ID Q84I42_9ACTN Unreviewed; 473 AA. AC Q84I42; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-NOV-2024, entry version 86. 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}; GN Name=sanX {ECO:0000313|EMBL:AAO33462.1}; OS Streptomyces ansochromogenes. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=115647 {ECO:0000313|EMBL:AAO33462.1}; RN [1] {ECO:0000313|EMBL:AAO33462.1} RP NUCLEOTIDE SEQUENCE. RA Li W., Tan H., Chen W.; RT "Cloning, sequencing and function of SanX, a gene related to nikkomycin RT biosynthesis of Streptomyces ansochromogenes."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine. {ECO:0000256|ARBA:ARBA00037534}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + phosphate; 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; AF469956; AAO33462.1; -; Genomic_DNA. DR AlphaFoldDB; Q84I42; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. 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; IPR050068; MurA_subfamily. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR010916; TonB_box_CS. 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. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 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 19..445 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 473 AA; 50383 MW; A5D8EB0D8F37F0F4 CRC64; MQDRRREPAP PGEPLLEIHG GNRLSGAVRT SGFKHSLVTT VAAAATASAP VRIENCPDIV ETAVLGEIFR AAGAHAHYDG AAETFTVDAS AWDRAELPAD LVGRIHGSLY LLPALVSRNG VARLSASGGC PIGEGPRGRP VEHLLDVMGR FGVTTRLTAD GSVDLTAQRL TPCTIDMLDY TRNKALMSGP CYSGAVKTAL LMGAVTHGTT TLKHPYLKPD VTDMVTVLRD LGADIEFAGP ETWVIHGRGP ESLDRPADVT LIPDLIEVVT WICAGVLLAD EPLRITGPGI DRAVHALAPE FDLLDRMGVR VDVGVDEVTA HPLTKPLRPV EFTAMSRGVF SDSQPFLALL GAYAEGPTYI REAVWEHRFG FAPELGALGV RTAVDDTVLR VDGPCPPYRP GTDLHATDLR AAAVLLLAAL TVPGRTTLRN HHHLARGYRD LVEDLVKLGA DIRHTTAPDV RPKPTAGAGV DPA //