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UniProtKB/Swiss-Prot entry Q2IG29

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

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Entry information
Entry name MURD_ANADE
Primary accession number Q2IG29
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on March 7, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 26)
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: Adeh_3769
From
Anaeromyxobacter dehalogenans (strain 2CP-C) [TaxID: 290397] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000251; ABC83535.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_466972.1; -.
3D structure databases
ModBase Q2IG29.
Enzyme and pathway databases
BioCyc ADEH290397:ADEH_3769-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.
IPR000713; Mur_ligase_N.
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 PF01225; Mur_ligase; 1.
PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01087; murD; 1.
ProtoNet Q2IG29.
Genome annotation databases
GeneID 3886505; -.
GenomeReviews CP000251_GR; Adeh_3769.
KEGG ade:Adeh_3769; -.
Phylogenomic databases
HOGENOM Q2IG29; -.
Genome annotation databases
CMR Q2IG29; Adeh_3769.
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   462  462     UDP-N-acetylmuramoylalanine--D-glutamate ligase. PRO_0000257165
NP_BIND   118   124  7     ATP (Potential). 
Sequence information
Length: 462 AA [This is the length of the unprocessed precursor] Molecular weight: 48010 Da [This is the MW of the unprocessed precursor] CRC64: 0F78BB8BB8EB59A6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAAPELKGTR VTVVGLAKSG VAAARLCARE GARVTVTDRR GEAALGGALA ALPASVTRRL 

        70         80         90        100        110        120 
GGHDAADFTG ADLVVASPGV PLANPEIQAA RRRGVPVWGE VELAARFLGG LPIVGITGTN 

       130        140        150        160        170        180 
GKSTTTALTG ALLARHRRTF VGGNLGTPLS ELVLSGEPAA AAVVELSSFQ LEGIERFRAR 

       190        200        210        220        230        240 
VAAVLNVTPD HLDRYPDVDA YAAAKARLFA TQEPDDVAVA NARDPRALAM AGASRGDLHT 

       250        260        270        280        290        300 
FGFGAPVPAS ARDEGGEPGP GGTAIWYTPR GRAPERYQLH NRALRGRHNR ENAMAAVLCA 

       310        320        330        340        350        360 
RLMGVPGEAV QAGLDAFPGL HHRLELVAEG RGVEWVNDSK ATNVDSTFVG LAAFPAGAPR 

       370        380        390        400        410        420 
VVLIMGGRGK KAPYAPLRPL FGGRVKALLT IGEDAPAIER ELGDLAPTEP CGDLPGAVRR 

       430        440        450        460 
AAVLSGPGDV VLLSPACASY DQFASYEERG EAFRRLATEQ AR
Q2IG29 in FASTA format

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