ID A0A1E5PXH8_9ACTN Unreviewed; 509 AA.
AC A0A1E5PXH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BGK67_25440 {ECO:0000313|EMBL:OEJ34235.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ34235.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ34235.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ34235.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-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:OEJ34235.1}.
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DR EMBL; MEHK01000001; OEJ34235.1; -; Genomic_DNA.
DR RefSeq; WP_069922428.1; NZ_MEHK01000001.1.
DR AlphaFoldDB; A0A1E5PXH8; -.
DR STRING; 36818.BGK67_25440; -.
DR OrthoDB; 9803760at2; -.
DR Proteomes; UP000095705; 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:UP000095705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEJ34235.1}.
FT DOMAIN 13..67
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 509 AA; 56168 MW; A4ECC2789E86D043 CRC64;
MADDYLVRIG KLIRDARQHR GWTQSQLADA LGTSQSAVNR IERGNQNISL EMIARIGEAL
DSEIVSLGYA GPMHLRVVGG RRLSGAIDVK TSKNACVALL CASLLNKGRT VLRRVARIEE
VYRLLEVLGS IGVRTRWIND GVDLELIPPA RLDMESMDAD AARRTRSIIM FLGPLLHRMD
QFRLPYAGGC DLGTRTIEPH MIALRRFGLD ITATEGIYHA RVATGVSPDR PIVLTERGDT
VTENALLAAA RHDGVTVIRN ASSNYMVQDL CFFLEALGVK VEGIGTTTLT VHGIPNIDVD
VDYCPSEDPV EAMSLLAAAV VTESELTIRR VPIEFMEIEL AVLEEMGLDH DRSAEYSADN
GRTRLVDLTV RPSKLEAPID KIHPMPFPGL NIDNVPFFAA IAAVAQGQTL IHDWVYDNRA
IYLTDLNRLG GRLQLLDPHR VLVEGPTRWR AAEMMCPPAL RPAVVVLLAM MAAEGTSVLR
NVYVINRGYE ELAERLNSVG AQIEIFRDI
//
