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Database: UniProt
Entry: H0Q1G8_9RHOO
LinkDB: H0Q1G8_9RHOO
Original site: H0Q1G8_9RHOO 
ID   H0Q1G8_9RHOO            Unreviewed;       563 AA.
AC   H0Q1G8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=aceF {ECO:0000313|EMBL:BAL23768.1};
GN   ORFNames=AZKH_1446 {ECO:0000313|EMBL:BAL23768.1};
OS   Azoarcus sp. KH32C.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL23768.1, ECO:0000313|Proteomes:UP000007106};
RN   [1] {ECO:0000313|EMBL:BAL23768.1, ECO:0000313|Proteomes:UP000007106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH32C {ECO:0000313|EMBL:BAL23768.1,
RC   ECO:0000313|Proteomes:UP000007106};
RA   Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA   Senoo K.;
RT   "Complete genome sequence of Azoarcus sp. KH32C.";
RL   Submitted (NOV-2011) 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|ARBA:ARBA00011484,
CC       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; AP012304; BAL23768.1; -; Genomic_DNA.
DR   RefSeq; WP_015435075.1; NC_020516.1.
DR   AlphaFoldDB; H0Q1G8; -.
DR   STRING; 748247.AZKH_1446; -.
DR   KEGG; aza:AZKH_1446; -.
DR   PATRIC; fig|748247.4.peg.1408; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_4; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000007106; 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:BAL23768.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:BAL23768.1}.
FT   DOMAIN          4..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          121..195
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          258..295
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   563 AA;  57494 MW;  1111BD4B1050C8CB CRC64;
     MSQIIEVKVP DIGDFDAVPV IELFVKVGDT IKVDDAIATL ESDKATMDVP SSAAGVVKEV
     LVGVGDKVSE GVALIKVETA NGAKAEAPAA APAPAAAPAP AAAAPAPASA PAAAPAAAAG
     PVEVAVPDIG DFSEVPVIEL FVKVGDTIKV DDAIATLESD KATMDVPSSA AGVVKEVKVK
     VGDKVSMGTV LIVVEGAGAA PAAAAAPAPA AAPAPASTPS GAVPAASTAA FSQSALSAPP
     QGAAPAAPSA VTLGGKVHAS PSVRAYSREL GVDLAQVKAT GPKARILKED VTAFVKGAMQ
     TGVVPGKAAP AAAGASLGGG LDLLPWPKVD FSKFGEIESK PLSRIKKISG QNLARNWVMI
     PAVTYHEDAD ITDLEAFRVQ MNKEYEKSGK KLTMLAFIIK ASVRALQQFP EFNTSLDGDN
     LIYKKYFNIA FAADTPNGLV VPVIKNADKK SVFEIAAESG ELAKKARDGK LGPADMSGAC
     FTISSLGGIG GTYFAPIVNA PEVAILGVNK SVMKPVWDGK QFVPRLTLPM SLTADHRVID
     GALATRFNVY LAQLLADFRR VML
//
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