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UniProtKB/Swiss-Prot entry Q89AQ2

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

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Entry information
Entry name MURD_BUCBP
Primary accession number Q89AQ2
Secondary accession numbers None
Integrated into Swiss-Prot on May 23, 2003
Sequence was last modified on May 23, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 48)
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: bbp_200
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO26932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777827.1; -.
3D structure databases
HSSP P14900; 4UAG. [HSSP ENTRY / PDB]
ModBase Q89AQ2.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_200-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 IPR002110; ANK.
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.
PRINTS PR01415; ANKYRIN.
TIGRFAMs TIGR01087; murD; 1.
BLOCKS Q89AQ2.
ProtoNet Q89AQ2.
Genome annotation databases
GeneID 1058151; -.
GenomeReviews AE016826_GR; bbp_200.
KEGG bab:bbp200; -.
Phylogenomic databases
HOGENOM Q89AQ2; -.
Genome annotation databases
CMR Q89AQ2; bbp_200.
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   442  442     UDP-N-acetylmuramoylalanine--D-glutamate ligase. PRO_0000108985
Sequence information
Length: 442 AA [This is the length of the unprocessed precursor] Molecular weight: 50066 Da [This is the MW of the unprocessed precursor] CRC64: C4876568C23CE357 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTRNYLHKKI LIFGMGLTGI SCLNFFLSKG IYPKIMDTDK RPKHIEKIIK FKNICYHTGS 

        70         80         90        100        110        120 
VNYSWILQSN LIIVSPGITP SHPALKFATK KNIEIIGDIE LFVQETKVPI IAITGSNGKS 

       130        140        150        160        170        180 
SVTKIVKEII QKAGFTTYIG GNIGIPALNI VNKFAHFFIL ELSSFQLERT FSLKAYIATI 

       190        200        210        220        230        240 
LNITPDHLNR YSSDIKEYEK AKQKIYKNSK ICIINVDNPV TINRQAQLTK CISFGVHSGD 

       250        260        270        280        290        300 
YHLSHTYTNT WLCYKSLKLI NTKKLKLSGR HNYINMLSAL AIVHELKISF KISVRILKNF 

       310        320        330        340        350        360 
LGLPHRCQKV YKNNNITWIN DSKSTNIAST KSAIQSINTK GKIRLILGGD KKSSNLNLLK 

       370        380        390        400        410        420 
PILKNNAIVI YCYGKDKKEL FNLYPHKSKI FETLQEVMQH ISVQVQPGDV VLLSPACSSL 

       430        440 
DQFSGFEERG NTFVKLIQEL IH
Q89AQ2 in FASTA format

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