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Database: UniProt/TrEMBL
Entry: Q1D8Y6_MYXXD
LinkDB: Q1D8Y6_MYXXD
Original site: Q1D8Y6_MYXXD 
ID   Q1D8Y6_MYXXD            Unreviewed;       527 AA.
AC   Q1D8Y6;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   07-JUN-2017, entry version 81.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=pdhC {ECO:0000313|EMBL:ABF88747.1};
GN   OrderedLocusNames=MXAN_2668 {ECO:0000313|EMBL:ABF88747.1};
OS   Myxococcus xanthus (strain DK 1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88747.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF88747.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK 1622 {ECO:0000313|EMBL:ABF88747.1,
RC   ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP000113; ABF88747.1; -; Genomic_DNA.
DR   RefSeq; WP_011552738.1; NC_008095.1.
DR   ProteinModelPortal; Q1D8Y6; -.
DR   STRING; 246197.MXAN_2668; -.
DR   EnsemblBacteria; ABF88747; ABF88747; MXAN_2668.
DR   KEGG; mxa:MXAN_2668; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; SWRLGCD; -.
DR   OrthoDB; POG091H0NG1; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate 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; IPR004167; E3-bd.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ABF88747.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002402};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:ABF88747.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ABF88747.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      124    199       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   527 AA;  55096 MW;  51320C2A91FF945E CRC64;
     MAIPIQMPSL SPTMTEGKIV KWLKKQGDKV SSGDAVAEVE TDKSNLEIEA YDDGYLLQVL
     VGEGEMAKVG APIAYIGAKG EKVGAGKQVA PAAAPPEQKP QPAPAAPAPQ AAAKPASSGG
     GDNRIAIQMP SLSPTMTEGK IVKWLKKQGD KVSSGDAVAE VETDKSNLEI EAYDNGTLAE
     IVVGENQMAK VGAPIAYLTA KGAKAAPAAP AAQPKPPAPA PEKPAAAKPA AAPAQAGGRR
     LRASPVAKRI AREKGLDLTQ VSGSGPSGRV VKRDIEEALA RGPAAVPAAK KAPAAQPAPG
     VRPEPTVLPL SSMRKVIAQR MTEVKPGVPH FYLTIEVDME AASKVREEAK AMDLKVSVND
     LIVKAVAMAV RRYPKINVSL QGDKVVQFHS VDVGIAVALE EGLITPILRD ADQKGLQAIA
     SGVRELAERA RKRALKPEEY TGGSITVSNL GMYGIDQFVA VINPPQASIL AVGAVSEKAV
     VRDGQLAVRK MMTATLSCDH RVIDGAIGAE FLRELRGLLE HPTRLLF
//
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