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UniProtKB/Swiss-Prot entry B0C915


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

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Entry information
Entry name MURD_ACAM1
Primary accession number B0C915
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on February 26, 2008 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 8)
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: AM1_1525
From
Acaryochloris marina (strain MBIC 11017) [TaxID: 329726] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Acaryochloris.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0709772105; PubMed=18252824 [NCBI, ExPASy, EBI, Israel, Japan]
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.;
"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina.";
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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
CP000828; ABW26550.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001515864.1; -.
3D structure databases
ModBase B0C915.
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:0009252; Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
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.
TIGRFAMs TIGR01087; murD; 1.
BLOCKS B0C915.
ProtoNet B0C915.
Genome annotation databases
GeneID 5680345; -.
GenomeReviews CP000828_GR; AM1_1525.
KEGG amr:AM1_1525; -.
CMR B0C915; AM1_1525.
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   461  461     UDP-N-acetylmuramoylalanine--D-glutamate ligase. PRO_1000082675
NP_BIND   118   124  7     ATP (Potential). 
Sequence information
Length: 461 AA [This is the length of the unprocessed precursor] Molecular weight: 49514 Da [This is the MW of the unprocessed precursor] CRC64: A7F9BD8FA96EBF8E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPAVHIIGLG RSGIAAARLL RREGWQVSVG DAGHSEGLVA TQKTLAAEGI PVHLNLKFSL 

        70         80         90        100        110        120 
SALAELSLDR PDRIVVSPGV PWQLPALEEA RSQGIETFGE LELAWRSLKQ YPWVGITGTN 

       130        140        150        160        170        180 
GKTTTTAIVE AIFKAAGLRA PACGNIGYSA CELALAGDPL DWVIAEVSSY QIESSPTLAP 

       190        200        210        220        230        240 
TIGVWTTFSP DHLERHGTVE CYREIKALLL NQSKQKILNG DDQGLIKGLP WRWADAYWTS 

       250        260        270        280        290        300 
SHGPSLPDAC NGQRCPVPNI FIEEGWVKVE GEPIVQVSSM RMLGVHNQQN LLLAVAVAHL 

       310        320        330        340        350        360 
AGIGKDAIAT AVSTFPGVAH RLEHICTWQG VDFINDSKAT NYEAAQTGLA AVNSPAILIA 

       370        380        390        400        410        420 
GGEAKVGDDQ AWLQTIQAQA AKVLLIGSAA GAFSQRLKAI GYDDYEIVDT MNKAVTRAAE 

       430        440        450        460 
LAPSLQAKSV LLSPACASFD QYQNFERRGD HFRQLCQDLS Q 

B0C915 in FASTA format

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