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Database: UniProt/TrEMBL
Entry: B9IRR9_BACCQ
LinkDB: B9IRR9_BACCQ
Original site: B9IRR9_BACCQ 
ID   B9IRR9_BACCQ            Unreviewed;       434 AA.
AC   B9IRR9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   OrderedLocusNames=BCQ_5127 {ECO:0000313|EMBL:ACM15527.1};
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM15527.1, ECO:0000313|Proteomes:UP000000441};
RN   [1] {ECO:0000313|EMBL:ACM15527.1, ECO:0000313|Proteomes:UP000000441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1 {ECO:0000313|EMBL:ACM15527.1,
RC   ECO:0000313|Proteomes:UP000000441};
RX   PubMed=19060151; DOI=10.1128/JB.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L.,
RA   Xu X., Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain
RT   Q1 with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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}.
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DR   EMBL; CP000227; ACM15527.1; -; Genomic_DNA.
DR   RefSeq; WP_000411260.1; NC_011969.1.
DR   ProteinModelPortal; B9IRR9; -.
DR   EnsemblBacteria; ACM15527; ACM15527; BCQ_5127.
DR   KEGG; bcq:BCQ_5127; -.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000441; 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:UP000000441};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:ACM15527.1}.
FT   DOMAIN        6    407       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      122    126       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    117    117       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING      93     93       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     306    306       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     328    328       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   MOD_RES     117    117       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   434 AA;  46800 MW;  868437CB8F7000BF CRC64;
     MEKIIVRGGK RLNGTVRVEG AKNAVLPIIA AALLASDGKN VLSEVPVLSD VYTINEVLRH
     LNAEVVFENN KVTIDASKEL NIEAPFEYVR KMRASVQVMG PLLARNGRAR IALPGGCAIG
     SRPIDQHLKG FEAMGAKVQV GNGFVEAYVE GELKGAKIYL DFPSVGATEN IMSAATLAKG
     TTILENAAKE PEIVDLANFL NAMGAKVRGA GTGTIRIEGV DKLYGANHSI IPDRIEAGTF
     MVAAAITGGD ILIENAVPEH LRSITAKMEE MGVKIIEENE GVRVIGPDKL KAVDIKTMPH
     PGFPTDMQSQ MMALLLQAEG TSMITETVFE NRFMHVEEFR RMNADIKIEG RSVIMNGPNS
     LQGAEVAATD LRAAAALILA GLVSEGYTRV TELKHLDRGY VNFHKKLAAL GATIERVNEK
     VEEVKEQEVS DLHA
//
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