(data stored in SCRATCH3701 zone)

SWISSPROT: MURD_VIBVY

ID   MURD_VIBVY              Reviewed;         442 AA.
AC   Q7MNV3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 109.
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=VV0612;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
DR   EMBL; BA000037; BAC93376.1; -; Genomic_DNA.
DR   RefSeq; WP_011149502.1; NC_005139.1.
DR   SMR; Q7MNV3; -.
DR   STRING; 672.VV93_v1c05550; -.
DR   EnsemblBacteria; BAC93376; BAC93376; BAC93376.
DR   GeneID; 2623381; -.
DR   KEGG; vvy:VV0612; -.
DR   PATRIC; fig|196600.6.peg.631; -.
DR   HOGENOM; HOG000049427; -.
DR   KO; K01925; -.
DR   OMA; CSSFDMF; -.
DR   OrthoDB; 1093223at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002675; Chromosome I.
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; UDP-N-AcMur-Glu_ligase.
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;
DR   PRODOM; Q7MNV3.
DR   SWISS-2DPAGE; Q7MNV3.
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..442
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000109123"
FT   NP_BIND         115..121
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   442 AA;  47978 MW;  E8C63EFD1E340C05 CRC64;
     MDRWQDIKQV VVVGLGITGL SVVRHLRKTQ PQLQVKVIDT RPTPPGVEQL PPDIALHVGS
     WNEAWLAEAD LVVTNPGIAL ATPQIQTVLA RGVAVVGDIE LFAWAADKPV IAITGSNGKS
     TVTDLTGVMA NACGVKCAIG GNIGVPALDL LEQEVELYVL ELSSFQLETT TSLHLVAAAF
     LNLSEDHMDR YQGMDDYRQA KLRIFQHAKH GVVNRDDRQT YPETSHGQQS LALVTFGSDD
     KEFGVMSHQG ESWLSYNQQP ILASRELKLV GQHNVANVLV VLALLTCAGI DYRKGLSALK
     SYTGLTHRCQ VVADNRGIKW VNDSKATNLA STQAALSGLN CAGKLYLLVG GDGKGADFSP
     LKPILAQLNL QLCCFGADGD QFMPLHASAT RFERMEDVIE HISPQLQSGD MVMLSPACAS
     FDQFSNFMAR GDRFAELARQ YA
//

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