ID B9IRR9_BACCQ Unreviewed; 434 AA.
AC B9IRR9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase;
DE EC=2.5.1.7;
DE AltName: Full=Enoylpyruvate transferase;
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase;
GN Name=murA1; Synonyms=murA; OrderedLocusNames=BCQ_5127;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-
CC glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-
CC D-glucosamine.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
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DR EMBL; CP000227; ACM15527.1; -; Genomic_DNA.
DR RefSeq; YP_002532816.1; NC_011969.1.
DR ProteinModelPortal; B9IRR9; -.
DR STRING; 361100.BCQ_5127; -.
DR EnsemblBacteria; ACM15527; ACM15527; BCQ_5127.
DR GeneID; 7376578; -.
DR KEGG; bcq:BCQ_5127; -.
DR PATRIC; 18918078; VBIBacCer120424_5177.
DR eggNOG; COG0766; -.
DR HOGENOM; HOG000075602; -.
DR KO; K00790; -.
DR OMA; SIWALAP; -.
DR ProtClustDB; PRK09369; -.
DR BioCyc; BCER361100:GJ7M-5114-MONOMER; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:HAMAP.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA: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 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 PANTHER; PTHR21090:SF4; PTHR21090:SF4; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 1.
DR TIGRFAMs; TIGR01072; murA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW Peptidoglycan synthesis; Transferase.
FT ACT_SITE 117 117 Proton donor (By similarity).
FT MOD_RES 117 117 2-(S-cysteinyl)pyruvic acid O-
FT phosphothioketal (By similarity).
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
//
