="Catalytic"
FT ACT_SITE 611
FT /evidence="ECO:0000255"
FT MOD_RES 40
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 157
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 262
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1IYU"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1IYU"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 417..432
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 455..460
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 468..481
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1EAA"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:1DPB"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 587..592
FT /evidence="ECO:0007829|PDB:1DPB"
FT STRAND 594..610
FT /evidence="ECO:0007829|PDB:1DPB"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 616..631
FT /evidence="ECO:0007829|PDB:1DPB"
FT HELIX 633..637
FT /evidence="ECO:0007829|PDB:1DPB"
SQ SEQUENCE 638 AA; 65045 MW; 8B92CB5ADEA0BEA1 CRC64;
MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA GVVKSVSVKL
GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA EAPSPGASAT PAPAAASQEV
RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL IVLESDKASM EIPSPASGVV ESVAIQLNAE
VGTGDLILTL RTTGAQAQPT APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE
VLVKAGDQVQ AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA
APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF GVELAAINST
GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP PVDFAKYGEI EEVPMTRLMQ
IGATNLHRSW LNVPHVTQFE SADITELEAF RVAQKAVAEK AGVKLTVLPL LLKACAYLLK
ELPDFNSSLA PSGQALIRKK YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK
ARSKKLGADA MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR
LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL
