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Database: UniProt
Entry: D5MLE7_9BACT
LinkDB: D5MLE7_9BACT
Original site: D5MLE7_9BACT 
ID   D5MLE7_9BACT            Unreviewed;       403 AA.
AC   D5MLE7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   10-APR-2019, entry version 44.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=sucB {ECO:0000313|EMBL:CBE67813.1};
GN   ORFNames=DAMO_0746 {ECO:0000313|EMBL:CBE67813.1};
OS   Candidatus Methylomirabilis oxyfera.
OC   Bacteria; candidate division NC10; Candidatus Methylomirabilis.
OX   NCBI_TaxID=671143 {ECO:0000313|EMBL:CBE67813.1, ECO:0000313|Proteomes:UP000006898};
RN   [1] {ECO:0000313|EMBL:CBE67813.1, ECO:0000313|Proteomes:UP000006898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20336137; DOI=10.1038/nature08883;
RA   Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S.,
RA   Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D.,
RA   Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M.,
RA   van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M.,
RA   Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M.,
RA   Strous M.;
RT   "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria.";
RL   Nature 464:543-548(2010).
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; FP565575; CBE67813.1; -; Genomic_DNA.
DR   STRING; 671143.DAMO_0746; -.
DR   KEGG; mox:DAMO_0746; -.
DR   PATRIC; fig|671143.5.peg.646; -.
DR   KO; K00658; -.
DR   Proteomes; UP000006898; Chromosome.
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   ECO:0000313|EMBL:CBE67813.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006898};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CBE67813.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      114    151       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   403 AA;  43384 MW;  CA5A62FFB1FA5DD1 CRC64;
     MLIEVVMPQM GESVAEGTVV TWLKKVGDSI AKDEPLVAIS TDKVDVEIPA PSAGVLSQIV
     VQEGVTASVG AVLAYIGEAS HAGAVSPDRS VVERQDGVQT AAPAVEAAAP ATRWYSPAVL
     DLAQEHDVDL TQVRGTGADG RVTRKDLLDF IAQRSETVAA SPRVSPELPA PLIEDRILPI
     SPMRKAIAEH MIRSKRTAAH VTQIHEVDMT AIDRYRQAHH SAFLKETGTA LTFLPFVVKA
     VADGLRAYPL INASFTHKGI IVKHAINIGI AVALEEGLIV PVLREADKKS FLTLTKQLTD
     LAVRARDKRL SLEEVHEGTF TVNNFGALGT MIGTPIIVQP QAAILGLGRV VKRPVVIDDA
     IVIRSMAYLC LSYDHRLIDG AYASAFLNHV RATLEGFDFS VIR
//
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