GenomeNet

Database: UniProt
Entry: A4ALR4_9ACTN
LinkDB: A4ALR4_9ACTN
Original site: A4ALR4_9ACTN 
ID   A4ALR4_9ACTN            Unreviewed;       488 AA.
AC   A4ALR4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 81.
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=A20C1_03683 {ECO:0000313|EMBL:EAR23755.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR23755.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR23755.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR23755.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR23755.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAOB01000016; EAR23755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4ALR4; -.
DR   STRING; 312284.A20C1_03683; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_1_11; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000003868; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; 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; IPR014276; 2-oxoglutarate_DH_E2.
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; TIGR02927; SucB_Actino; 1.
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; 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 {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003868};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EAR23755.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          191..228
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          77..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  50353 MW;  0BA550EB9C27CEDE CRC64;
     MSESVNLPAL GESVTEGTVT RWLKQVGERV EVDEPLLEVS TDKVDTEIPS PVAGVIEEIL
     VAEDETVEVG TALVRIGDGS GGAEAAPTTD AEEAPAEAEA EPAAETAPAA EASAPAEAEP
     AEAEPEAASA AEKPAASEEP APAEAPAEAP AEQASEAPAA PAADQEAVQA PASTETNADD
     SDDDDDSQAG YLTPLVRKLA NERGVDLTTI TGTGVGGRIR KQDVLAASEA ASSTEETAAS
     SAQAAPREVS PLRGTTVPMS RLRKVIAERA VISMQSSAQL TSVVEVDVTA VANYRTSVKD
     EFLAKTGTKL SFLPFFALAA AEALTSNPII NATIEDNSIV YPAQENISIA VDTERGLLTP
     VIRDAASLDL AGLASQIADL AARTRDNKLT PDELSGGTFT LTNTGSRGAL FDTPIVFLPQ
     SAILGTGIVT KKPVVISDVN GDSIGIRSMV YLALSYDHRI VDGADAARFL VDVKNRLEGG
     DFADKLGI
//
DBGET integrated database retrieval system