ID C5NUE5_9BACL Unreviewed; 465 AA.
AC C5NUE5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=acoC {ECO:0000313|EMBL:EER69189.1};
GN ORFNames=GEMHA0001_0047 {ECO:0000313|EMBL:EER69189.1};
OS Gemella haemolysans ATCC 10379.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=546270 {ECO:0000313|EMBL:EER69189.1, ECO:0000313|Proteomes:UP000006004};
RN [1] {ECO:0000313|EMBL:EER69189.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69189.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EER69189.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69189.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000925};
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:EER69189.1}.
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DR EMBL; ACDZ02000004; EER69189.1; -; Genomic_DNA.
DR RefSeq; WP_004392823.1; NZ_ACDZ02000004.1.
DR AlphaFoldDB; C5NUE5; -.
DR GeneID; 78010823; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000006004; Unassembled WGS sequence.
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; 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; 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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
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 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 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 166..203
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 465 AA; 49162 MW; 15A7926384D9CF31 CRC64;
MAVEVIMPKA GSEMEEGEIV QWFKQEGDEV KEGEILLEIV TDKVNMEVEA EASGTLLKIV
HPAGSVVPVV QTIAWIGQAG EAVPGAGAAP AAAATPVEET VVETKVEAAP AQEVVEFDNS
GLRATPAARA YARENGIDLS QVKGTGAKGR VHKDDVVDYK LNAKAKISPL AARIAEVEGI
NTDGIVGTGP KGKIMKADVL SVLNGSASEA AASAEVAAPA SAKSAKAPNE NQWGVVETVP
MSPMRKVISK RMSESYFSAP TFVVNVEVDM TELLALRKKV VDAIIEETGK KATVTDFISL
AVIKSLMKHP YVNASLSSDE KEMYLHHYVN LSIAVGMDSG LVVPVIKGAD KMSLKELVVA
SKEITTKALA GKLKPDEMAD STFTISNLGM YGVKSFVPII NQPNTAILGV SATVQKPVVL
NGEVTVRPIM TLTLTADHRV VDGLEGAKFM KTLKEAIENP LSLLI
//