MURD_RHIME
ID MURD_RHIME Reviewed; 463 AA.
AC Q52953;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE EC=6.3.2.9;
DE AltName: Full=D-glutamic acid-adding enzyme;
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
GN Name=murD; OrderedLocusNames=R02178; ORFNames=SMc01864;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-344.
RC STRAIN=1021;
RX PubMed=7926844; DOI=10.1016/0378-1119(94)90238-0;
RA Leach F., Wacks D.B., Signer E.R.;
RT "Rhizobium meliloti homologs of Escherichia coli mur genes.";
RL Gene 148:87-90(1994).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000250}.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA66472.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL591688; CAC46757.1; -; Genomic_DNA.
DR EMBL; L25875; AAA66472.1; ALT_FRAME; Genomic_DNA.
DR PIR; JC2567; JC2567.
DR RefSeq; NP_386284.1; NC_003047.1.
DR RefSeq; WP_010969748.1; NC_003047.1.
DR AlphaFoldDB; Q52953; -.
DR SMR; Q52953; -.
DR STRING; 266834.SMc01864; -.
DR PRIDE; Q52953; -.
DR EnsemblBacteria; CAC46757; CAC46757; SMc01864.
DR GeneID; 61603642; -.
DR KEGG; sme:SMc01864; -.
DR PATRIC; fig|266834.11.peg.3644; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_3_0_5; -.
DR OMA; CNFENYL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001976; Chromosome.
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: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; 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 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..463
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109069"
FT BINDING 121..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 132
FT /note="I -> V (in Ref. 3; AAA66472)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> S (in Ref. 3; AAA66472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 48067 MW; E123D25E142D819E CRC64;
MIPVTSFKGR KVALFGLGGS GLATAQALVS GGADVVAWDD NPDSVAKAAA AGIATADLRG
ADWHAFAAFV LSPGVPLTHP KPHWSVDLAH QAGVEIIGDV ELFVRERRKH APDCPFIAIT
GTNGKSTTTA LIAHILRTSG RDTQLGGNIG TAVLTLDPPK AGRFYVVECS SYQIDLAPTL
DPTAGILLNL TPDHLDRHGT MQHYADIKER LVAGSGTAVV GVDDSLSSLI ADRVERAGTK
VVRISRRHPL AEGIYAEGSA LMRAQDGASS LFTDLAGIQT LRGGHNAQNA AAAIAACLAV
GISGKDIVDG LRSFPGLKHR MQPVAKKGEV VFVNDSKATN AEAAAPALSS YDRIYWIAGG
LPKEGGITSL APFFPKIVKA YLIGEAAPSF AATLGEAVPY EISGTLEKAV AHAAADAARD
SQGPAAVMLS PACASFDQYK NFEVRGDAFV GHVAALEGVS MLI
