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Database: UniProt
Entry: A0A1S2QJ12_9ACTN
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ID   A0A1S2QJ12_9ACTN        Unreviewed;       509 AA.
AC   A0A1S2QJ12;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=BIV23_09100 {ECO:0000313|EMBL:OIK06138.1};
OS   Streptomyces monashensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIK06138.1, ECO:0000313|Proteomes:UP000179642};
RN   [1] {ECO:0000313|EMBL:OIK06138.1, ECO:0000313|Proteomes:UP000179642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 1 {ECO:0000313|EMBL:OIK06138.1,
RC   ECO:0000313|Proteomes:UP000179642};
RA   Lee L.-H., Ser H.-L., Law J.W.-F.;
RT   "Genome sequence of Streptomyces sp. MUSC 1.";
RL   Submitted (OCT-2016) 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:OIK06138.1}.
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DR   EMBL; MLYO01000016; OIK06138.1; -; Genomic_DNA.
DR   RefSeq; WP_071380264.1; NZ_MLYO01000016.1.
DR   AlphaFoldDB; A0A1S2QJ12; -.
DR   OrthoDB; 9803760at2; -.
DR   Proteomes; UP000179642; 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: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   CDD; cd00093; HTH_XRE; 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   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:UP000179642};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OIK06138.1}.
FT   DOMAIN          13..67
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   509 AA;  56249 MW;  93F794F302F8CD52 CRC64;
     MSDDYLVRIG KLIRDARQHR GWTQTQLAEA LGTSQSAVNR IERGNQNISL EMIARIGEAL
     DSEIVSLGYA GPMHLRVVGG RRLSGAIDVK TSKNACVALL CASLLNKGRT VLRRVARIEE
     VYRLLEVLNS IGVRTRWIND GVDLELVPPA ELEMAAIDAE AAVRTRSIIM FLGPLLHRMD
     AFKLPYAGGC DLGTRTIEPH MIALRRFGLD IAATEGQYHA RVDRTVRPDR PIVLTERGDT
     VTENALLAAA RHDGVTVIRN ASSNYMVQDL CFFLETLGVK VEGIGTTTLT VHGMPNIDVD
     VDYSPSEDPV EAMSLLAAAV VTESELTVRR VPIEFLEIEL AVLEEMGLDH DRSPEYCADN
     GRTRLVDLTV RPSKLEAPID KIHPMPFPGL NIDNVPFFAA IAATAQGQTL IHDWVYDNRA
     IYLTDLNRLG GRLQLLDPHR VLVEGPTRWR AAEMMCPPAL RPAVVVLLAM MAAEGTSVLR
     NVYVINRGYE DLAERLNSVG AQIEIFRDI
//
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