ID T5HUD2_BACLI Unreviewed; 377 AA.
AC T5HUD2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=N399_04410 {ECO:0000313|EMBL:EQM29261.1};
OS Bacillus licheniformis CG-B52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1368424 {ECO:0000313|EMBL:EQM29261.1, ECO:0000313|Proteomes:UP000017025};
RN [1] {ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|Proteomes:UP000017025};
RA Galvez-Bobadilla E.J., Zarate-Bonilla L.J., Carrillo-Castro K., Guiza L.,
RA Pieper D.H., Salazar M., Junca H.;
RT "Draft genome of a Bacillus sp. strain CG-B52 virulent to shrimps.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQM29261.1, ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|EMBL:EQM29261.1,
RC ECO:0000313|Proteomes:UP000017025};
RX PubMed=27174263;
RA Galvez E.J., Carrillo-Castro K., Zarate L., Guiza L., Pieper D.H.,
RA Garcia-Bonilla E., Salazar M., Junca H.;
RT "Draft Genome Sequence of Bacillus licheniformis CG-B52, a Highly Virulent
RT Bacterium of Pacific White Shrimp (Litopenaeus vannamei), Isolated from a
RT Colombian Caribbean Aquaculture Outbreak.";
RL Genome Announc. 4:0-0(2016).
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:EQM29261.1}.
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DR EMBL; AVEZ01000004; EQM29261.1; -; Genomic_DNA.
DR AlphaFoldDB; T5HUD2; -.
DR PATRIC; fig|1368424.3.peg.343; -.
DR Proteomes; UP000017025; 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; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 99..136
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 40734 MW; BCB32DD17ADB7E26 CRC64;
MAVEVVMPKL GMSMKEGTVS VWNKKVGEAV EKGESIASIN SEKIEMEIES PANGTVLDIQ
VSEGEGVPPG TVICRIGNEN EQTQESQTKQ PDPTKERIKI SPAARKIAQS ANIDIKTLKG
TGPGGRITKA DVLQALPGRP NKQAAKAEAE ERPPASPMRK TIAARMTESL QNSAQLTITM
KADITKLTVL QKQLNETAQS RYDTKLTITD FAARAAVFSL LDHPAMNSVY QDGRLATFEH
VHLGVAAALD EGLAVPVIRH AERLPLIELA KKIKWYAKKA REGRLLHDEI EGSTFTITNL
GAYGVEHFTP ILNPPETGIL GVGQMYSAPV YQDGELTKGA ILPLSLTFDH RALDGAPAAA
FLSDVKNYLE DPASILL
//