ID A0A3M9M0J1_9MICO Unreviewed; 510 AA.
AC A0A3M9M0J1;
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=EFY87_17720 {ECO:0000313|EMBL:RNI18393.1};
OS Flexivirga caeni.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Flexivirga.
OX NCBI_TaxID=2294115 {ECO:0000313|EMBL:RNI18393.1, ECO:0000313|Proteomes:UP000271678};
RN [1] {ECO:0000313|EMBL:RNI18393.1, ECO:0000313|Proteomes:UP000271678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BO-16 {ECO:0000313|EMBL:RNI18393.1,
RC ECO:0000313|Proteomes:UP000271678};
RA Im W.T.;
RT "Draft genome of Simplicispira Flexivirga sp. BO-16.";
RL Submitted (NOV-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:RNI18393.1}.
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DR EMBL; RJJQ01000022; RNI18393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9M0J1; -.
DR OrthoDB; 9803760at2; -.
DR Proteomes; UP000271678; 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:UP000271678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RNI18393.1}.
FT DOMAIN 13..67
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 510 AA; 56120 MW; F72EDDCFBF5E55DC CRC64;
MTDDYLSRVG TLIRDARRHK KLTQSELAEA LQTSQSAVAR IEQGKQNLSL ETLARISEAL
DTEVVAVASS TPLNLRIKGG RKLSGEIDVR TSKNAAVACL CAALLNKGKT TLRNLARIEE
VNRITEVLAS IGVKTRWLPD SSDLEITPPA VLDLDAMDET AARRTRTILM FLGPLLHQFG
EFQLPNAGGC DLGSRTVEPH LFALRAFGLD VVASHGYYHA KVDSSVRPSK PIILTERGDT
VTENALFAAA LYDGETVIHN ASPNYMVQDL CFMLEKFGVR IDGVGTTTLR VHGVQEINKD
VEYHPSEDPI EAMTLVAAAV VTESEITIRR VPIEFMEIEL TLLEGMGMKY DIEGDEYVSA
NGKTRLIDIT TKPGPLKAPK DKIHPMPFPG LNIDNLPFFA VIAAYAQGTT TLHDWVYENR
AIYLTELNAL GARVQLMDPH RVMIQGPTKW RAAEVMSPPA LRPAVVILLG MLAAPGVSVL
RNIYVIDRGY EELDTRLNKL GADIQTFRDI
//
