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UniProtKB/Swiss-Prot entry Q8K9T2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MURD_BUCAP
Primary accession number Q8K9T2
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name UDP-N-acetylmuramoylalanine--D-glutamate ligase
Synonyms EC 6.3.2.9
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
D-glutamic acid-adding enzyme
Gene name
Name: murD
OrderedLocusNames: BUsg_212
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE013218; AAM67775.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660564.1; -.
3D structure databases
HSSP P14900; 1E0D. [HSSP ENTRY / PDB]
ModBase Q8K9T2.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG212-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0008764; Molecular function: UDP-N-acetylmuramoylalanine-D-glutamate ligase activity (inferred from electronic annotation from HAMAP).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301; Biological process: cell division (inferred from electronic annotation from InterPro).
GO:0009252; Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360; Biological process: regulation of cell shape (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00639; -; 1.
PBIL [Tree]
InterPro IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
IPR016040; NAD(P)-bd.
IPR005762; UDP-N-AcMur-Glu_ligase.
Graphical view of domain structure.
Gene3D G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01087; murD; 1.
ProtoNet Q8K9T2.
Genome annotation databases
GeneID 1005411; -.
GenomeReviews AE013218_GR; BUsg_212.
KEGG bas:BUsg212; -.
Phylogenomic databases
HOGENOM Q8K9T2; -.
Genome annotation databases
CMR Q8K9T2; BUsg_212.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Peptidoglycan synthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   440  440     UDP-N-acetylmuramoylalanine--D-glutamate ligase. PRO_0000108986
NP_BIND   113   119  7     ATP (Potential). 
Sequence information
Length: 440 AA [This is the length of the unprocessed precursor] Molecular weight: 49855 Da [This is the MW of the unprocessed precursor] CRC64: DD9C28B6B8E8974E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSYNYFGKKI LILGLGLTGI SCINFFLKKG IQPRVIDESN KPIFLNKIPK NIEYKLGNLK 

        70         80         90        100        110        120 
ENWILESDLI IISPGISSFK PILMKARSLG IDIISDIELF SRETKCPIIS ITGTNGKSTV 

       130        140        150        160        170        180 
ATMVKKIAEK SGYKVLLGGN IGFPVLEMLN KKASLYVLEL SSFQLETTFN LKSKIAVVLN 

       190        200        210        220        230        240 
ITEDHLDRYP EGFEQYKKTK LSIYNKAKIC LIKLKKGEKK PFNTKSKKYI SFGTCNNNDY 

       250        260        270        280        290        300 
YINYEKEKAI LFHKNKKIVD TSNILLNGHH NYENILTSLA ISDQMKFDQK VSINVLKKFL 

       310        320        330        340        350        360 
GLPHRFQTVH INNNISWIND SKSTNVDSTK AALKNLKIKG TIWLLLGGDG KSSNFNILKK 

       370        380        390        400        410        420 
YFEKIKIKIY CFGKDGLNLS KLCKKKSIYT KTLKQAIILI SKKIQPGDVV LLSPGCSSKD 

       430        440 
QFSNFEERGN LFIKLSKEIN
Q8K9T2 in FASTA format

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