MURA1_STAAM
ID MURA1_STAAM Reviewed; 421 AA.
AC Q931H5; Q931H4; Q99SF8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=SAV2099;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=15141945; DOI=10.1093/dnares/11.1.51;
RA Ohta T., Hirakawa H., Morikawa K., Maruyama A., Inose Y., Yamashita A.,
RA Oshima K., Kuroda M., Hattori M., Hiramatsu K., Kuhara S., Hayashi H.;
RT "Nucleotide substitutions in Staphylococcus aureus strains, Mu50, Mu3, and
RT N315.";
RL DNA Res. 11:51-56(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000017; BAB58261.2; -; Genomic_DNA.
DR RefSeq; WP_000358006.1; NC_002758.2.
DR AlphaFoldDB; Q931H5; -.
DR SMR; Q931H5; -.
DR World-2DPAGE; 0002:Q931H5; -.
DR PaxDb; Q931H5; -.
DR EnsemblBacteria; BAB58261; BAB58261; SAV2099.
DR KEGG; sav:SAV2099; -.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CDPHRAT; -.
DR PhylomeDB; Q931H5; -.
DR BioCyc; SAUR158878:SAV_RS11490-MON; -.
DR SABIO-RK; Q931H5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002481; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase.
FT CHAIN 1..421
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1"
FT /id="PRO_0000178916"
FT ACT_SITE 119
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 95
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 124..128
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 308
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 330
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 119
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ SEQUENCE 421 AA; 44996 MW; 1365C4EF6C9683CB CRC64;
MDKIVIKGGN KLTGEVKVEG AKNAVLPILT ASLLASDKPS KLVNVPALSD VETINNVLTT
LNADVTYKKD ENAVVVDATK TLNEEAPYEY VSKMRASILV MGPLLARLGH AIVALPGGCA
IGSRPIEQHI KGFEALGAEI HLENGNIYAN AKDGLKGTSI HLDFPSVGAT QNIIMAASLA
KGKTLIENAA KEPEIVDLAN YINEMGGRIT GAGTDTITIN GVESLHGVEH AIIPDRIEAG
TLLIAGAITR GDIFVRGAIK EHMASLVYKL EEMGVELDYQ EDGIRVRAEG ELQPVDIKTL
PHPGFPTDMQ SQMMALLLTA NGHKVVTETV FENRFMHVAE FKRMNANINV EGRSAKLEGK
SQLQGAQVKA TDLRAAAALI LAGLVADGKT SVTELTHLDR GYVDLHGKLK QLGADIERIN
D
