ID A0A0G0BJ00_9BACT Unreviewed; 417 AA.
AC A0A0G0BJ00;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=UR21_C0018G0013 {ECO:0000313|EMBL:KKP31022.1};
OS Candidatus Woesebacteria bacterium GW2011_GWC2_31_9.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618586 {ECO:0000313|EMBL:KKP31022.1, ECO:0000313|Proteomes:UP000034803};
RN [1] {ECO:0000313|EMBL:KKP31022.1, ECO:0000313|Proteomes:UP000034803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP31022.1}.
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; LBOI01000018; KKP31022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0BJ00; -.
DR PATRIC; fig|1618586.3.peg.828; -.
DR Proteomes; UP000034803; 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 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 {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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKP31022.1}.
FT DOMAIN 7..406
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
SQ SEQUENCE 417 AA; 45735 MW; B49C450A85A20DCE CRC64;
MAKFLIKGGN KLEGEIKLSG NKNSALKLIP ACLASTEKSV LTNVPDISDV RVILQIIEKL
GAKVTFEKNV VEIDPSGLNS FEPDSDLCAK LRASVVLAAP LLVRFGRAVI TPPGGDQIGD
RLLDTHFNLM QKLGVNFERK DGKFYLSWDK RLSGRVFLEE ASVTATEMGL IMASSMNEEV
IIEDAAAEPH VEDLAKFLCK MGAKISGIGT NTLVCSGGNL HGAEHKVMPD HIEGGTFAIA
SAITGGKVKI NDFNINNYHM ILNYLGNMGI KYEIEKESLV ILPSKLKAQR RKFQTRPWPG
FPTDLMSPFI VLATQTEGTI LCHDWMYEWR MFFVDDLIGM GANILIADPH RVIVSGPTKL
ISDRLFCKDI RAGISVILAA MVAEGTSTIE NVEVVNRGYE DIQNRLTSLG ASIKRED
//
