ID   A0A2M7B544_9BACT        Unreviewed;       421 AA.
AC   A0A2M7B544;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   12-AUG-2020, entry version 8.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000256|HAMAP-Rule:MF_00111,
GN   ECO:0000313|EMBL:PIU98237.1};
GN   ORFNames=COS61_02520 {ECO:0000313|EMBL:PIU98237.1};
OS   Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_40_12.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1975069 {ECO:0000313|EMBL:PIU98237.1, ECO:0000313|Proteomes:UP000228949};
RN   [1] {ECO:0000313|Proteomes:UP000228949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111}.
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|HAMAP-Rule:MF_00111};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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:PIU98237.1}.
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DR   EMBL; PEVJ01000062; PIU98237.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000228949; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
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   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00111};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00111}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00111, ECO:0000313|EMBL:PIU98237.1}.
FT   DOMAIN          7..409
FT                   /note="EPSP_synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   REGION          22..23
FT                   /note="Phosphoenolpyruvate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         93
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         308
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         330
FT                   /note="UDP-N-acetylglucosamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   MOD_RES         117
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   421 AA;  45964 MW;  D2D0BE4FF9A95310 CRC64;
     MAKFIIQGRK PLKGEIKVAG SKNAALKIFP VSLLTKETIR LSNTPEIEDV FRAGEIVTSL
     GGEVKKIKPG VFXXXFKNRR RSALPQDLVS KFRASIMFVG PMLAVDGEAE FPHPGGCVIG
     AGVRPIDMFL DGFKKMGAEI KILDNHYRLT AKKLKGTDIF FPKITVTGTE SLMMTAVLAQ
     GATILKNCAM EPEIARLADF LNSLGAKIEG AGGPTIKIKG VKKLGAGECR IMPDRIEAGT
     FAMLAAASNS GEVVIKNAEP NHLEALWVLL DKIGANYVLY KDRIKISPAK KLFTCDVTTH
     EYPGFATDLQ SPYAVLMTQA EGSSLIHETI YDRRLLFADL LSQMGANVVL CDPHRIVVSG
     PTKLYGRKLV SPDLRAGISL VMAALISDGK TEIDNIYQID RGYERLDERL RQLGADIKRV
     D
//