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
//