ID A0A3N0VG45_9GAMM Unreviewed; 416 AA.
AC A0A3N0VG45;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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 ORFNames=ED208_04550 {ECO:0000313|EMBL:ROH91664.1};
OS Stagnimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stagnimonas.
OX NCBI_TaxID=2689987 {ECO:0000313|EMBL:ROH91664.1, ECO:0000313|Proteomes:UP000282106};
RN [1] {ECO:0000313|EMBL:ROH91664.1, ECO:0000313|Proteomes:UP000282106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THS-13 {ECO:0000313|EMBL:ROH91664.1,
RC ECO:0000313|Proteomes:UP000282106};
RA Chen W.-M.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROH91664.1}.
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DR EMBL; RJVO01000002; ROH91664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0VG45; -.
DR InParanoid; A0A3N0VG45; -.
DR Proteomes; UP000282106; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:InterPro.
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 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 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000282106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ROH91664.1}.
FT DOMAIN 8..407
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
SQ SEQUENCE 416 AA; 44775 MW; D5DD17F91E7600D6 CRC64;
MKTVSIEKSR LNGTVEISGA KNSALRLLAA TILTDEKVVL NNYPSNILDA QIHVGMLNAL
GKSHVLHGQD QIEIQQSAPL ISTLEWQDRS IRNTLLILGA LVAKTGHGAV PLPGGCKLGE
RAYDLHVMLL EKLGARVWET ENELLAEAPK GGLVGADIHL PIRSTGATEN AILAGSLARG
ITRVWNPHVR PEIMDLIAML TKMGAKITVY GQEHIEIVGV EGLTGVSHSV IPDNMEAITW
LVASVMTQGD IEMINFPHQD LEVPLIHLRD SGARFYRGED RMIVRGGRCL PLEISTGPHP
GINSDVQPIL AAYAACARGE SKIIDLRFPG RYGYADEMAK MGVASVTDGN ILRIQGNGGR
MSGATVRALD LRAGAALTLC GMVADGVTTV TDSWQIERGY NDFWSKLRAM GGVIHA
//
