ID   MURD2_XANOM             Reviewed;         468 AA.
AC   Q2P5V2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE            EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000269|PubMed:28294606};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE            Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN   Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN   OrderedLocusNames=XOO1320;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=MAFF 311018;
RX   PubMed=28294606; DOI=10.1021/jacs.7b01221;
RA   Feng R., Satoh Y., Ogasawara Y., Yoshimura T., Dairi T.;
RT   "A glycopeptidyl-glutamate epimerase for bacterial peptidoglycan
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 139:4243-4245(2017).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine. Has weak
CC       activity with D-glutamate. {ECO:0000269|PubMed:28294606}.
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         ECO:0000269|PubMed:28294606};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305|PubMed:28294606}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208,
CC       ECO:0000305}.
CC   -!- MISCELLANEOUS: The combined activity of MurD2 and MurL provides an
CC       alternative route for incorporating D-glutamate into peptidoglycan.
CC       {ECO:0000305|PubMed:28294606}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305}.
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; AP008229; BAE68075.1; -; Genomic_DNA.
DR   RefSeq; WP_011258236.1; NC_007705.1.
DR   AlphaFoldDB; Q2P5V2; -.
DR   SMR; Q2P5V2; -.
DR   KEGG; xom:XOO1320; -.
DR   HOGENOM; CLU_032540_4_1_6; -.
DR   OMA; KGMHNVE; -.
DR   BioCyc; MetaCyc:MON-20388; -.
DR   UniPathway; UPA00219; -.
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   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..468
FT                   /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT                   /id="PRO_0000257263"
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