MURD2_XANAC
ID MURD2_XANAC Reviewed; 468 AA.
AC Q8PII9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208};
DE EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
DE Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
GN Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208}; OrderedLocusNames=XAC2908;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC EC=6.3.2.53; Evidence={ECO:0000255|HAMAP-Rule:MF_02208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
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DR EMBL; AE008923; AAM37753.1; -; Genomic_DNA.
DR RefSeq; WP_011051916.1; NC_003919.1.
DR AlphaFoldDB; Q8PII9; -.
DR SMR; Q8PII9; -.
DR STRING; 190486.XAC2908; -.
DR EnsemblBacteria; AAM37753; AAM37753; XAC2908.
DR GeneID; 66911985; -.
DR KEGG; xac:XAC2908; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_4_1_6; -.
DR OMA; KGMHNVE; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000576; 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:InterPro.
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 HAMAP; MF_02208; MurD2_subfam; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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 InterPro; IPR043687; MurD2.
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.
FT CHAIN 1..468
FT /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT /id="PRO_0000109126"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ SEQUENCE 468 AA; 49388 MW; 4220319C924C163D CRC64;
MRISQLEGKA VALWGWGREG RAAYRALRAR LPTQALTVFC NAEEAREIGA LADAALQVET
DASAQALGRF EIVVKSPGIS PYRAEALAAA AQGTHFIGGT ALWFAEHAQA DGSVPGVVCI
TGTKGKSTTT ALLAHVLRAA GHRTALVGNI GQPLLEVLAP QPPPAYWAVE LSSYQTGDVG
RSGARPQLAL VLNLFPEHLD WHGDEARYVR DKLSLVTEGR PRIALLNAAD PLLAGLQLPD
SQVRWFNQPA GWHLRGEVVY RGEQAIFDTA DVPLPGEHNR RNLCAVLAAV EALGLDAAAL
APAAASFRPL PNRLQLLGSV DGISYVNDSI STTPHASLAA LACFARRRVA LLVGGHDRGL
DWHDFAQQMA QQAPLEIVTM GANGPRIHAL LAPLAEAGHF GLHAANDLEH AMGLARNALG
EQGGVVLLSP GAPSFGAYSD YVARGRHFAQ LAGFDPAAIS AIDGLGVH
