MURD_MYCLE
ID MURD_MYCLE Reviewed; 490 AA.
AC P57995; O69554;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=ML0912; ORFNames=MLCB268.04c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; AL583920; CAC31293.1; -; Genomic_DNA.
DR EMBL; AL022602; CAA18670.1; -; Genomic_DNA.
DR PIR; B87023; B87023.
DR RefSeq; NP_301695.1; NC_002677.1.
DR RefSeq; WP_010908019.1; NC_002677.1.
DR AlphaFoldDB; P57995; -.
DR SMR; P57995; -.
DR STRING; 272631.ML0912; -.
DR EnsemblBacteria; CAC31293; CAC31293; CAC31293.
DR KEGG; mle:ML0912; -.
DR PATRIC; fig|272631.5.peg.1655; -.
DR Leproma; ML0912; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_0_0_11; -.
DR OMA; CNFENYL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000806; 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; 2.
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..490
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109044"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 50583 MW; 1385495843830536 CRC64;
MLDTLVPGAP VLVAGGGVTG RAVLAALTRF GMAATLCDDD PAALQQYADN GVATVSAATA
TQQMFERGRK YVLVVTSPGF APTTPVLVAA SAARVPIWGD VELAWRLDAA GYYGPPRRWL
VVTGTNGKTT TTSMLHAMLA ADNRRSLLCG NIGRPVLDVL TEFAEPSDFL AVELSSFQLH
WAPSLRPEAG VVLNIAEDHL DWHSTMADYT MAKARVLTGR VAVVGLDDSR AAALLSTTVA
PVRVGFRFGE PAVGELGVRD GYLVDRAFAE DLALMPVTSI PVSGPVGVLD ALAAAALARS
VGVGATAIAD AVALFRLGRH RAEVVAVADG IRYVDDSKAT NPHAALVSVL AYPRVVWVAG
GLLKGASVDA EVARMAPQLV GAVLIGRDRA MVAEALSRHA PNVPVVQVVA GEDAGMHAVA
VVSGTDVISI SDVGGTIGTR VMVAAVAAAR DLAQPGDTVL LAPAGASFDQ FSGYADRGDT
FATAVRAAIR
