MURA_ALIFM
ID MURA_ALIFM Reviewed; 422 AA.
AC B5F9P4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=VFMJ11_0391;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:3VCY}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN.
RC STRAIN=MJ11 {ECO:0000303|PubMed:22505403};
RX PubMed=22505403; DOI=10.1107/s1744309112006720;
RA Bensen D.C., Rodriguez S., Nix J., Cunningham M.L., Tari L.W.;
RT "Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from
RT Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the
RT drug fosfomycin.";
RL Acta Crystallogr. F 68:382-385(2012).
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; CP001139; ACH66965.1; -; Genomic_DNA.
DR RefSeq; WP_005417511.1; NC_011184.1.
DR PDB; 3VCY; X-ray; 1.92 A; A/B/C/D=1-422.
DR PDBsum; 3VCY; -.
DR AlphaFoldDB; B5F9P4; -.
DR SMR; B5F9P4; -.
DR EnsemblBacteria; ACH66965; ACH66965; VFMJ11_0391.
DR GeneID; 64241827; -.
DR KEGG; vfm:VFMJ11_0391; -.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OMA; CDPHRAT; -.
DR BRENDA; 2.5.1.7; 71.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001857; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; Transferase.
FT CHAIN 1..422
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_1000094731"
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:0000305|PubMed:22505403,
FT ECO:0007744|PDB:3VCY"
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:0000269|PubMed:22505403,
FT ECO:0007744|PDB:3VCY"
FT BINDING 161..165
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:22505403,
FT ECO:0007744|PDB:3VCY"
FT BINDING 306
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22505403,
FT ECO:0007744|PDB:3VCY"
FT BINDING 328
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22505403,
FT ECO:0007744|PDB:3VCY"
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:3VCY"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3VCY"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:3VCY"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:3VCY"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:3VCY"
SQ SEQUENCE 422 AA; 44726 MW; EBEDB6832F3D273D CRC64;
MYKFRIQGSD KPLSGEVTIS GAKNAALPIL FASLLAEEPV EVANVPKLRD VDTTMELLKR
LGAEVSRNGS VHIDASGVND FCAPYDLVKT MRASIWALGP LVARFGKGQV SLPGGCAIGA
RPVDLHIHGL EQLGATIKLE EGYVKAEVDG RLKGAHIVMD KVSVGATITV MCAATLAEGT
TVLENAAREP EIVDTANFLN AIGAKVSGMG TDTITIEGVE RLGGGYHEVV ADRIETGTFL
VAAAVSGGKI VCKNTKAHLL EAVLAKLEEA GADVQTGDDW ISLDMTGREL KAVNIRTAPH
PAFPTDMQAQ FTLLNMMAKG SGIITETIFE NRFMHIPELQ RMGAHAEIEG NTAICGDTDG
LSGAQVMATD LRASASLVIA GCIAKGETIV DRIYHIDRGY DKIEDKLTAL GANIERVHSD
DL
