ID U1LRP5_9MICO Unreviewed; 453 AA.
AC U1LRP5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=L332_09820 {ECO:0000313|EMBL:ERG64742.1};
OS Agrococcus pavilionensis RW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG64742.1, ECO:0000313|Proteomes:UP000016462};
RN [1] {ECO:0000313|EMBL:ERG64742.1, ECO:0000313|Proteomes:UP000016462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW1 {ECO:0000313|EMBL:ERG64742.1,
RC ECO:0000313|Proteomes:UP000016462};
RX PubMed=23814108;
RA White R.A.III., Grassa C.J., Suttle C.A.;
RT "First draft genome sequence from a member of the genus agrococcus,
RT isolated from modern microbialites.";
RL Genome Announc. 1:e00391-13(2013).
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000256|ARBA:ARBA00037534, ECO:0000256|HAMAP-
CC 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}.
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:ERG64742.1}.
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DR EMBL; ASHR01000016; ERG64742.1; -; Genomic_DNA.
DR AlphaFoldDB; U1LRP5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000016462; Unassembled WGS sequence.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000016462};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00111}.
FT DOMAIN 23..442
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 39..40
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT BINDING 111
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 135
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ SEQUENCE 453 AA; 48730 MW; 7E9377F7B9DA8F2A CRC64;
MNLTEFSKSA GAAVGMNVDR ITVRGGKPLQ GRIQMKGAKN LVTKAMVAAL LGESPSELRS
VPEISDVRVV QGLLELHGVT VERDGDTLRL DPANVRTAHE TSINAHAGSS RIPILFCGPL
LHQLGEAFIP DLGGCHIGDR PIDYHLEVLR NFGAVVEKLP SGIRMSAPNG LHGAKIHLPY
PSVGATEQVL LGAVRAKGRT ELTGAAVEPE IMDLIAILQK MGAEIQVDTD RTIRIEGVDK
LVGYRHTALF DRNEAASWAC AALATGGDVF LEGARQPEMT TFLNVFRKAG GAFEIEDDGI
RFWHPGGDLK PVVVETDVHP GFMTDWQQPL VVALAKANGI SIVHETVYEQ RFGFTEALVE
MGARIQIHTD CLGSHACRFG QRNYEHSAVI AGPVELHGAD VVVPDLRGGF SHLVAALTAE
GTSRISNVGI IARGYERFIE KLETLGADFD VEG
//
