GenomeNet

Database: UniProt/TrEMBL
Entry: E4NBV9_KITSK
LinkDB: E4NBV9_KITSK
Original site: E4NBV9_KITSK 
ID   E4NBV9_KITSK            Unreviewed;       451 AA.
AC   E4NBV9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA1 {ECO:0000313|EMBL:BAJ28690.1};
GN   Synonyms=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   OrderedLocusNames=KSE_28790 {ECO:0000313|EMBL:BAJ28690.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC
OS   A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ28690.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ28690.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T.,
RA   Horinouchi S., Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A.,
RA   Nomoto F., Miura H., Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767217}.
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|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767208}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767211}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010968; BAJ28690.1; -; Genomic_DNA.
DR   RefSeq; WP_014136003.1; NC_016109.1.
DR   ProteinModelPortal; E4NBV9; -.
DR   STRING; 452652.KSE_28790; -.
DR   EnsemblBacteria; BAJ28690; BAJ28690; KSE_28790.
DR   KEGG; ksk:KSE_28790; -.
DR   PATRIC; fig|452652.3.peg.2885; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   KO; K00790; -.
DR   OMA; CRFGQRN; -.
DR   OrthoDB; POG091H01PG; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007076; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767221};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767191};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767246};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767261};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007076};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767234};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767219};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:BAJ28690.1}.
FT   DOMAIN        9    429       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       24     25       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    122    122       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING      98     98       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     312    312       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     334    334       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   MOD_RES     122    122       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   451 AA;  48339 MW;  780D89E33625CF2E CRC64;
     MTDDVLLVHG GNPLEGEIQI RGAKNLVPKA MVAALLGQGP SRLRNVPDIR DVKVVRGLLQ
     LHGVTVRTGD EDGELILDPS HVESANVADI DAHAGSSRIP ILFCGPLLHR LGHAFIPGLG
     GCDIGGRPVD FHFEVLRQFG ATIEKHPQGT YLVATQRLRG TKIELPYPSV GATEQVLLTA
     VLAEGVTELR NAAIEPEIVD LICVLQKMGA IISLGTDRTI LVTGVDELDG YTHRALPDRL
     EAASWACAAL ATKGDIYVRG AEQIPMMTFL NTFRKVGGAY EIDDEGIRFW HPGGELKAIA
     LETDVHPGFQ TDWQQPLVVA LTQATGLSIV HETVYESRLG FTGALNQMGA HIQLYSECLG
     GTPCRFGARN FMHSAVVSGP SKLVGGELVI PDLRGGFSYL IAALAAEGTS TVHGIDLINR
     GYENFMDKLR DLGAHIELPA AAEVAEVQLT A
//
DBGET integrated database retrieval system