ID A9VSD2_BACWK Unreviewed; 429 AA.
AC A9VSD2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 43.
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=murA; OrderedLocusNames=BcerKBAB4_5132;
OS Bacillus weihenstephanensis (strain KBAB4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H.,
RA Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY46278.1; -; Genomic_DNA.
DR RefSeq; YP_001647906.1; NC_010184.1.
DR ProteinModelPortal; A9VSD2; -.
DR STRING; 315730.BcerKBAB4_5132; -.
DR EnsemblBacteria; ABY46278; ABY46278; BcerKBAB4_5132.
DR GeneID; 5845373; -.
DR KEGG; bwe:BcerKBAB4_5132; -.
DR PATRIC; 19015019; VBIBacWei55973_5796.
DR eggNOG; COG0766; -.
DR HOGENOM; HOG000075602; -.
DR KO; K00790; -.
DR OMA; EHTMLPD; -.
DR ProtClustDB; PRK12830; -.
DR BioCyc; BWEI315730:GHRU-5276-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 429 AA; 45923 MW; C8C6DB85C836B536 CRC64;
MEKLLIEGGR ALNGTIRVSG AKNSAVALIP ATILADTPVT IGGVPNISDV KMLGDLLEEI
GGKVTYGQEE EMVVDPSNMV AMPLPNGKVK KLRASYYLMG AMLGRFKKAV IGLPGGCHLG
PRPIDQHIKG FEALGAYVTN EQGAIYLRAD ELRGARIYLD VVSVGATINI MLVAVRAKGR
TVIENAAKEP EIIDVATLLT SMGARIKGAG TDVIRIDGVD SLHGCHHTII PDRIEAGTYM
ILGAASGGEV TVDNVIPQHL ESVTAKLREA GVQIETNDDQ ITVNGNRRLK VVDVKTLVYP
GFPTDLQQPF TTLLTKAHGT GVVTDTIYSA RFKHIDELRR MNAQIKVEGR SAIVTGPVLL
QGAKVKASDL RAGASLVIAG LMADGITEVT GLDHIDRGYE NIVDKLKGLG ANIWREQMTK
QEIEEMKNA
//
