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   27-MAR-2024, 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;
GN   Name=pdhC; Synonyms=pdhB; OrderedLocusNames=ZMO0510;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; 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 /
RC   NCIMB 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=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
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   KEGG; zmo:ZMO0510; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_5; -.
DR   Proteomes; UP000001173; Chromosome.
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   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; 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
//