ID   MURD_BURVG              Reviewed;         503 AA.
AC   A4JB92;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 104.
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};
GN   OrderedLocusNames=Bcep1808_0533;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia;
OC   Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) 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=UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate + ATP =
CC         UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + ADP + phosphate
CC         + H(+); Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898,
CC         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; CP000614; ABO53545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JB92; -.
DR   SMR; A4JB92; -.
DR   KEGG; bvi:Bcep1808_0533; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_1_1_4; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002287; Chromosome 1.
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:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01087; murD; 1.
DR   PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF21799; MurD-like_N; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 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..503
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_1000056877"
FT   BINDING         129..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   503 AA;  52752 MW;  EA186E73EF2B4368 CRC64;
     MFGDRQRPMV LVLGLGESGL AIARWCARHG CRLRIADTRE APPNLAALQA EGIDAEFVGG
     PFTPALLDGG IDIVGLSPGL SPLEPALAAL LAAASERAIA VWGELEFFAQ ALRALGTSGY
     QPKVLAITGT NGKTTTTSLT GLLCQRAGKK VAVAGNISPA MLDRLASAID ETALPDVWVL
     ELSSFQLETA RTFAPDAAAI LNITQDHLDW HGSFDAYAAA KGRIFGATTT RVLNRDDAAV
     MKFAPAAGAA DAARTVTFGL GEPTRDGDYG LSRDNGIAWL VEAIDRDAPD ETTTTRRRKR
     DGAHTPDIAH KRLMPVDALR IRGLHNAANA LAAFALARAI DLPAAPLLHA LREYRGEAHR
     VEVIATIDDV DYVDDSKGTN VGATVAALDG LAQKIVLIAG GDGKGQDFAP LVAPVARWCR
     AVMLIGRDAP ALRATLADTG VPLADHATLE GAVRAAAELA EPGDAVLLSP ACASLDMFRN
     YAHRADVFRA AVDEIAIDKG ATP
//