ODP2_ZYMMO
ID ODP2_ZYMMO Reviewed; 440 AA.
AC O66119; Q5NQ71;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
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;
GN Name=pdhC; Synonyms=pdhB; OrderedLocusNames=ZMO0510;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=9515924; DOI=10.1128/jb.180.6.1540-1548.1998;
RA Neveling U., Klasen R., Bringer-Meyer S., Sahm H.;
RT "Purification of the pyruvate dehydrogenase multienzyme complex of
RT Zymomonas mobilis and identification and sequence analysis of the
RT corresponding genes.";
RL J. Bacteriol. 180:1540-1548(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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) (By similarity). {ECO:0000250}.
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 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X93605; CAA63808.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89134.1; -; Genomic_DNA.
DR RefSeq; WP_011240414.1; NZ_CP035711.1.
DR AlphaFoldDB; O66119; -.
DR SMR; O66119; -.
DR STRING; 264203.ZMO0510; -.
DR EnsemblBacteria; AAV89134; AAV89134; ZMO0510.
DR GeneID; 58026345; -.
DR KEGG; zmo:ZMO0510; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_5; -.
DR OMA; VPHYHLS; -.
DR OrthoDB; 1626282at2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Transferase.
FT CHAIN 1..440
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162296"
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 149..186
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT CONFLICT 169
FT /note="N -> S (in Ref. 1; CAA63808)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..188
FT /note="IAE -> VTG (in Ref. 1; CAA63808)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> V (in Ref. 1; CAA63808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 46833 MW; 6BC8A592FC0AF6B3 CRC64;
MSIEVKMPAL SPTMTEGTLA KWLVKEGDAV KAGDILAEIE TDKAIMEFET VDAGIIAKIL
VPEGSENIAV GQVIAVMAEA GEDVSQVAAS ASSQISEPSE KADVAQKETA DSETISIDAS
LDKAISNAGY GNKTENMTAS YQEKAGRIKA SPLAKRLAKK NHVDLKQVNG SGPHGRIIKA
DIEAFIAEAN QASSNPSVST PEASGKITHD TPHNSIKLSN MRRVIARRLT ESKQNIPHIY
LTVDVQMDAL LKLRSELNES LAVQNIKISV NDMLIKAQAL ALKATPNVNV AFDGDQMLQF
SQADISVAVS VEGGLITPIL KQADTKSLSA LSVEMKELIA RAREGRLQPQ EYQGGTSSIS
NMGMFGIKQF NAVINPPQAS ILAIGSGERR PWVIDDAITI ATVATITGSF DHRVIDGADA
AAFMSAFKHL VEKPLGILAQ
