ID A0A1H3JMU5_9ACTN Unreviewed; 624 AA.
AC A0A1H3JMU5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05661080_03388 {ECO:0000313|EMBL:SDY40939.1};
OS Modestobacter sp. DSM 44400.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1550230 {ECO:0000313|EMBL:SDY40939.1, ECO:0000313|Proteomes:UP000199500};
RN [1] {ECO:0000313|EMBL:SDY40939.1, ECO:0000313|Proteomes:UP000199500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44400 {ECO:0000313|EMBL:SDY40939.1,
RC ECO:0000313|Proteomes:UP000199500};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNOZ01000029; SDY40939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3JMU5; -.
DR STRING; 1550230.SAMN05661080_03388; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000199500; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000199500};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 149..224
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 314..351
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 74..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 62465 MW; B695B74E29E8DABD CRC64;
MPTSVTMPAL GESVTEGTVT RWLKQEGDQV EVDEPLLEVS TDKVDTEIPS PAAGVLTKIL
VAEDETVDVG AELAVIGGDG GGGDAGGPAE QVPAQPAPTE EAPAQEAPAQ EAPAQEAPAE
QAEPAAAQPV ASGSADSGSG GGSTGGGEGT SVTMPALGES VTEGTVTRWL KAVGDEVTAD
EPLLEVSTDK VDTEIPAPVS GTLLSISVAE DETVDVGAEL AVIGTAGGTP ASAPAAPAPA
EAPSAPASPA STAGSAESDY SGPAPEAEVA TTPEAKEPAP APKAPAAAPA APSTPAPAAA
SADGAAGDGA AGAYVTPLVR RLAAEHGVDL SSVQGTGVGG RIRKQDVLAA ATPAAPEAPA
APATAAPAAA AGKPSAAASQ DPSLRGRTEK LSRLRTVIAR RMVESLEISA QLTTVVEADV
TRIARLRDQA KADFGAREGV KLSFLPFFAK AAVEALKVHP SVNSSVDLEA GTVTYHDSEN
LGVAVDTERG LLVPVIQSAG DLSLAGIARK IADLAERTRT NKVTPDELGG GTFTLTNTGS
RGALFDTPII NQPQVAILGV GSVVKRPVVV QDPELGEVIA VRSMVYLALT YDHRIVDGAD
AARFLTTVRE RLEAGQFQGE LGLA
//
