MURD2_XANOR
ID MURD2_XANOR Reviewed; 468 AA.
AC Q5H2Y1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208};
DE EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
DE Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
GN Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208}; OrderedLocusNames=XOO1436;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC EC=6.3.2.53; Evidence={ECO:0000255|HAMAP-Rule:MF_02208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
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DR EMBL; AE013598; AAW74690.1; -; Genomic_DNA.
DR RefSeq; WP_011258236.1; NC_006834.1.
DR AlphaFoldDB; Q5H2Y1; -.
DR SMR; Q5H2Y1; -.
DR STRING; 291331.XOO1436; -.
DR EnsemblBacteria; AAW74690; AAW74690; XOO1436.
DR KEGG; xoo:XOO1436; -.
DR HOGENOM; CLU_032540_4_1_6; -.
DR OMA; KGMHNVE; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
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 Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00639; MurD; 1.
DR HAMAP; MF_02208; MurD2_subfam; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR InterPro; IPR043687; MurD2.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01087; murD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..468
FT /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT /id="PRO_0000109129"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ SEQUENCE 468 AA; 49747 MW; CD065547238CB0FA CRC64;
MRISQFEGKA VALWGWGREG RGAYRALRAQ LPTQSLTMFC NAEEVRELES LADAALHVET
DASAQALGRF EIVVKSPGIS PYRAEALAAA AQGTQFIGGT ALWFAEHAQP DGSVPGAICV
TGTKGKSTTT ALLAHLLRVA GHRTALVGNI GQPLLEVLAP QPPPAYWAIE LSSYQTGDVG
RSGARPELAV VLNLFPEHLD WHGDEARYVR DKLSLVTEGR PRIVLLNAAD PLLASLQLPD
SEVLWFNHPE GWHLRGDVVY RGEQAIFDSA DVPLPGVHNR RNLCAVLAAL EALGLDAEAL
APAALSFRPL PNRLQVLGSV DGISYVNDSI STTPYASLAA LACFAQRRVA LLVGGHDRGL
DWHDFARHMA QQAPLEIVTM AANGPRIHAL LAPLADAGRF GLHAANDLEH AMQLARDALG
GQGGVVLLSP GAPSFGAYSD YVARGRHFAQ LAGFDPAAIS AIPGLGVH
