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Database: UniProt
Entry: B8J6I7_ANAD2
LinkDB: B8J6I7_ANAD2
Original site: B8J6I7_ANAD2 
ID   B8J6I7_ANAD2            Unreviewed;       552 AA.
AC   B8J6I7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   OrderedLocusNames=A2cp1_1826 {ECO:0000313|EMBL:ACL65168.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL65168.1, ECO:0000313|Proteomes:UP000007089};
RN   [1] {ECO:0000313|EMBL:ACL65168.1, ECO:0000313|Proteomes:UP000007089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|ARBA:ARBA00025211}.
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         Evidence={ECO:0000256|ARBA:ARBA00000925,
CC         ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP001359; ACL65168.1; -; Genomic_DNA.
DR   RefSeq; WP_012633090.1; NC_011891.1.
DR   AlphaFoldDB; B8J6I7; -.
DR   KEGG; acp:A2cp1_1826; -.
DR   HOGENOM; CLU_016733_10_0_7; -.
DR   OMA; HPCIMAP; -.
DR   Proteomes; UP000007089; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; 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   NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:ACL65168.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:ACL65168.1}.
FT   DOMAIN          3..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          130..204
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          256..293
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          84..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..122
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..244
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  57234 MW;  6953F3DABE95ED07 CRC64;
     MRTIEVKVPN IGDYKDVPVI DVLVKPGEQV DADAPLVTLE SDKATLDVPA PAAGTIREVK
     VKVGDRVSEG SLVVTLEASD GQAKAEAPAA PAQAAPPKPA AAAPAPAPSP APAAPSAPPA
     AASPAGAPRT VEVKVPNIGD FKDVPVIEVL VKPGDRVEAD APLATLESEK ATLDVPAPAA
     GTIREVALKA GDKVSEGSLV AILDAVAPAA ATTAAAPAPS QPAAAPAAKA AAPPPAPSPA
     APPVAPETGA QGQVPHASPS VRKLARELGV NLGRVEGSGP RGRILQDDVQ KFVKASLARL
     ESGGGGGGAL DLAPWPKVDF TRFGPVERQP LSRIRKLSRT NLARNWVMIP HVTQFDEADI
     TELERFRVEL NREHEKQGVK VTLLAFLVKA CVAAMRRFPE LNASLDGDEL VLKRYFHVGF
     AADTPQGLVV PVLKDADQKG VLQLAKELGE LAAKARDGKL SPADVQGGCF SISSLGGIGG
     TAFTPIINAP EVAILGVSRS AMRPVWDGTQ FQPRLMLPLS LSYDHRVIDG ALAARITTYL
     AQLLGDMRRI VL
//
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