ID A0A1V2Q2Q0_9PSEU Unreviewed; 454 AA.
AC A0A1V2Q2Q0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=ALI22I_39640 {ECO:0000313|EMBL:ONI82249.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI82249.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI82249.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI82249.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI82249.1}.
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DR EMBL; MTQP01000068; ONI82249.1; -; Genomic_DNA.
DR RefSeq; WP_077010715.1; NZ_MTQP01000068.1.
DR AlphaFoldDB; A0A1V2Q2Q0; -.
DR STRING; 1933778.ALI22I_39640; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000188617; 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; 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; 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; 1.
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; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
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:UP000188617};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 170..207
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 118..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 47237 MW; 5887DD2B3E4537BD CRC64;
MPQFKQFSMP DTAEGLTEAE ILTWHVKPGD AVKVNQIILE IETAKAAVEL PCPWDGVVTE
LLAEVGQTVE VGVPIITIDV DPSGAAPAAP APAAAAAPAP AESNGKIGEE MPGGRIATLV
GYGPRSGAAK RRPRKDAPAP VAAAPAPVAA PVPAPVVPEP VVTPGGYVPL AKPPVRKLAK
ELGVDLYALS GSGPGGVITR EDVEQAVAPA APTPPASVVD SGARERRVPI KGVRKATAQA
MVDSAFTAPH VTEFLTVDVT PMMELRARLK NKPEFRDVKL TPLAFAAKAV VLAARRTPDV
NATWDAEAQE IVYKDYVHLG IAAATPRGLV VPKVRDADRM SLRELAVALD NLATTARDGK
TTPADMMGGT FTITNVGVFG VDTGTPIINP GESAILAFGA IRDMPWVVDG QVVPRKVCQL
ALSFDHRVVD GQQGSQFLAD VGALLADPGV AITY
//
