ID   MURD_NITMU              Reviewed;         473 AA.
AC   Q2Y636;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639};
DE            EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; OrderedLocusNames=Nmul_A2496;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00639};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00639}.
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DR   EMBL; CP000103; ABB75785.1; -; Genomic_DNA.
DR   RefSeq; WP_011381784.1; NZ_FNVK01000005.1.
DR   AlphaFoldDB; Q2Y636; -.
DR   SMR; Q2Y636; -.
DR   STRING; 323848.Nmul_A2496; -.
DR   PRIDE; Q2Y636; -.
DR   EnsemblBacteria; ABB75785; ABB75785; Nmul_A2496.
DR   KEGG; nmu:Nmul_A2496; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_1_0_4; -.
DR   OMA; CNFENYL; -.
DR   OrthoDB; 1093223at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002718; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase 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   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   Pfam; PF02875; Mur_ligase_C; 1.
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..473
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000257209"
FT   BINDING         120..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   473 AA;  49802 MW;  D47D0A5001BCFF43 CRC64;
     MNLQGRTVLV LGLGETGLSM AKWLFRRGAL VRAADTRNEP PAMRAFNSLL PQAEVFTGSL
     AGRAFYGVDL IAISPGLPLS EPLVQQALKE GIPVVGDMEL FACAVGGTGG GMPKLVGITG
     SNGKTTVTAM TGAMLKKAGW DVEVAGNIGP AVLDALMRRE DTGKMPQAWV LELSSFQLET
     TKSLGLDAAA VLNVSEDHLD RYAGMQEYAA AKARIFLGDS EGVQILNGDD PVVRQMTLAG
     RPHVTFSLAT PQSADDFGLL REGGDTWLMQ GDTRLMDARE LAITGRHNCA NALAALALCR
     ALAVPFEPLL QALREFRGLP HRVEKVAAFS GITFYDDSKG TNVGATVAAL KGLGQPVVLI
     AGGDGKAQNF SPLAAPIGEH GRAVVLIGRD AEKIAVAINE CGVPLHRAQT MEEAVRKSFQ
     LAREGDAVLM SPACASFDMF DNYVHRAEAF VAAVRSMQAA RAGGNSAGVA GRH