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UniProtKB/Swiss-Prot entry Q89EM1

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

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Entry information
Entry name PURA_BRAJA
Primary accession number Q89EM1
Secondary accession numbers None
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 38)
Name and origin of the protein
Protein name Adenylosuccinate synthetase
Synonyms EC 6.3.4.4
IMP--aspartate ligase
AdSS
AMPSase
Gene name
Name: purA
OrderedLocusNames: bll7052
From
Bradyrhizobium japonicum [TaxID: 375] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(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
BA000040; BAC52317.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_773692.1; -.
3D structure databases
HSSP P12283; 1ADE. [HSSP ENTRY / PDB]
ModBase Q89EM1.
Enzyme and pathway databases
BioCyc BJAP224911:BLL7052-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004019; Molecular function: adenylosuccinate synthase activity (inferred from electronic annotation from HAMAP).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00011; -; 1.
PBIL [Tree]
InterPro IPR001114; AdlSucc_Synth.
Graphical view of domain structure.
PANTHER PTHR11846; Asucc_synthtase; 1.
Pfam PF00709; Adenylsucc_synt; 1.
Pfam graphical view of domain structure.
ProDom PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00184; purA; 1.
PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.
BLOCKS Q89EM1.
ProtoNet Q89EM1.
Genome annotation databases
GeneID 1048009; -.
GenomeReviews BA000040_GR; bll7052.
KEGG bja:bll7052; -.
NMPDR fig|224911.1.peg.7052; -.
Phylogenomic databases
HOGENOM Q89EM1; -.
Genome annotation databases
CMR Q89EM1; bll7052.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   430  430     Adenylosuccinate synthetase. PRO_0000095152
NP_BIND   12    18  7     GTP (Potential). 
ACT_SITE   141   141        By similarity. 
ACT_SITE   148   148        By similarity. 
METAL   13    13        Magnesium (By similarity). 
METAL   40    40        Magnesium; via carbonyl oxygen (By similarity). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 46787 Da [This is the MW of the unprocessed precursor] CRC64: 6B69D4B09B13D14C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MANVVVVGAQ WGDEGKGKIV DWLSEQADIV VRFQGGHNAG HTLVINGKTY KLALLPSGVL 

        70         80         90        100        110        120 
REHKLSVIGN GVVFDPAAFL DEVTKLRAQG VAVSPENLRV AENVTLILPL HRELDAHRES 

       130        140        150        160        170        180 
ANAATAIGTT RRGIGPAYED KVGRRAIRLM DLADLDTLPH KIDRLLAHHN ALRRGLNLPE 

       190        200        210        220        230        240 
FDGKDILKEL TALAPQLLPY AETVWRLLDI KRREGKRMLF EGAQGALLDV DHGTYPYVTS 

       250        260        270        280        290        300 
SNTVAAQAAT GSGLGPGAVG YVLGLCKAYT TRVGQGPFPT EQDNEIGRKI GERGREFGTN 

       310        320        330        340        350        360 
TGRPRRCGWF DAVLVRQAVR TCGINGLALT KLDILDGFDS IEVCTGYKLD GKEIDHFPAG 

       370        380        390        400        410        420 
EGAQARVEPI YETIEGWKEP TASARSWADL PAQAIKYVRR IEELVGCPVA LLSTSPERED 

       430 
TILVQNPFEA
Q89EM1 in FASTA format

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