MURA_STRMK
ID MURA_STRMK Reviewed; 423 AA.
AC B2FRX1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Smlt1119;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44676.1; -; Genomic_DNA.
DR RefSeq; WP_005408397.1; NC_010943.1.
DR PDB; 6WFM; X-ray; 1.95 A; A/B=1-423.
DR PDBsum; 6WFM; -.
DR AlphaFoldDB; B2FRX1; -.
DR SMR; B2FRX1; -.
DR STRING; 522373.Smlt1119; -.
DR EnsemblBacteria; CAQ44676; CAQ44676; Smlt1119.
DR KEGG; sml:Smlt1119; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OMA; CDPHRAT; -.
DR OrthoDB; 537477at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008840; 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..423
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_1000094727"
FT ACT_SITE 122
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 98
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 127..131
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 333
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 122
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:6WFM"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:6WFM"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:6WFM"
SQ SEQUENCE 423 AA; 44487 MW; 5710F1222D07C741 CRC64;
MAKIVVTGGA ALHGEVSISG AKNAVLPILC ATLLADEPVE ITNVPHLHDV VTTVKLLGEL
GAKVTIDQGT LSRGSAIVVD PRPVNQHVAP YELVKTMRAS ILVLGPLLAR FGAAEVSLPG
GCAIGSRPVD QHIKGLQALG AEIVVENGFI KASAKRLKGG HFTFDMVSVT GTENVLMGAV
LAEGTTVLDN CAMEPEVTDL AHCLIALGAK IEGLGTARLV IEGVERLSGG RHEVLPDRIE
TGTFLVAAAM TGGKVTVNRA RPNTMDAVLS KLVEAGAKIE TTDDSITLDM QGRRPKAVNL
TTAPYPAFPT DMQAQFMALN CVADGVGVIN ETIFENRFMH VNELLRLGAD IQVEGHTAIV
RGSEHLSGAP VMATDLRASA SLILAGLMAS GDTTIDRIYH LDRGYENIEE KLSSLGATIR
RVP
