ID A0A2T0LWU5_9PSEU Unreviewed; 636 AA.
AC A0A2T0LWU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=B0I33_104307 {ECO:0000313|EMBL:PRX48490.1};
OS Prauserella shujinwangii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=1453103 {ECO:0000313|EMBL:PRX48490.1, ECO:0000313|Proteomes:UP000238362};
RN [1] {ECO:0000313|EMBL:PRX48490.1, ECO:0000313|Proteomes:UP000238362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7125 {ECO:0000313|EMBL:PRX48490.1,
RC ECO:0000313|Proteomes:UP000238362};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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}.
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:PRX48490.1}.
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DR EMBL; PVNH01000004; PRX48490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0LWU5; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000238362; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000238362};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 149..224
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 317..354
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 64..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 68014 MW; E9E941755A8F538F CRC64;
MAYSVTLPEL GESVTEGTVT RWLKQEGDRV EVDEPLLEIS TDKVDTEVPS PVAGTVQKIV
AREDETVEVG GELAVIDDGS GGGGGAESAA EAARPQQEQQ EQPQQQQEQQ QAAPQEAQQA
PQPAQREQAQ PEPAAQQQQQ PPSGGQGQGT PVTLPELGES VTEGTVTRWL KQVGDQVEVD
EPLLEISTDK VDTEVPSPVA GTVLEISAQE DETVEVGGQL AVIGEPGAQA ETPAAPAEPQ
QREQQARPQA PAEEPAPAAP QQQQTQPAPQ QPTQPEQPER PEQPEPAPQQ QAQPPAQQQA
PQQQASQPSQ DGAGTPYVTP LVRKLASEHD IDLNSLRGTG VGGRIRKQDV LAAVEEKQQR
EQQAPQPEPQ APAAPAPAAQ APAAPRPTVS ESEKAALRGT VQKASRIRQI TAQKTKESLQ
LSAQLTQVHE VDVTKIARLR QRAKEAFRQR EGVNLTFLPF FAKATVEALK QHPNVNASYN
EETKEITYHG AVHLGIAVDT ERGLLSVVIH DAGELSLAGL AHRIADLADR ARTNRIKPEE
LTGGTFTVTN IGSQGALFDT PIIVQPQSGI LGTGAVVKRP VVSADADGND TIAIRSMAYL
PLTYDHRLID GADAGRFLTT IKQRLEEGNF EDELGL
//
