ID A0A0G0TD69_9BACT Unreviewed; 438 AA.
AC A0A0G0TD69;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=UU18_C0017G0006 {ECO:0000313|EMBL:KKR74869.1};
OS Parcubacteria group bacterium GW2011_GWB2_40_8.
OC Bacteria.
OX NCBI_TaxID=1618890 {ECO:0000313|EMBL:KKR74869.1, ECO:0000313|Proteomes:UP000034552};
RN [1] {ECO:0000313|EMBL:KKR74869.1, ECO:0000313|Proteomes:UP000034552}
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:KKR74869.1}.
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DR EMBL; LBZQ01000017; KKR74869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0TD69; -.
DR Proteomes; UP000034552; Unassembled WGS sequence.
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: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 6..420
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
SQ SEQUENCE 438 AA; 48765 MW; 52233A18B193F895 CRC64;
MHSYVVNGGK KLKGSIAVNP SKNASIAILI ASLLNEKETV IKNLPKIEEV FRVIEVIESL
GARTEWKDDH VFKITPPKEI TLKNLNVEAA LKTRIMILLI GVLAHKFKNF SLPFSGGCKL
GRRTIMPHIY ALENFGVNIK VSKDKYEVSH NGLKSCDNVI MYESGDTATE NAILAASMIE
GKTVLKFASA NYQVQDVCFF LKKLGVRFEG IGGTTLTIHG KKSLSKKIDF SITEDPIEAM
FFISTAIVTK SSIVIKRCPI EFLELELFKL KKMGFKFNMS EEYKSENGYS RLVDIETFPS
NLSAPCEKIY GRPFPGLNID NLPFFAPIAT QAKGETLVHD WVFENRAIYF MELGKMGANV
TLADPHRVFI KGPVKLKPAD IVSIPALRPS AIMLVAMLGA KGKSILRNVY IIERGYEDLC
GRLKSIGADI ERVTNDKY
//
