MURA_VIBCH
ID MURA_VIBCH Reviewed; 419 AA.
AC Q9KP62;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; OrderedLocusNames=VC_2514;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN.
RG Center for structural genomics of infectious diseases (CSGID);
RT "Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Vibrio
RT cholerae in complex with substrate UDP-N-acetylglucosamine and the drug
RT fosfomycin.";
RL Submitted (AUG-2014) to the PDB data bank.
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR EMBL; AE003852; AAF95656.1; -; Genomic_DNA.
DR PIR; D82067; D82067.
DR RefSeq; NP_232143.1; NC_002505.1.
DR RefSeq; WP_000410586.1; NZ_LT906614.1.
DR PDB; 4R7U; X-ray; 2.45 A; A/B/C/D=1-419.
DR PDBsum; 4R7U; -.
DR AlphaFoldDB; Q9KP62; -.
DR SMR; Q9KP62; -.
DR STRING; 243277.VC_2514; -.
DR DNASU; 2615178; -.
DR EnsemblBacteria; AAF95656; AAF95656; VC_2514.
DR GeneID; 57741121; -.
DR KEGG; vch:VC_2514; -.
DR PATRIC; fig|243277.26.peg.2395; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OMA; CDPHRAT; -.
DR BioCyc; VCHO:VC2514-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR036968; Enolpyruvate_Tfrase_sf.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178948"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 23..24
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0007744|PDB:4R7U"
FT BINDING 92
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 121..125
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:4R7U"
FT BINDING 161..165
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:4R7U"
FT BINDING 306
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:4R7U"
FT BINDING 328
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:4R7U"
FT MOD_RES 116
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4R7U"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:4R7U"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4R7U"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:4R7U"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:4R7U"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:4R7U"
SQ SEQUENCE 419 AA; 44686 MW; 6DC5D7D2716D2DE8 CRC64;
MEKFRVIGST QPLQGEVTIS GAKNAALPIL FASILAEEPV EVANVPHLRD IDTTMELLER
LGAKVERNGS VHVDAGPINQ YCAPYDLVKT MRASIWALGP LVARFGQGQV SLPGGCAIGA
RPVDLHIHGL EQLGATITLE DGYVKAHVDG RLQGAHIVMD KVSVGATITI MCAATLAEGT
TVLDNAAREP EIVDTAMFLN KLGAKISGAG TDSITIEGVE RLGGGKHAVV PDRIETGTFL
VAAAVSRGKI VCRNTHAHLL EAVLAKLEEA GAEIECGEDW ISLDMTGREL KAVTVRTAPH
PGFPTDMQAQ FTLLNMMAKG GGVITETIFE NRFMHVPELK RMGAKAEIEG NTVICGDVDR
LSGAQVMATD LRASASLVIA GCIAKGETIV DRIYHIDRGY ERIEDKLSAL GANIERFRD
