ID A0A3M0GC15_9ACTN Unreviewed; 513 AA.
AC A0A3M0GC15;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=EAX62_10640 {ECO:0000313|EMBL:RMB60142.1};
OS Tessaracoccus antarcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2479848 {ECO:0000313|EMBL:RMB60142.1, ECO:0000313|Proteomes:UP000275256};
RN [1] {ECO:0000313|EMBL:RMB60142.1, ECO:0000313|Proteomes:UP000275256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDX10 {ECO:0000313|EMBL:RMB60142.1,
RC ECO:0000313|Proteomes:UP000275256};
RA Zhou L.Y., Du Z.J.;
RT "Tessaracoccus antarcticuss sp. nov., isolated from sediment.";
RL Submitted (OCT-2018) 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:RMB60142.1}.
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DR EMBL; REFW01000002; RMB60142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0GC15; -.
DR OrthoDB; 9803760at2; -.
DR Proteomes; UP000275256; 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:UniProtKB-EC.
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:UP000275256};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RMB60142.1}.
FT DOMAIN 12..66
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 513 AA; 56406 MW; AF1ED1E80C4464F3 CRC64;
MSTTSQAIGT MIRDGRVARG WSQQRLADEL GTAQSAVHRI ENGQQNLSLS MIDRLADALD
MPLIHTATEG KLNFQITGPT KLSGDIAVRT SKNAAVALLC ASLLNRGTTV LRGIARIEEV
DRICEVLTSI GVTMKWIGDR SQDLEIRRPE VLTPATINQR AARRTRSILM FLGPLMHDFD
TFELPYAGGC DLGARTVHPH MSALRRFGLG VEATDGQYQA SVDKCTLSER HITLVERGDT
VTENALMAAA RTEGVSVLRN ASGNYMVQDL CFFLQKLGVR IEGIGTTTLR VEGVKNIDVD
VEYFISEDPI EAMSLLTAGI VTNSEITVRR CPIEFLEVEI AVLEEMGQQM EMSAEYTSNN
GCTRLVDVTV KPSKLVAPLD KIHPMPFPGL NIDNLPFFAV ICATAEGQSV IYDWVYDNRA
IHLKKLADFG ANVQLMDAHR LLIIGPTRWR GRNIECPPAL RPAVCLLLAA MASRGTTNLL
DVYVINRGYE DLPQRLNALG ANINVFWGEP NAD
//
