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Q0B2T2 (Q0B2T2_BURCM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase 2 HAMAP MF_00011
Short name=AMPSase 2 HAMAP MF_00011
Short name=AdSS 2 HAMAP MF_00011
EC=6.3.4.4 HAMAP MF_00011
Alternative name(s):
IMP--aspartate ligase 2 HAMAP MF_00011
Gene names
Name:purA2 HAMAP MF_00011
Ordered Locus Names:Bamb_5997
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis By similarity. RuleBase RU000520

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP By similarity. HAMAP MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011 RuleBase RU000520

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00011

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011 RuleBase RU000520

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family. HAMAP MF_00011 RuleBase RU004163

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 187GTP By similarity HAMAP MF_00011
Nucleotide binding40 – 423GTP By similarity HAMAP MF_00011
Nucleotide binding329 – 3313GTP By similarity HAMAP MF_00011
Nucleotide binding411 – 4133GTP By similarity HAMAP MF_00011
Region13 – 164IMP binding By similarity HAMAP MF_00011
Region38 – 414IMP binding By similarity HAMAP MF_00011
Region297 – 3037Substrate binding By similarity HAMAP MF_00011

Sites

Active site131Proton acceptor By similarity HAMAP MF_00011
Active site411Proton donor By similarity HAMAP MF_00011
Metal binding131Magnesium By similarity HAMAP MF_00011
Metal binding401Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1281IMP By similarity HAMAP MF_00011
Binding site1421IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site2221IMP By similarity HAMAP MF_00011
Binding site2371IMP By similarity HAMAP MF_00011
Binding site3011IMP By similarity HAMAP MF_00011
Binding site3031GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
Q0B2T2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: F70B45BCA942F3E5

FASTA42945,613
        10         20         30         40         50         60 
MPNVVVVGAQ WGDEGKGRVV DWLAAQADLV ARYNGGHNAG HTLVVGDKTY KLALLPSGIV 

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

       130        140        150        160        170        180 
RREPIGTTLR GIGPAYEDKV GRRGLRVADL AEPGRLADKL DVLVDYHNAW FRGLGLEPCS 

       190        200        210        220        230        240 
RDAMLATLVD IAPKILPFVR PVWADLNDAN DRGERILFEG SQAVMLDIDW GTYPFVTSSG 

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

       310        320        330        340        350        360 
RPRRCGWLDA AQLRQAVRIS GIDSLALTKL DVLDGFASIE LCVGYELDGA RVDHLPASLD 

       370        380        390        400        410        420 
AQARAMPVYE TFTGWDGTVK GVRERAALPR AAQDFIARVE AVAGVPVSMI TTGAERDDTI 


VLSNPFEQA

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References

[1]"Complete sequence of chromosome 3 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000442 Genomic DNA. Translation: ABI91541.1.
RefSeqYP_777875.1. NC_008392.1.

3D structure databases

ProteinModelPortalQ0B2T2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0B2T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4314901.
GenomeReviewsGene locus Bamb_5997 in contig CP000442_GR.
KEGGbam:Bamb_5997.
NMPDRfig|339670.3.peg.3572.
PATRIC19028066. VBIBurAmb61564_6277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAPIHRAID.
ProtClustDBCLSK941367.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. PurA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0B2T2_BURCM
AccessionPrimary (citable) accession number: Q0B2T2
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info