MURA1_STRPI
ID MURA1_STRPI Reviewed; 419 AA.
AC B1IBM3;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Short=EPT {ECO:0000305};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA1 {ECO:0000312|EMBL:ACA37082.1};
GN Synonyms=murA {ECO:0000255|HAMAP-Rule:MF_00111};
GN OrderedLocusNames=SPH_1173 {ECO:0000312|EMBL:ACA37082.1};
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214 {ECO:0000312|EMBL:ACA37082.1};
RN [1] {ECO:0000312|Proteomes:UP000002163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6 {ECO:0000312|Proteomes:UP000002163};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
RN [2] {ECO:0007744|PDB:3ZH4}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, AND MISCELLANEOUS.
RC STRAIN=Hungary19A-6 {ECO:0000303|PubMed:23571543};
RX PubMed=23571543; DOI=10.1128/aac.00223-13;
RA Engel H., Gutierrez-Fernandez J., Fluckiger C., Martinez-Ripoll M.,
RA Muhlemann K., Hermoso J.A., Hilty M., Hathaway L.J.;
RT "Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae
RT and depends on the murA1 gene.";
RL Antimicrob. Agents Chemother. 57:2801-2808(2013).
CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine (By similarity). Target for the antibiotic
CC fosfomycin. {ECO:0000255|HAMAP-Rule:MF_00111,
CC ECO:0000269|PubMed:23571543}.
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 -!- MISCELLANEOUS: This strain of S.pneumoniae has no heteroresistance to
CC fosfomycin unlike other strains of this bacterium in which MurA1 is
CC required for heteroresistance along with other as yet unknown
CC factor(s). Heteroresistance is the ability of a clonal population to
CC grow one or several subpopulations at a frequency of 10(-7) to 10(-3)
CC in the presence of a higher antibiotic concentration than that
CC predicted to be effective by measurement of the minimum inhibitory
CC concentration (MIC). {ECO:0000269|PubMed:23571543}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR EMBL; CP000936; ACA37082.1; -; Genomic_DNA.
DR RefSeq; WP_001227085.1; NC_010380.1.
DR PDB; 3ZH4; X-ray; 1.80 A; A=1-419.
DR PDBsum; 3ZH4; -.
DR AlphaFoldDB; B1IBM3; -.
DR SMR; B1IBM3; -.
DR EnsemblBacteria; ACA37082; ACA37082; SPH_1173.
DR GeneID; 66806189; -.
DR KEGG; spv:SPH_1173; -.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CRFGQRN; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002163; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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; Transferase.
FT CHAIN 1..419
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000436447"
FT ACT_SITE 116
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 92
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 121..125
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 306
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT BINDING 328
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0A749"
FT MOD_RES 116
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:3ZH4"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3ZH4"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:3ZH4"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:3ZH4"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:3ZH4"
SQ SEQUENCE 419 AA; 45055 MW; A217CD0CB16DF8F9 CRC64;
MRKIVINGGL PLQGEITISG AKNSVVALIP AIILADDVVT LDCVPDISDV ASLVEIMELM
GATVKRYDDV LEIDPRGVQN IPMPYGKINS LRASYYFYGS LLGRFGEATV GLPGGCDLGP
RPIDLHLKAF EAMGATASYE GDNMKLSAKD TGLHGASIYM DTVSVGATIN TMIAAVKANG
RTIIENAARE PEIIDVATLL NNMGAHIRGA GTNIIIIDGV ERLHGTRHQV IPDRIEAGTY
ISLAAAVGKG IRINNVLYEH LEGFIAKLEE MGVRMTVSED SIFVEEQSNL KAINIKTAPY
PGFATDLQQP LTPLLLRANG RGTIVDTIYE KRVNHVFELA KMDADISTTN GHILYTGGRD
LRGTSVKATD LRAGAALVIA GLMAEGKTEI TNIEFILRGY SDIIEKLRNL GADIRLVED
