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Database: UniProt/TrEMBL
Entry: Q9L1U5_STRCO
LinkDB: Q9L1U5_STRCO
Original site: Q9L1U5_STRCO 
ID   Q9L1U5_STRCO            Unreviewed;       448 AA.
AC   Q9L1U5;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   29-OCT-2014, entry version 80.
DE   SubName: Full=UDP-N-acetylglucosamine transferase {ECO:0000313|EMBL:CAB72195.1};
GN   OrderedLocusNames=SCO2949 {ECO:0000313|EMBL:CAB72195.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces;
OC   Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAB72195.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|SAAS:SAAS00085359}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-
CC       glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-
CC       D-glucosamine. {ECO:0000256|SAAS:SAAS00085422}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|SAAS:SAAS00085294}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00085410}.
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DR   EMBL; AL939114; CAB72195.1; -; Genomic_DNA.
DR   RefSeq; NP_627173.1; NC_003888.3.
DR   ProteinModelPortal; Q9L1U5; -.
DR   STRING; 100226.SCO2949; -.
DR   PRIDE; Q9L1U5; -.
DR   EnsemblBacteria; CAB72195; CAB72195; CAB72195.
DR   GeneID; 1098382; -.
DR   KEGG; sco:SCO2949; -.
DR   PATRIC; 23735626; VBIStrCoe124346_3008.
DR   HOGENOM; HOG000075602; -.
DR   InParanoid; Q9L1U5; -.
DR   KO; K00790; -.
DR   OMA; CRFGQRN; -.
DR   OrthoDB; EOG68M4GK; -.
DR   PhylomeDB; Q9L1U5; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.65.10.10; -; 2.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   PANTHER; PTHR21090:SF4; PTHR21090:SF4; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|SAAS:SAAS00085439};
KW   Cell division {ECO:0000256|SAAS:SAAS00085392};
KW   Cell shape {ECO:0000256|SAAS:SAAS00085275};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00085335};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001973};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00085389};
KW   Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00085404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW   Transferase {ECO:0000256|SAAS:SAAS00085368,
KW   ECO:0000313|EMBL:CAB72195.1}.
SQ   SEQUENCE   448 AA;  48177 MW;  1DB4D9060DF586BB CRC64;
     MTVNGADDVL LVHGGTPLEG EIRVRGAKNL VPKAMVAALL GSAPSRLRNV PDIRDVRVVR
     GLLQLHGVTV RPGEEPGELV LDPTHVESAN VADIDAHAGS SRIPILFCGP LLHRLGHAFI
     PGLGGCDIGG RPIDFHFDVL RQFGAKIEKR ADGQYLEAPQ RLRGTKINLP YPSVGATEQV
     LLTAVLAEGV TELSNAAVEP EIEDLICVLQ KMGAIIAMDT DRTIRVTGVD ELGGYTHRAL
     SDRLEAASWA SAALATEGNV YVRGAQQRSM MTFLNTFRKV GGAFEIDDEG IRFWHPGGRL
     KSIALETDVH PGFQTDWQQP LVVALTQATG LSIVHETVYE SRLGFTSALN QMGAHIQLYR
     ECLGGSDCRF GQRNFLHSAV VSGPTKLEGA DLVIPDLRGG FSYLIAALAA QGTSRVHGID
     LINRGYENFM DKLVELGAKV ELPGKALG
//
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