ID A0A1U7NSQ9_9DEIO Unreviewed; 593 AA.
AC A0A1U7NSQ9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BOO71_0013189 {ECO:0000313|EMBL:OLV15941.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV15941.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV15941.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV15941.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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:OLV15941.1}.
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DR EMBL; MSTI01000157; OLV15941.1; -; Genomic_DNA.
DR RefSeq; WP_075836342.1; NZ_MSTI01000157.1.
DR AlphaFoldDB; A0A1U7NSQ9; -.
DR STRING; 249408.BOO71_0013189; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000186607; Unassembled WGS sequence.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:OLV15941.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OLV15941.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 291..328
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 88..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 60620 MW; F4D3D1E6A74FF3A6 CRC64;
MATELKLPDV GDNIEKGTVV TVLVKAGDTI AEGDPIIEIE TDKAVIEVPA SEGGTVEAVS
VNVGDTVNVG GVILTLSGGG AAPAAAAPAQ AEAPKAEAPK QEAAAPAPAA SAPAQSGGGS
TVVALPDVGD NIEKGTVVTV LVNVGDTVKE GDPVIEIETD KAVIEVPSSA GGTVESIGVA
VGDTVNVGGT ILTLSGGAGG AAAAAPAQTS TTQGGGDQAA NVESSGTAAD AGTANRVAQA
QQEAQKAQAA PQAQPSLPSG AQAGGEQPKA QFPGAQGTYN TQTYDGRTVI PAAPSVRRMA
REIGVDIHTV HGTGIAGRIS EEDVRRTAGT PSVQPAAAAA QAPTAHSPQP TAPLPNFEKW
GTVKREDMSG IRKATVRSMT ASWTTIPMVT HFDKADVTAM EETRKRFGAR VEKAGGKLTM
THILMKVVAN ALRQFPKFGA SLDLGAEQVV FKDYINIGVA VDTPVGLLVP VVKDADRKSI
TELVLELAEL AGRARERKLK PDEMSGATFT ISNLGGIGGH AFTPIVNSPE VAILGVSRGG
LEPVWNKEKG EFEPRNMLPL SLTYDHRLID GADAARFVRF IAEALEDPFL ISL
//