MURA_PSEAE
ID MURA_PSEAE Reviewed; 421 AA.
AC Q9HVW7;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; OrderedLocusNames=PA4450;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:5BQ2}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RA Abendroth J., Dranow D.M., Lorimer D.D., Edwards T.E.;
RT "Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase
RT (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas
RT aeruginosa.";
RL Submitted (MAY-2015) to the PDB data bank.
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00111};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR EMBL; AE004091; AAG07838.1; -; Genomic_DNA.
DR PIR; F83089; F83089.
DR RefSeq; NP_253140.1; NC_002516.2.
DR RefSeq; WP_003094332.1; NZ_QZGE01000004.1.
DR PDB; 5BQ2; X-ray; 1.70 A; A/B/C/D=1-421.
DR PDBsum; 5BQ2; -.
DR AlphaFoldDB; Q9HVW7; -.
DR SMR; Q9HVW7; -.
DR STRING; 287.DR97_1628; -.
DR BindingDB; Q9HVW7; -.
DR ChEMBL; CHEMBL1075208; -.
DR DrugCentral; Q9HVW7; -.
DR PaxDb; Q9HVW7; -.
DR PRIDE; Q9HVW7; -.
DR DNASU; 880969; -.
DR EnsemblBacteria; AAG07838; AAG07838; PA4450.
DR GeneID; 880969; -.
DR KEGG; pae:PA4450; -.
DR PATRIC; fig|208964.12.peg.4660; -.
DR PseudoCAP; PA4450; -.
DR HOGENOM; CLU_027387_0_0_6; -.
DR InParanoid; Q9HVW7; -.
DR OMA; CDPHRAT; -.
DR PhylomeDB; Q9HVW7; -.
DR BioCyc; PAER208964:G1FZ6-4538-MON; -.
DR SABIO-RK; Q9HVW7; -.
DR UniPathway; UPA00219; -.
DR PHI-base; PHI:7630; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; -; 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 Pfam; PF00275; EPSP_synthase; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01072; murA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178901"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0007744|PDB:5BQ2"
FT BINDING 93
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 122..126
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:5BQ2"
FT BINDING 165..167
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:5BQ2"
FT BINDING 308
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:5BQ2"
FT BINDING 330
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0007744|PDB:5BQ2"
FT MOD_RES 117
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:5BQ2"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:5BQ2"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:5BQ2"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:5BQ2"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:5BQ2"
SQ SEQUENCE 421 AA; 44646 MW; E1F2E9621974A59F CRC64;
MDKLIITGGN RLDGEIRISG AKNSALPILA ATLLADTPVT VCNLPHLHDI TTMIELFGRM
GVQPIIDEKL NVEVDASSIK TLVAPYELVK TMRASILVLG PMLARFGEAE VALPGGCAIG
SRPVDLHIRG LEAMGAQIEV EGGYIKAKAP AGGLRGGHFF FDTVSVTGTE NLMMAAALAN
GRTVLQNAAR EPEVVDLANC LNAMGANVQG AGSDTIVIEG VKRLGGARYD VLPDRIETGT
YLVAAAATGG RVKLKDTDPT ILEAVLQKLE EAGAHISTGS NWIELDMKGN RPKAVNVRTA
PYPAFPTDMQ AQFISMNAVA EGTGAVIETV FENRFMHVYE MNRMGAQILV EGNTAIVTGV
PKLKGAPVMA TDLRASASLV IAGLVAEGDT LIDRIYHIDR GYECIEEKLQ LLGAKIRRVP
G
