ID A0A0N0TN58_9PSEU Unreviewed; 504 AA.
AC A0A0N0TN58;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADK67_40470 {ECO:0000313|EMBL:KOX16250.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX16250.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX16250.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX16250.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
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:KOX16250.1}.
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DR EMBL; LGED01000247; KOX16250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0TN58; -.
DR STRING; 1415542.ADK67_40470; -.
DR PATRIC; fig|1415542.3.peg.8703; -.
DR Proteomes; UP000037722; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOX16250.1}.
FT DOMAIN 8..62
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 504 AA; 55128 MW; A37A57249C9DAE8A CRC64;
MTQIGNLIRD SRRHRGWTQA QLATAVSTSQ SAINRIERGN QNLSLEMLSR ISEALDSGIV
SLGQAAPLHL RVTGGRTLSG SITVKTSKNA GVALLCAALL NSGRTTLRKV ARIEEVNRIL
EVLTSIGVRT RWLNDDNDLE IVPPKKLDLG GIDVEAARRT RSIIMMMGPL LHHQDTFELP
YAGGCALGTR TVEPHMVALR PFGLDVKAAA GRYEVAVDRK VGPRRPIVLT ERGDTVTENA
LMAAARHDGV TVIRNASPNY MVQDLCFFLT ELGVRIDGIG TTTLTVHGVE RLDRDVDYAP
SEDPIEAMSL ISAAIVTSSE ITVRRVPIEF MEIELALLEE MGLDYDRSAE YPAANGRTRL
VDVVVRPSAL RAPIDKIHPM PFPGLNIDNL PFFALIAATA HGSTLIHDWV YENRALYLTE
LTKLGGKVAL LDPHRVYVEG PTHWSGAEVI CPPALRPAVV VLLAMLAAKG TSVLRNVYVI
NRGYEQLADR LNQLGAEITT FRDI
//
