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Database: UniProt
Entry: A0A1T4PHY3_9GAMM
LinkDB: A0A1T4PHY3_9GAMM
Original site: A0A1T4PHY3_9GAMM 
ID   A0A1T4PHY3_9GAMM        Unreviewed;       467 AA.
AC   A0A1T4PHY3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
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=SAMN02745674_01214 {ECO:0000313|EMBL:SJZ91145.1};
OS   Lysobacter spongiicola DSM 21749.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1122188 {ECO:0000313|EMBL:SJZ91145.1, ECO:0000313|Proteomes:UP000190061};
RN   [1] {ECO:0000313|EMBL:SJZ91145.1, ECO:0000313|Proteomes:UP000190061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21749 {ECO:0000313|EMBL:SJZ91145.1,
RC   ECO:0000313|Proteomes:UP000190061};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; FUXP01000003; SJZ91145.1; -; Genomic_DNA.
DR   BioCyc; GCF_900167055:B5D37_RS06020-MONOMER; -.
DR   Proteomes; UP000190061; Unassembled WGS sequence.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 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   Complete proteome {ECO:0000313|Proteomes:UP000190061};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SJZ91145.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190061};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SJZ91145.1}.
FT   DOMAIN        4     79       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      167    204       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       84    161       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1T4PHY3}.
FT   REGION      204    261       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1T4PHY3}.
FT   COMPBIAS    109    138       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1T4PHY3}.
FT   COMPBIAS    144    161       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1T4PHY3}.
FT   COMPBIAS    230    247       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1T4PHY3}.
SQ   SEQUENCE   467 AA;  48480 MW;  FA2364ADAE189D1B CRC64;
     MSNKKSFFLP DLGEGLPDAT IVEWTVKVGD TIQLDDALVS METAKAVVEV PSPVSGKVLK
     LAGEPGDVIN TGAMLAEFEI DPSMPQRSEG QDTGHHHGGG QPSKGVGSED PAPDDRVVAS
     DDGGAIEDDG EAPAKGKTRE DSGTVVGAMQ SSDTVRSEQA SSIGGVKAMP AVRALARKLK
     VDLSRVNATG TDGVVTMADV KKAAADGSAP AGAAPRAAGR AERAPAPSNA QAPAQRSTLS
     QSGKPMRTQP PGVAASGQPE QLKGVRRNMA RVMADAHAKV VPTTLCDDAD LHAWIGKQDI
     TARLIRAIVA ACKAVPALNA WFDGEKLVRT MHPQVDIGIA VDTEDGLFVP ALRNADVLDA
     AGIRSSIQRL RAQVEDRSIP ASELSGYTIS LSNFGMFAGR YATPVVVPPT VAIVGAGKLS
     HDVVAVMGGV EVHRRMPISL TFDHRACTGG EAARFLKALL DDLGSPQ
//
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