Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2NFM9 (PURA_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase

Short name=AMPSase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:purA
Ordered Locus Names:Msp_0986
OrganismMethanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000861

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding42 – 443GTP By similarity
Nucleotide binding284 – 2863GTP By similarity
Nucleotide binding324 – 3263GTP By similarity
Region13 – 164IMP binding By similarity
Region40 – 434IMP binding By similarity
Region252 – 2587Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site431Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding421Magnesium; via carbonyl oxygen By similarity
Binding site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site1791IMP By similarity
Binding site1941IMP By similarity
Binding site2561IMP By similarity
Binding site2581GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NFM9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 716072FEF3FC1DD3

FASTA34137,346
        10         20         30         40         50         60 
MTCTILVGGQ WGDEGKGKCI TYFCTQDKPE IIARAGVGPN AGHSVEFNGE KYGLRLTPSG 

        70         80         90        100        110        120 
FFNKEARLLI GAGVLVNPEV FEHELEYLSK YAVEGRTFMD ANCAIITDKH TKQDKDSAYL 

       130        140        150        160        170        180 
SKKIGTTGSG CGPANADRIN RTIDYAKDVP ELEKYITDVP SEINKAIDEG KDVFIEGSQG 

       190        200        210        220        230        240 
FGLSLYYGTY PYVTSKDTCA STAAADVGVG PTKVDEVIVI FKSYITRVGE GPFPTEISPE 

       250        260        270        280        290        300 
EAEKMGIEEY GVVTGRKRRV GLFDKDFAKR SCMINGATQI ALTCIDRLYP ECAKVNKYED 

       310        320        330        340 
LSQEARDYIE DIEENVGVPI TIISTGPDLA DTIDLRNEKL N 

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed: 16385054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 3091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC57374.1.
RefSeqYP_448017.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NFM9.
SMRQ2NFM9. Positions 1-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NFM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3855974.
GenomeReviewsGene locus Msp_0986 in contig CP000102_GR.
KEGGmst:Msp_0986.
NMPDRfig|339860.6.peg.945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04146.
HOGENOMHBG658237.
OMAIDPHVGI.
ProtClustDBPRK04293.

Enzyme and pathway databases

BioCycMSTA339860:MSP_0986-MONOMER.

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. 3 hits.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_METST
AccessionPrimary (citable) accession number: Q2NFM9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: November 16, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families