MURA_PSEPK
ID MURA_PSEPK Reviewed; 421 AA.
AC Q88P88;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=PP_0964;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66589.1; -; Genomic_DNA.
DR RefSeq; NP_743125.1; NC_002947.4.
DR RefSeq; WP_003255119.1; NC_002947.4.
DR PDB; 6CN1; X-ray; 2.75 A; A/B/C/D/E/F/G/H=1-421.
DR PDBsum; 6CN1; -.
DR AlphaFoldDB; Q88P88; -.
DR SMR; Q88P88; -.
DR STRING; 160488.PP_0964; -.
DR EnsemblBacteria; AAN66589; AAN66589; PP_0964.
DR KEGG; ppu:PP_0964; -.
DR PATRIC; fig|160488.4.peg.1026; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OMA; CDPHRAT; -.
DR PhylomeDB; Q88P88; -.
DR BioCyc; PPUT160488:G1G01-1038-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000556; 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; -; 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_0000178903"
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:0000255|HAMAP-Rule:MF_00111"
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:0000255|HAMAP-Rule:MF_00111"
FT BINDING 308
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 330
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
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:6CN1"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:6CN1"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:6CN1"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:6CN1"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:6CN1"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6CN1"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:6CN1"
SQ SEQUENCE 421 AA; 44973 MW; A7427A6554F1A164 CRC64;
MDKLIITGGA RLDGEIRISG AKNAALPILA ATLLADGPVT VGNLPHLHDI TTMIELFGRM
GIEPVIDEKL SVEIDPRTIK TLVAPYELVK TMRASILVLG PMVARFGEAE VALPGGCAIG
SRPVDLHIRG LEAMGAKIEV EGGYIKAKAP EGGLRGAHFF FDTVSVTGTE NIMMAAALAK
GRSVLQNAAR EPEVVDLANF INAMGGNIQG AGTDTITIDG VERLDSANYR VMPDRIETGT
YLVAAAVTGG RVKVKDTDPT ILEAVLEKLK EAGADINTGE DWIELDMHGK RPKAVNLRTA
PYPAFPTDMQ AQFISLNAIA EGTGAVIETI FENRFMHVYE MHRMGAQIQV EGNTAIVTGV
KALKGAPVMA TDLRASASLV LSALVAEGDT LIDRIYHIDR GYECIEEKLQ MLGAKIRRVP
G
