MURA1_LISMO
ID MURA1_LISMO Reviewed; 430 AA.
AC Q8Y4C4;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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}; Synonyms=murA;
GN OrderedLocusNames=lmo2526;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0007744|PDB:3R38}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
RG Center for structural genomics of infectious diseases (CSGID);
RT "2.23 Angstrom resolution crystal structure of UDP-N-acetylglucosamine 1-
RT carboxyvinyltransferase (murA) from Listeria monocytogenes EGD-e.";
RL Submitted (MAR-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; AL591983; CAD00604.1; -; Genomic_DNA.
DR PIR; AF1390; AF1390.
DR RefSeq; NP_466049.1; NC_003210.1.
DR RefSeq; WP_003723459.1; NZ_CP023861.1.
DR PDB; 3R38; X-ray; 2.23 A; A=1-430.
DR PDBsum; 3R38; -.
DR AlphaFoldDB; Q8Y4C4; -.
DR SMR; Q8Y4C4; -.
DR STRING; 169963.lmo2526; -.
DR PaxDb; Q8Y4C4; -.
DR EnsemblBacteria; CAD00604; CAD00604; CAD00604.
DR GeneID; 984514; -.
DR KEGG; lmo:lmo2526; -.
DR PATRIC; fig|169963.11.peg.2587; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CDPHRAT; -.
DR PhylomeDB; Q8Y4C4; -.
DR BioCyc; LMON169963:LMO2526-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000817; 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..430
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1"
FT /id="PRO_0000178887"
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:0000250|UniProtKB:P0A749"
FT BINDING 93
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 122..126
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 305
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 327
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
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:3R38"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:3R38"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:3R38"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:3R38"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:3R38"
SQ SEQUENCE 430 AA; 45979 MW; F73905754D13BFB9 CRC64;
MEKIIVRGGK QLNGSVKMEG AKNAVLPVIA ATLLASKGTS VLKNVPNLSD VFTINEVLKY
LNADVSFVND EVTVDATGEI TSDAPFEYVR KMRASIVVMG PLLARTGSAR VALPGGCAIG
SRPVDLHLKG FEAMGAVVKI ENGYIEATAE KLVGAKVYLD FPSVGATQNI MMAATLAEGT
TVIENVAREP EIVDLANFLN QMGARVIGAG TEVIRIEGVK ELTATEHSII PDRIEAGTFM
IAAAITGGNV LIEDAVPEHI SSLIAKLEEM GVQIIEEENG IRVIGPDKLK AVDVKTMPHP
GFPTDMQSQM MVIQMLSEGT SIMTETVFEN RFMHVEEMRR MNADMKIEGH SVIISGPAKL
QGAEVAATDL RAAAALILAG LVADGYTQVT ELKYLDRGYN NFHGKLQALG ADVERVDDSK
VDVTNLASLF
