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Database: UniProt/TrEMBL
Entry: G0J0R4_CYCMS
LinkDB: G0J0R4_CYCMS
Original site: G0J0R4_CYCMS 
ID   G0J0R4_CYCMS            Unreviewed;       550 AA.
AC   G0J0R4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-MAR-2018, entry version 37.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   OrderedLocusNames=Cycma_0702 {ECO:0000313|EMBL:AEL24476.1};
OS   Cyclobacterium marinum (strain ATCC 25205 / DSM 745) (Flectobacillus
OS   marinus).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL24476.1, ECO:0000313|Proteomes:UP000001635};
RN   [1] {ECO:0000313|Proteomes:UP000001635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25205 / DSM 745 {ECO:0000313|Proteomes:UP000001635};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Schuetze A., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Cyclobacterium marinum DSM 745.";
RL   Submitted (JUL-2011) 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).
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; CP002955; AEL24476.1; -; Genomic_DNA.
DR   RefSeq; WP_014018774.1; NC_015914.1.
DR   STRING; 880070.Cycma_0702; -.
DR   EnsemblBacteria; AEL24476; AEL24476; Cycma_0702.
DR   KEGG; cmr:Cycma_0702; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H0NG1; -.
DR   BioCyc; CMAR880070:GHDK-709-MONOMER; -.
DR   Proteomes; UP000001635; 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; 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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001635};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AEL24476.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001635};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AEL24476.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      130    205       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      265    302       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   550 AA;  59068 MW;  C664540B8242F3A7 CRC64;
     MAEIIRMPKM SDTMEEGVIA QWLKKVGDKV KPGDILAEVE TDKATMELES YDEGTLLHIG
     VKEKDAVPVN GVIAILGEEG ENIDDLLKDV DSGGSSESAS TETKEDAAEE KSEDKAKETT
     SEIDVSGIAA TVITMPKMSD TMQEGTIASW LKKEGDEVKS GDVLAEVETD KATMELESYD
     DGTLLYIGVS EGESVEVNGV IAIIGEKDAD YKTLLKAHQQ KSSGAEEVKA EPVKEEKSAP
     KAEEGKPSNA VADSSTSTTD KGRIKASPLA KKMASEKGID ISLVKGTGDN GRIIKKDIEN
     FDPSKVTAAS SSSSDAPSGV AIGQESYTDV KVSQMRKVIA KRLAESKFTA PHFYLTMEIN
     MDKAIEARKS MNEVAPVKIS FNDMVIKAAA ASLKQHPAVN SAWMEDKIRY NDHVHIGMAV
     AIDDGLLVPV IRFTDSKSLS QISQEAKSLA GKAKNKELQP KDWEGNTFTV SNLGMFGIEE
     FTAIINPPDA CILAIGGIKQ TPIVKDGEIK IGNVMKVTLS CDHRVVDGAV GSAFLKTLKS
     LLEDPVRLLI
//
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