ID Q8Y863_LISMO Unreviewed; 544 AA.
AC Q8Y863;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:CAC99132.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99132.1, ECO:0000313|Proteomes:UP000000817};
RN [1] {ECO:0000313|EMBL:CAC99132.1, ECO:0000313|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591977; CAC99132.1; -; Genomic_DNA.
DR PIR; AF1206; AF1206.
DR RefSeq; NP_464579.1; NC_003210.1.
DR RefSeq; WP_010989651.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y863; -.
DR STRING; 169963.gene:17593710; -.
DR PaxDb; 169963-lmo1054; -.
DR EnsemblBacteria; CAC99132; CAC99132; CAC99132.
DR GeneID; 986301; -.
DR KEGG; lmo:lmo1054; -.
DR PATRIC; fig|169963.11.peg.1083; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_9; -.
DR OrthoDB; 9805770at2; -.
DR PhylomeDB; Q8Y863; -.
DR BioCyc; LMON169963:LMO1054-MONOMER; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000000817};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 112..187
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 237..274
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 58194 MW; 07FC9DCE4A332B62 CRC64;
MAYSFKLPDI GEGIHEGEIV KWFVQPGDKI EEDESLFEVQ NDKSVEEITS PVSGTIKEIK
VAEGTVATVG QVLVTFDGVE GHEDDAEEES AAPKAESTES TPAPAQASGK GIFEFKLPDI
GEGIHEGEIV KWFIQPGDKV EEDQSIFEVQ NDKSVEEITS PVDGTVKDIL VSEGTVATVG
QVLVTFEGDF EGEASHESTP ESPAEDAALA NNDATSAPAT GGNGTPSSKK DPNGLVIAMP
SVRKYAREKG VNIAEVAGSG KNNRVVKADI DAFLNGEQPA AATTTAQTEE KAAAPKAEKA
AGKQPVASSD AYPETREKLT PTRRAIAKAM VNSKHTAPHV TLMDEIEVTA LMAHRKRFKE
VAAEKGIKLT FLPYMVKALV ATLRDFPVLN TTLDDATEEL VYKHYFNVGI AADTDHGLYV
PVIKNADKKS VFQISDEINE LAGKARDGKL TADEMRHGSA TISNIGSAGG QWFTPVINYP
EVAILGVGRI AQKPIVKDGE IVAAPVLALS LSFDHRVIDG ATAQKAMNNI KRLLNDPELL
LMEV
//
