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Database: UniProt
Entry: A0A2Z3GXA4_9BACT
LinkDB: A0A2Z3GXA4_9BACT
Original site: A0A2Z3GXA4_9BACT 
ID   A0A2Z3GXA4_9BACT        Unreviewed;       551 AA.
AC   A0A2Z3GXA4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=C1280_09750 {ECO:0000313|EMBL:AWM37281.1};
OS   Gemmata obscuriglobus.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=114 {ECO:0000313|EMBL:AWM37281.1, ECO:0000313|Proteomes:UP000245802};
RN   [1] {ECO:0000313|EMBL:AWM37281.1, ECO:0000313|Proteomes:UP000245802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5831 {ECO:0000313|EMBL:AWM37281.1,
RC   ECO:0000313|Proteomes:UP000245802};
RA   Franke J., Blomberg W., Selmecki A.;
RT   "G. obscuriglobus.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP025958; AWM37281.1; -; Genomic_DNA.
DR   RefSeq; WP_010046355.1; NZ_CP042911.1.
DR   AlphaFoldDB; A0A2Z3GXA4; -.
DR   KEGG; gog:C1280_09750; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000245802; Chromosome.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; 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; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:AWM37281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245802};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..75
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          115..190
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          243..280
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          73..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  56869 MW;  3D1CCE3E66DE608A CRC64;
     MDFHLPNLGE GIEGGTITSV LVKPGDTVTT GQPVMSVETD KASMEVNAES DGTVDAVLVK
     PGDKVSIGAP LLKLGGGQKA EPKAEAKPAA KAAAEAKPEP PPKAAPAPAP SSGAATAFAL
     PALGEGIEGG TITAVFVKAG DAVKAGQNVV AIETDKAAME VAAEADGTVE AVHVKPGDKV
     SIGGPLLTLN GGAAPQPQPK ASAPTPQPPA TKQPATEQAK PQPQPTHAAS ANGSNGATKA
     IIPAGPATRK LARELGVALA EVKGTARGGR VTLDDLKGFV KGERTRAKES GSAGGALAAD
     AVVVNKYALP PLPDFSKYGA VEVADVATIR QTIAKNLTAG WRTMPMVTQH ELADITDLEA
     GRKRFVDQLP KGASKITMTV LAIKACVAAL KEFPRFNSSY DMNAGKLILK KYFHIGIAVD
     TERGLVVPVI RDADKKSIRD LAAEVSALAV KARDNKLSID EMRGGTFTIT NLGGIGGTAF
     TPIVNYPEVA ILGLSKSAMQ PIVKDGQIVA RLMMPLSLTY DHRVIDGADG CRFTVRLAQL
     FSDPLRLLME T
//
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