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Database: UniProt
Entry: A0A0M9ZQT6_9ACTN
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ID   A0A0M9ZQT6_9ACTN        Unreviewed;       509 AA.
AC   A0A0M9ZQT6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=ADK64_05755 {ECO:0000313|EMBL:KOV69222.1};
OS   Streptomyces sp. MMG1121.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV69222.1, ECO:0000313|Proteomes:UP000037687};
RN   [1] {ECO:0000313|Proteomes:UP000037687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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 =
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:KOV69222.1}.
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DR   EMBL; LGDV01000038; KOV69222.1; -; Genomic_DNA.
DR   RefSeq; WP_053655445.1; NZ_LGDV01000038.1.
DR   AlphaFoldDB; A0A0M9ZQT6; -.
DR   STRING; 1415544.ADK64_05755; -.
DR   PATRIC; fig|1415544.3.peg.1211; -.
DR   OrthoDB; 9803760at2; -.
DR   Proteomes; UP000037687; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd00093; HTH_XRE; 1.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_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   Pfam; PF01381; HTH_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS50943; HTH_CROC1; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037687};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOV69222.1}.
FT   DOMAIN          13..67
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   509 AA;  56141 MW;  7438B9F3AB1FC3AC CRC64;
     MADDYLVRIG KLIRDARQHR GWTQAQLAEA LGTSQSAVNR IERGNQNISL EMIARIGEAL
     DSEIVSLGYA GPMHLRVVGG RRLSGAIDVK TSKNACVALL CASLLNKGRT VLRRVARIEE
     VYRLLEVLNS IGVRTRWIND GVDLELVPPA ELEMAAIDAD AAVRTRSIIM FLGPLLHRMD
     SFKLPYAGGC DLGTRTIEPH MIALRRFGLD IAATEGQYHA RVDRAVRPDR PIVLTERGDT
     VTENALLAAA RHDGVTVIRN ASSNYMVQDL CFFLEALGVK VEGIGTTTLT VHGVPNIDVD
     VDYSPSEDPV EAMSLLAAAV VTESELTVRR VPIEFLEIEL AVLEEMGLDH DRSPEYFADN
     GRTRLVDLTV RPSKLEAPID KIHPMPFPGL NIDNVPFFAA IAAVAQGQTL IHDWVYDNRA
     IYLTDLNRLG GRLQLLDPHR VLVEGPTRWR AAEMMCPPAL RPAVVVLLAM MAAEGTSVLR
     NVYVINRGYE DLAERLNSVG AKIDIFRDI
//
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