MURD_PSEAE
ID MURD_PSEAE Reviewed; 448 AA.
AC Q9HVZ9; Q9EY46;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PA4414;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=11281713; DOI=10.1006/prep.2001.1390;
RA Azzolina B.A., Yuan X., Anderson M.S., El-Sherbeini M.;
RT "The cell wall and cell division gene cluster in the Mra operon of
RT Pseudomonas aeruginosa: cloning, production, and purification of active
RT enzymes.";
RL Protein Expr. Purif. 21:393-400(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
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; AY008276; AAG45237.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07802.1; -; Genomic_DNA.
DR PIR; G83094; G83094.
DR RefSeq; NP_253104.1; NC_002516.2.
DR RefSeq; WP_003103104.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q9HVZ9; -.
DR SMR; Q9HVZ9; -.
DR STRING; 287.DR97_1592; -.
DR PaxDb; Q9HVZ9; -.
DR PRIDE; Q9HVZ9; -.
DR EnsemblBacteria; AAG07802; AAG07802; PA4414.
DR GeneID; 881268; -.
DR KEGG; pae:PA4414; -.
DR PATRIC; fig|208964.12.peg.4623; -.
DR PseudoCAP; PA4414; -.
DR HOGENOM; CLU_032540_1_0_6; -.
DR InParanoid; Q9HVZ9; -.
DR OMA; CNFENYL; -.
DR PhylomeDB; Q9HVZ9; -.
DR BioCyc; PAER208964:G1FZ6-4501-MON; -.
DR UniPathway; UPA00219; -.
DR PHI-base; PHI:7631; -.
DR Proteomes; UP000002438; 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 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; Reference proteome.
FT CHAIN 1..448
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109062"
FT BINDING 116..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
FT CONFLICT 57
FT /note="V -> A (in Ref. 1; AAG45237)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 1; AAG45237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 48080 MW; 0CFF8F1A7676B266 CRC64;
MSLIASDHFR IVVGLGKSGM SLVRYLARRG LPFAVVDTRE NPPELATLRA QYPQVEVRCG
ELDAEFLCSA RELYVSPGLS LRTPALVQAA AKGVRISGDI DLFAREAKAP IVAITGSNAK
STVTTLVGEM AVAADKRVAV GGNLGTPALD LLADDIELYV LELSSFQLET CDRLNAEVAT
VLNVSEDHMD RYDGMADYHL AKHRIFRGAR QVVVNRADAL TRPLIADTVP CWSFGLNKPD
FKAFGLIEED GQKWLAFQFD KLLPVGELKI RGAHNYSNAL AALALGHAVG LPFDAMLGAL
KAFSGLAHRC QWVRERQGVS YYDDSKATNV GAALAAIEGL GADIDGKLVL LAGGDGKGAD
FHDLREPVAR FCRAVVLLGR DAGLIAQALG NAVPLVRVAT LDEAVRQAAE LAREGDAVLL
SPACASLDMF KNFEERGRLF AKAVEELA
