MURA1_STRPN
ID MURA1_STRPN Reviewed; 427 AA.
AC Q97NQ4;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=SP_1966;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; AE005672; AAK76033.1; -; Genomic_DNA.
DR PIR; H95229; H95229.
DR RefSeq; WP_000358028.1; NZ_AKVY01000001.1.
DR PDB; 5WI5; X-ray; 2.00 A; A/B/C/D=1-427.
DR PDB; 6NKJ; X-ray; 1.30 A; A/B=1-427.
DR PDBsum; 5WI5; -.
DR PDBsum; 6NKJ; -.
DR AlphaFoldDB; Q97NQ4; -.
DR SMR; Q97NQ4; -.
DR STRING; 170187.SP_1966; -.
DR EnsemblBacteria; AAK76033; AAK76033; SP_1966.
DR GeneID; 66807029; -.
DR KEGG; spn:SP_1966; -.
DR eggNOG; COG0766; Bacteria.
DR OMA; CDPHRAT; -.
DR PhylomeDB; Q97NQ4; -.
DR BioCyc; SPNE170187:G1FZB-2020-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000585; 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; Transferase.
FT CHAIN 1..427
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1"
FT /id="PRO_0000178930"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 23..24
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 96
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 125..129
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 309
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 331
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 120
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:6NKJ"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:6NKJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6NKJ"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5WI5"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 374..386
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:6NKJ"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6NKJ"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:6NKJ"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6NKJ"
SQ SEQUENCE 427 AA; 45868 MW; F0E341DAB4B89C2E CRC64;
MDKIVVQGGD NRLVGSVTIE GAKNAVLPLL AATILASEGK TVLQNVPILS DVFIMNQVVG
GLNAKVDFDE EAHLVKVDAT GDITEEAPYK YVSKMRASIV VLGPILARVG HAKVSMPGGC
TIGSRPIDLH LKGLEAMGVK ISQTAGYIEA KAERLHGAHI YMDFPSVGAT QNLMMAATLA
DGVTVIENAA REPEIVDLAI LLNEMGAKVK GAGTETITIT GVEKLHGTTH NVVQDRIEAG
TFMVAAAMTG GDVLIRDAVW EHNRPLIAKL LEMGVEVIEE DEGIRVRSQL ENLKAVHVKT
LPHPGFPTDM QAQFTALMTV AKGESTMVET VFENRFQHLE EMRRMGLHSE IIRDTARIVG
GQPLQGAEVL STDLRASAAL ILTGLVAQGE TVVGKLVHLD RGYYGFHEKL AQLGAKIQRI
EASDEDE
