ID J9ZCS1_LEPFM Unreviewed; 442 AA.
AC J9ZCS1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN OrderedLocusNames=LFML04_2234 {ECO:0000313|EMBL:AFS54425.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS54425.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS54425.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS54425.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000256|ARBA:ARBA00038367, ECO:0000256|HAMAP-Rule:MF_00111}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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DR EMBL; CP002919; AFS54425.1; -; Genomic_DNA.
DR RefSeq; WP_014961929.1; NC_018649.1.
DR AlphaFoldDB; J9ZCS1; -.
DR STRING; 1048260.LFML04_2234; -.
DR KEGG; lfi:LFML04_2234; -.
DR PATRIC; fig|1048260.3.peg.2431; -.
DR HOGENOM; CLU_027387_0_0_0; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; cd01555; UdpNAET; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR HAMAP; MF_00111; MurA; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR NCBIfam; TIGR01072; murA; 1.
DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR Pfam; PF00275; EPSP_synthase; 2.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00111};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00111};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00111};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00111}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00111}.
FT DOMAIN 8..62
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 98..426
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 113
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 325
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 347
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT MOD_RES 137
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ SEQUENCE 442 AA; 47511 MW; 299F03F850A829DF CRC64;
MDRFHIVGGS PLRGEVIVSG SKNSALPILF SALLGGGLEI SNIPSLRDIR TAFSLLSQLG
IRADPLVSAD PEKTDLTQGI PSHKNDGWPG KYRLLEESIE AHEAPYDLVR TMRASILCLG
PLLARRKRGR VSLPGGCLIG ARPVDIHLNA FVRMGAKISI DHGYIDAHTN GLTGCDIHLP
YPTVTGTENI MMAATLARGT TRIFNAAQEP EVSDLAFSLI ARGARIEGIG TSSIKITGVD
SLLEAPYTVM SDRIEAGTFL VAGALLGEDL MIRNVDVSCL DSLLGTLRDM GADFQEKNGS
VSISRIRKPR GTSARTEPYP GFPTDMQAQI LPLMAIAEGP STVVETVFEN RFTHVMEMNR
MGANIDIHGS RAFVRGGASL EGASVMASDL RASAGLVLAA LIAKGESEIQ RVYHIDRGYE
KIETKLESIG ARIKRVRGEE IS
//
