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Database: UniProt
Entry: A0A101R1T5_9ACTN
LinkDB: A0A101R1T5_9ACTN
Original site: A0A101R1T5_9ACTN 
ID   A0A101R1T5_9ACTN        Unreviewed;       509 AA.
AC   A0A101R1T5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=AQJ30_05460 {ECO:0000313|EMBL:KUN40130.1};
OS   Streptomyces longwoodensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN40130.1, ECO:0000313|Proteomes:UP000053271};
RN   [1] {ECO:0000313|EMBL:KUN40130.1, ECO:0000313|Proteomes:UP000053271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN40130.1,
RC   ECO:0000313|Proteomes:UP000053271};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT   for the species Streptomyces longwoodensis.";
RL   Submitted (OCT-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:KUN40130.1}.
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DR   EMBL; LMWS01000008; KUN40130.1; -; Genomic_DNA.
DR   RefSeq; WP_067229280.1; NZ_KQ948550.1.
DR   AlphaFoldDB; A0A101R1T5; -.
DR   STRING; 68231.AQJ30_05460; -.
DR   Proteomes; UP000053271; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053271};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUN40130.1}.
FT   DOMAIN          13..67
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   509 AA;  56156 MW;  C38E706F36C12C10 CRC64;
     MSDDYLVRIG KLIRDARQHR GWTQTQLAEA LGTSQSAVNR IERGNQNISL EMIARIGEAL
     DSEIVSLGYA GPMHLRVVGG RRLSGAIDVK TSKNACVALL CASLLNTGRT VLRRVARIEE
     VYRLLEVLNS IGVRTRWISD GVDLEIVPPA DLNLAAIDAE AAVRTRSIIM FLGPLLHRMD
     RFMLPYAGGC DLGTRTIEPH MIALRRFGLE VAATEGQYHA VVDRSVRPDR PIVLTERGDT
     VTENALLAAA RHDGVTVIRN ASSNYMVQDL CFFLEALGVE VEGIGTTTLT VHGVPRIDVD
     VDYSPSEDPV EAMSLVAAAV VTESELTVRR VPIEFLEIEL AVLEEMGLDH DRTPEYVADN
     GRTRLVDLTV RPSKLEAPID KIHPMPFPGL NIDNVPFFAA IAATAQGQTL IHDWVYDNRA
     IYLTDLNRLG GRLQLLDPHR VLVEGPTRWR AAEMMCPPAL RPAVVVLLAM MAAEGTSVLR
     NVYVINRGYE DLAERLNSIG AQIEIFRDI
//
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