MURA1_BACAN
ID MURA1_BACAN Reviewed; 434 AA.
AC Q81K13; Q6HQL2; Q6KJY6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE Short=EPT 1 {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA1 {ECO:0000255|HAMAP-Rule:MF_00111};
GN OrderedLocusNames=BA_5529, GBAA_5529, BAS5137;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:3SG1}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RG Center for structural genomics of infectious diseases (CSGID);
RT "2.6 Angstrom crystal structure of UDP-N-acetylglucosamine 1-
RT carboxyvinyltransferase 1 (MurA1) from Bacillus anthracis.";
RL Submitted (JUN-2011) 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; AE016879; AAP29173.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34672.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57426.1; -; Genomic_DNA.
DR RefSeq; NP_847687.1; NC_003997.3.
DR RefSeq; WP_000411264.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031376.1; NC_005945.1.
DR PDB; 3SG1; X-ray; 2.60 A; A/B/C/D=1-434.
DR PDBsum; 3SG1; -.
DR AlphaFoldDB; Q81K13; -.
DR SMR; Q81K13; -.
DR STRING; 260799.BAS5137; -.
DR DNASU; 1085196; -.
DR EnsemblBacteria; AAP29173; AAP29173; BA_5529.
DR EnsemblBacteria; AAT34672; AAT34672; GBAA_5529.
DR GeneID; 45025117; -.
DR GeneID; 56655010; -.
DR KEGG; ban:BA_5529; -.
DR KEGG; bar:GBAA_5529; -.
DR KEGG; bat:BAS5137; -.
DR PATRIC; fig|198094.11.peg.5489; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CDPHRAT; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..434
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1"
FT /id="PRO_0000231153"
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 306
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 328
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..6
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 318..329
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3SG1"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:3SG1"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:3SG1"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:3SG1"
SQ SEQUENCE 434 AA; 46773 MW; 0C2E9D8741A59344 CRC64;
MEKIIVRGGK RLNGTVRVEG AKNAVLPIIA AALLASDGKN VLSEVPVLSD VYTINEVLRH
LNAEVVFENN QVTIDASKEL NIEAPFEYVR KMRASVQVMG PLLARNGRAR IALPGGCAIG
SRPIDQHLKG FEAMGAKVQV GNGFVEAYVE GELKGAKIYL DFPSVGATEN IMSAATLAKG
TTILENAAKE PEIVDLANFL NAMGAKVRGA GTGTIRIEGV DKLYGANHSI IPDRIEAGTF
MVAAAITGGD ILIENAVPEH LRSITAKMEE MGVKIIEENE GVRVIGPDKL KAVDIKTMPH
PGFPTDMQSQ MMALLLQADG TSMITETVFE NRFMHVEEFR RMNADIKIEG RSVIMNGPNS
LQGAEVGATD LRAAAALILA GLVSEGYTRV TELKHLDRGY VDFHKKLAAL GATIERVNEK
VEEVKEQEVS DLHA
