ID B9E3H4_CLOK1 Unreviewed; 444 AA.
AC B9E3H4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=CKR_1998 {ECO:0000313|EMBL:BAH07049.1};
OS Clostridium kluyveri (strain NBRC 12016).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH07049.1, ECO:0000313|Proteomes:UP000007969};
RN [1] {ECO:0000313|Proteomes:UP000007969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA Yukawa H.;
RT "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT of Clostridia species.";
RL Submitted (SEP-2005) 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; AP009049; BAH07049.1; -; Genomic_DNA.
DR RefSeq; WP_012102611.1; NC_011837.1.
DR AlphaFoldDB; B9E3H4; -.
DR KEGG; ckr:CKR_1998; -.
DR HOGENOM; CLU_016733_10_2_9; -.
DR Proteomes; UP000007969; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; 2.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
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|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 118..155
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 161..195
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 444 AA; 48690 MW; 52171049B0C257A0 CRC64;
MSCVEVMPKL GLTMTEGEIE TWHKSEGDEV KKGEVLFDVT TDKLTNEVEA KESGILRKIL
VKEGETAKCL EPVAIIAGAD EDISSLLKES VGKEVEVVPV EEPSIREDIP VEREGRIRIS
PLAKNLAKKS GVDYEVITGT GPLGRIVKKD VEEYIDKNRV KVSPVAAKLA KELNVDLSSI
NKQGRIMKED VLKAAEEAKQ KEKTIVQEPE NQAVTSKAAG RGEKVINMSS MRKVISARMS
ESVKISPTVT YNINIDISEL KRLKNNLKDT FKLTYTDFLI KIVSAALKQF PLVNCSISGG
KFILKDYVNM GVAVALDEGL IVPVVKDTDI KGLKQIAEEF KEIVKKAKSN SLSPDDMTGG
TFTITNLGML GIDSFSPIIN QPEVAILGVN TIVDTPVVEG EKIVVKPLMK LSLTADHRAI
DGAYAAKFLQ KIKEYIEKPE LLLL
//