ID A0A0M2H317_9MICO Unreviewed; 573 AA.
AC A0A0M2H317;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=aceF {ECO:0000313|EMBL:KJL37907.1};
GN ORFNames=RS81_02899 {ECO:0000313|EMBL:KJL37907.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL37907.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL37907.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL37907.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL37907.1}.
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DR EMBL; JYIZ01000056; KJL37907.1; -; Genomic_DNA.
DR RefSeq; WP_045276821.1; NZ_JYIZ01000056.1.
DR AlphaFoldDB; A0A0M2H317; -.
DR STRING; 92835.RS81_02899; -.
DR PATRIC; fig|92835.4.peg.2931; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000033956; 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 ECO:0000313|EMBL:KJL37907.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:KJL37907.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KJL37907.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..208
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 275..312
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 57639 MW; 8ED9D9DE49A72ABD CRC64;
MSTSVVLPAL GESVTEGTVT RWLKNVGDTV QADEGLLEIS TDKVDTEIPS PVSGVIEEIL
VQEDETVEVG AILAKIGDGS GAPASDDAPE AAPAEASAAP AEEAPAAEAP AAEAPAAEAP
ATEAAPAAPA SGGKEVVLPE LGESVTEGTV TRWLKQIGDE VAVDEPLLEI STDKVDTEIP
SPFAGVLQEI LVPEDETVAV GSALARIGEA GAAAPAEAAP AQPAPAAAEP APAPAAAAPA
AAAPAPAGAP AAPAPAAAPA PAAGPALTGD DDVAYVTPLV RRLAQQQNVD LASVTGTGVG
GRIRKEDVLK AAEAAAAPAA AAPAAAAAPA PLEVSALRGT TQPMSRLRKV IAERAVASMQ
ATAQLTTVVE VDVTKLAAFR DAVKGDFQAK TGDKLSFLPF FAVAAVEALQ AFPIINATVD
GTDIVYPATE NISIAVDTER GLLTPVVKSA AGKNLAQFAR EIADLAARTR DNKLTPDELA
GGTFTLTNTG SRGALFDTPI VFLPQSAILG LGAVVKKPGI VSVDGKDAIS VRSYVYLALS
YDHRIIDGAD AARFLGAVKA RLEAAQFEAQ LGY
//
