MURD_CHLL2
ID MURD_CHLL2 Reviewed; 465 AA.
AC B3EIL0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Clim_2504;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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; CP001097; ACD91522.1; -; Genomic_DNA.
DR RefSeq; WP_012467386.1; NC_010803.1.
DR AlphaFoldDB; B3EIL0; -.
DR SMR; B3EIL0; -.
DR STRING; 290315.Clim_2504; -.
DR EnsemblBacteria; ACD91522; ACD91522; Clim_2504.
DR KEGG; cli:Clim_2504; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_0_0_10; -.
DR OMA; CNFENYL; -.
DR OrthoDB; 1093223at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008841; 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..465
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_1000130837"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ SEQUENCE 465 AA; 50058 MW; 024990E5E20DFF26 CRC64;
MDVHGKKASI IGAKRSGVAA AELLAKSGAK VFVSELGEPG ASEAERLADC GIPWEQDGHT
DRVCDADFCV VSPGIPRTAG IIRRVLEQGI PLYSEIEAAS WFCKARIAGI TGTDGKTTTS
TLLHRIAEAD GMKNDYRAFS VGNIGVPFSS LVLDMAPADL AVVELSSYQL EGCETFRPDV
SVITNITPDH LDRYNGDMQL YAAAKFRIYA SQRASDTLVY NFDDPLLRAQ FSGNGRGFPF
RIVPFGIGND VPGSGSEEAF FYDEGMIRHL TAKGISEVFS GEDFLKSSFR GRHNIYNALA
ALAAAAALGI EESVARKAIS GFSGVEHRQE FVCSLDGVEW INDSKATNVN ALLQALDAVP
GSIVLIAGGR DKGNDYTVLF DVVRRKVVTV IAIGEAREKI LQVFEGITRT AGADTLDDAV
ALARESAEKG QTVLFSPGCA SFDMFENFEE RGRLFKRSIL ALNPC