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UniProtKB/Swiss-Prot entry Q39PN9

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

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Entry information
Entry name PURA2_BURS3
Primary accession number Q39PN9
Secondary accession numbers None
Integrated into Swiss-Prot on March 7, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 27)
Name and origin of the protein
Protein name Adenylosuccinate synthetase 2
Synonyms EC 6.3.4.4
IMP--aspartate ligase 2
AdSS 2
AMPSase 2
Gene name
Name: purA2
OrderedLocusNames: Bcep18194_C6526
From
Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [TaxID: 269483] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 3 of Burkholderia sp. 383.";
Submitted (OCT-2005) 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
CP000150; ABB05577.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_366221.1; -.
3D structure databases
ModBase Q39PN9.
Enzyme and pathway databases
BioCyc BSP36773:BCEP18194_C6526-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; atypical; 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.
ProtoNet Q39PN9.
Genome annotation databases
GeneID 3733882; -.
GenomeReviews CP000150_GR; Bcep18194_C6526.
KEGG bur:Bcep18194_C6526; -.
NMPDR fig|269483.3.peg.3735; -.
Phylogenomic databases
HOGENOM Q39PN9; -.
Genome annotation databases
CMR Q39PN9; Bcep18194_C6526.
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   432  432     Adenylosuccinate synthetase 2. PRO_0000224265
NP_BIND   12    18  7     GTP (Potential). 
ACT_SITE   139   139        By similarity. 
ACT_SITE   146   146        By similarity. 
METAL   13    13        Magnesium (By similarity). 
METAL   40    40        Magnesium; via carbonyl oxygen (By similarity). 
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 45920 Da [This is the MW of the unprocessed precursor] CRC64: E8B1AC0AA0B3D792 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPNVVVVGAQ WGDEGKGRVV DWLAAQADLV ARYNGGHNAG HTLVVGGKTY KLALLPSGVV 

        70         80         90        100        110        120 
RGKRGVIGNG VALDPEALLA EIGRMAELGL SVTPDNLSIA ENATLVLPIH RAIDQAQERL 

       130        140        150        160        170        180 
RREPIGTTLR GIGPAYEDKV GRRGLRVGDL AEPGRLAAKL DVLVDHHNAW FRGLGLDEYS 

       190        200        210        220        230        240 
RDAMLATLVD LAPRILPFVR PVWADLNDAT DRGERILFEG SQAVMLDIDW GTYPFVTSSG 

       250        260        270        280        290        300 
TVASAAAAGT GLGASKLGHV LGVTKAYATR VGGGPFLTEL SDATGETLRA RGQEFGVNTG 

       310        320        330        340        350        360 
RPRRCGWLDA AQLRQAVRIS GIDSLALTKL DVLDGFESIE LCVGYEFDGA RVDHLPASLD 

       370        380        390        400        410        420 
AQSRAKPVYE RFDGWRGTVK GVRERAALPR AAQDFIARVE AVAGAPVSMI TTGAERDDTI 

       430 
VLRNPFDAAA GA
Q39PN9 in FASTA format

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