ID A7XYN8_CHLTH Unreviewed; 185 AA. AC A7XYN8; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 29-MAY-2024, entry version 53. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00039754}; DE EC=2.5.1.7 {ECO:0000256|ARBA:ARBA00039108}; DE AltName: Full=Enoylpyruvate transferase {ECO:0000256|ARBA:ARBA00042443}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|ARBA:ARBA00042842}; DE Flags: Fragment; GN Name=murA {ECO:0000313|EMBL:ABV03243.1}; GN ORFNames=CT455 {ECO:0000313|EMBL:ABV03243.1}; OS Chlamydia trachomatis. OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=813 {ECO:0000313|EMBL:ABV03243.1}; RN [1] {ECO:0000313|EMBL:ABV03243.1} RP NUCLEOTIDE SEQUENCE. RA DeMars R.I., Weinfurter J.T.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABV03243.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18083799; DOI=10.1128/JB.01592-07; RA DeMars R., Weinfurter J.; RT "Interstrain gene transfer in Chlamydia trachomatis in vitro: mechanism and RT significance."; RL J. Bacteriol. 190:1605-1614(2008). 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:0000256|ARBA:ARBA00036669}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000256|ARBA:ARBA00038367}. 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; EU105039; ABV03243.1; -; Genomic_DNA. DR AlphaFoldDB; A7XYN8; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:TreeGrafter. 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-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. 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 {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..183 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABV03243.1" FT NON_TER 185 FT /evidence="ECO:0000313|EMBL:ABV03243.1" SQ SEQUENCE 185 AA; 20167 MW; E36F3E3724E62BDB CRC64; KKLGAEIVIS DEGYWASAPN GLVGAHITLP YPSVGATENL ILASVGAQGR TIIKNAALEV EIIDLIVFLQ KAGVEITTDN DKTIEIFGCQ DFYSVEHFII PDKIEAASFG MAAVVSQGRI FVEQARHEHM IPFLKVLRSI GGGFSVHENG IEFFYDKPLK GGVLLETDVH PGFITDWQQP FAVLL //