MURA_CAMJE
ID MURA_CAMJE Reviewed; 418 AA.
AC Q9PP65; Q0PA32;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Cj0858c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL34986.1; -; Genomic_DNA.
DR PIR; B81359; B81359.
DR RefSeq; WP_002857102.1; NC_002163.1.
DR RefSeq; YP_002344265.1; NC_002163.1.
DR PDB; 5UJS; X-ray; 2.46 A; A/B=1-418.
DR PDBsum; 5UJS; -.
DR AlphaFoldDB; Q9PP65; -.
DR SMR; Q9PP65; -.
DR IntAct; Q9PP65; 1.
DR STRING; 192222.Cj0858c; -.
DR PaxDb; Q9PP65; -.
DR PRIDE; Q9PP65; -.
DR EnsemblBacteria; CAL34986; CAL34986; Cj0858c.
DR GeneID; 905157; -.
DR KEGG; cje:Cj0858c; -.
DR PATRIC; fig|192222.6.peg.846; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_7; -.
DR OMA; CDPHRAT; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000799; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178856"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
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:0000255|HAMAP-Rule:MF_00111"
FT BINDING 305
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 327
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT MOD_RES 116
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:5UJS"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:5UJS"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:5UJS"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:5UJS"
SQ SEQUENCE 418 AA; 45186 MW; EDB9C63408C5B7F3 CRC64;
MTYLEIEGTN HLSGNVTISG AKNAALPLIV SSILAKNEVK INNVPNVADI KTLISLLENL
GAKVNFQNNS ALLNTNTLNQ TIAKYDIVRK MRASILTLGP LLARFGHCEV SLPGGCAIGQ
RPIDLHLLAL EKMGANIQIK QGYVVASGNL KGNEILFDKI TVTGSENIIM AAALAKGKTK
LLNVAKEPEV VQLCEVLKDA GLEIKGIGTD ELEIYGSDGE LLEFKEFSVI PDRIEAGTYL
CAGAITNSKI TLDKVNATHL SAVLAKLHQM GFETLITEDS ITLLPAKEIK PVEIMTSEYP
GFPTDMQAQF MALALKANGT SIIDERLFEN RFMHVSELLR MGADIKLNGH IATIVGGKEL
NAADVMATDL RASSALILAA LAAKGTSKVH RIYHLDRGYE NLEEKFKDLG AKITRLEE
