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Database: UniProt
Entry: A0A1U7NSQ9_9DEIO
LinkDB: A0A1U7NSQ9_9DEIO
Original site: A0A1U7NSQ9_9DEIO 
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
//
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