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Database: UniProt/TrEMBL
Entry: A0A1Z4RML2_9CHRO
LinkDB: A0A1Z4RML2_9CHRO
Original site: A0A1Z4RML2_9CHRO 
ID   A0A1Z4RML2_9CHRO        Unreviewed;       432 AA.
AC   A0A1Z4RML2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   31-JAN-2018, entry version 5.
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=NIES4102_07110 {ECO:0000313|EMBL:BAZ43710.1};
OS   Chondrocystis sp. NIES-4102.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Chondrocystis.
OX   NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ43710.1, ECO:0000313|Proteomes:UP000217698};
RN   [1] {ECO:0000313|EMBL:BAZ43710.1, ECO:0000313|Proteomes:UP000217698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ43710.1,
RC   ECO:0000313|Proteomes:UP000217698};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-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; AP018281; BAZ43710.1; -; Genomic_DNA.
DR   KEGG; chon:NIES4102_07110; -.
DR   KO; K00627; -.
DR   Proteomes; UP000217698; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000217698};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:BAZ43710.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      138    175       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED       69     96       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   432 AA;  45292 MW;  643EB210331B2602 CRC64;
     MIHDIFMPAL SSTMTEGKIV EWTKSPGDKI TKGETVLVVE SDKADMDVES FNEGYLAVIL
     VEAGQEAPVG SAIALIAETE AEIAEAKKQA ASLKSDNGAS TTAAKPETVK ANAQVDVTST
     TANNTASSNG SRAEGRIVAS PRAKKLAKQL NIDLKTLEGS GPYGRITTGD VEKASGKTST
     PTPATAVAPA PAPAPAPAPA PVPVVSSTPG ETVPLNTLQK AVVQNMMASL QVPTFHVSYT
     ITTDALDALY QQIKSKGVTM TALLAKAIAV TLKQHPVVNA GYRQDAISYN SEINIAVAVA
     MPDGGLITPV LRNADQMDIY SLSRTWKDLV DRSRAKQLKP EEYSTGTFTL SNLGMFGVDS
     FDAILPPGQG SILAVGGSKP QLVADNSGMM GVKRQMKVNI TSDHRIIYGA QAAAFLKDLA
     TLIETNPQSL TL
//
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