MURA1_STRP2
ID MURA1_STRP2 Reviewed; 419 AA.
AC A0A0H2ZNL3;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
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, ECO:0000303|PubMed:23571543};
GN Name=murA1 {ECO:0000303|PubMed:23571543, ECO:0000312|EMBL:ABJ54180.1};
GN Synonyms=murA {ECO:0000255|HAMAP-Rule:MF_00111};
GN OrderedLocusNames=SPD_0967 {ECO:0000312|EMBL:ABJ54180.1};
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153 {ECO:0000312|EMBL:ABJ54180.1};
RN [1] {ECO:0000312|EMBL:ABJ54180.1, ECO:0000312|Proteomes:UP000001452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466 {ECO:0000312|Proteomes:UP000001452};
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2] {ECO:0007744|PDB:3ZH3}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=D39 / NCTC 7466 {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. Involved in heteroresistance to antibiotic fosfomycin.
CC Heteroresistance is the ability of a clonal population to grow one or
CC several subpopulations at a frequency of 10(-7) to 10(-3) in the
CC presence of a higher antibiotic concentration than that predicted to be
CC effective by measurement of the minimum inhibitory concentration (MIC)
CC (PubMed:23571543). {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 -!- DISRUPTION PHENOTYPE: No heteroresistance to fosfomycin.
CC {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; CP000410; ABJ54180.1; -; Genomic_DNA.
DR RefSeq; WP_001227083.1; NC_008533.2.
DR PDB; 3ZH3; X-ray; 2.90 A; A=1-419.
DR PDBsum; 3ZH3; -.
DR AlphaFoldDB; A0A0H2ZNL3; -.
DR SMR; A0A0H2ZNL3; -.
DR STRING; 373153.SPD_0967; -.
DR EnsemblBacteria; ABJ54180; ABJ54180; SPD_0967.
DR KEGG; spd:SPD_0967; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CRFGQRN; -.
DR OrthoDB; 537477at2; -.
DR BioCyc; SPNE373153:G1G6V-1059-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001452; 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:0071236; P:cellular response to antibiotic; IMP:UniProtKB.
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_0000436448"
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 2..8
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:3ZH3"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:3ZH3"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:3ZH3"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:3ZH3"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:3ZH3"
SQ SEQUENCE 419 AA; 45025 MW; 5717D819B16DF8E3 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
LRGASVKATD LRAGAALVIA GLMAEGKTEI TNIEFILRGY SDIIEKLRNL GADIRLVED
