ID MURA_SHEPC Reviewed; 419 AA.
AC A4Y3C4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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};
GN OrderedLocusNames=Sputcn32_0727;
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 / ATCC BAA-453;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000681; ABP74457.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y3C4; -.
DR SMR; A4Y3C4; -.
DR STRING; 319224.Sputcn32_0727; -.
DR KEGG; spc:Sputcn32_0727; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR UniPathway; UPA00219; -.
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; Enolpyruvate transferase domain; 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 NCBIfam; TIGR01072; murA; 1.
DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase.
FT CHAIN 1..419
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_1000023103"
FT ACT_SITE 117
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 93
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 307
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 329
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 117
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ SEQUENCE 419 AA; 44727 MW; 9ACAEA214E9238B1 CRC64;
MDKLTIQASP PLAGDVIISG AKNAALPILM AGVLAETDFV VSNVPNLRDV STSCKLLRCL
GAEVTELGDG QIRISTTNLN EFCAPYDLVK TMRASILILG PLLARYGTAD VSLPGGCAIG
ARPVNLHLHG LEMMGAKIEV KEGYIKARVD GRLKGAHIFM DMVSVGATEN LLMAAALADG
ETVIENAARE PEVIDLANCL IAMGAKITGV GSATLRIQGV ERLQGCEYRV MPDRIETGSF
LVAAAVTRGR IRCLKADPAS LESVIAKLED AGAKITTGED WIELDMEGKR PKAVNIKTAP
YPGFPTDMQA QFCVLNALAQ GTATITETIF ENRFMHVPEL IRMGATMELE GNTCIIQGIE
SLSGAQVMAT DLRASASLVI AGLVADGKTI VDRIYHLDRG YEHIEQKFQG LGAHVERVQ
//
