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Reviewed, UniProtKB/Swiss-Prot Q8G6T9 (PURA_BIFLO)

Last modified February 9, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase
Gene names
Name: purA
Ordered Locus Names: BL0549
OrganismBifidobacterium longum [Complete proteome] [HAMAP]
Taxonomic identifier216816 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. HAMAP MF_00011

Catalytic activity

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095148

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1391 By similarity
Active site1461 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G6T9-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6C19E08701905430

FASTA42846,452
        10         20         30         40         50         60 
MPGIVLIGAQ WGDEGKGKAT DLIGTKVDYV ARFNGGNNAG HSVVVGDESY ALHLLPSGII 

        70         80         90        100        110        120 
NPNLTPVIGN GVVVDPEVLF EEIDGLESRG IDCSHLKVSE AAHIIAPYHR TLDKVTERFL 

       130        140        150        160        170        180 
GKHKIGTTGR GIGPAYADKI NRVGIRVHDL FNADHLHDKV EASLHQKNQM LVKLYNRRPI 

       190        200        210        220        230        240 
DVDQTTEELL KLGERLKPYV ANTGLILNKA LDEGKTVLFE GAQATMLDVD HGTYPFVTSS 

       250        260        270        280        290        300 
NPTAGGACTG TGVGPTRITR VVGVSKAYVT RVGEGPFPTE LLDESGEWLR QQGHEFGVTT 

       310        320        330        340        350        360 
GRPRRCGWFD AVVNRYASQV NGLTDIVLTK LDVLAGLKEI PICVAYDVDG ERHDDMPTDQ 

       370        380        390        400        410        420 
AAFAAAKPIY ETMPGWDEDI SNCHSFDELP ATCQAYVKRL EELSGCRISA IGTGPQRDHV 


IQINSLVD 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN24373.1.
RefSeqNP_695737.1.

3D structure databases

SMRQ8G6T9. Positions 3-426.
ModBaseSearch...

Genome annotation databases

GeneID1022076.
GenomeReviewsGene locus BL0549 in contig AE014295_GR.
KEGGblo:BL0549.
NMPDRfig|206672.1.peg.504.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAIPVCVAY.
PhylomeDBQ8G6T9.

Enzyme and pathway databases

BioCycBLON206672:BL0549-MONOMER.
BRENDA6.3.4.4. 39917.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
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 namePURA_BIFLO
AccessionPrimary (citable) accession number: Q8G6T9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents