MURA2_ALKCK
ID MURA2_ALKCK Reviewed; 428 AA.
AC Q5WB48;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=Enoylpyruvate transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE Short=EPT 2 {ECO:0000255|HAMAP-Rule:MF_00111};
GN Name=murA2 {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ;
GN OrderedLocusNames=ABC3881;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD66412.1; -; Genomic_DNA.
DR RefSeq; WP_011248715.1; NC_006582.1.
DR AlphaFoldDB; Q5WB48; -.
DR SMR; Q5WB48; -.
DR STRING; 66692.ABC3881; -.
DR EnsemblBacteria; BAD66412; BAD66412; ABC3881.
DR KEGG; bcl:ABC3881; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_9; -.
DR OMA; CRFGQRN; -.
DR OrthoDB; 537477at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001168; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..428
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2"
FT /id="PRO_0000231160"
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:0000255|HAMAP-Rule:MF_00111"
FT BINDING 92
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 121..125
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 304
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 326
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 116
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ SEQUENCE 428 AA; 45956 MW; FDAE3BDC2B65CEDA CRC64;
MQKLLIEGGH TLEGTVSISG AKNSAVALIP AAILADSAVV IDNLPVISDV DLLAELLREI
GGDVDLGNQT MTIHPEKMVA MPLPNGRVKK LRASYYLMGA MLGKFKKAVI GLPGGCNLGP
RPIDQHIKGF EALGAQVTNE QGAIYLRANE LRGAKIYLDV VSVGATINIM LAAVRAKGRT
IIENAAKEPE IIDVATLLTS MGAKIKGAGT NVIRIDGVDH LQGCRHSIIP DRIEAGTYMI
MAAAMGRRVH IDNVIPTHLE SVTAKLREMG TTVEEYDDQL IISGMDPKKG VDIKTLVYPG
FPTDLQQPFT SLLTSAEGTS IVTDTIYDAR FKHVDELRRM GASVKVEGRS SIVNGKSSLQ
GAKVKASDLR AGAALVIAGL MAEGITEVSG LEHIDRGYEH LETKLTRLGA KVWREELTEE
ELEQVKQS
