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Q12ZI9 (PURA_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:Mbur_0119
OrganismMethanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length423 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 – 423423Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000856

Regions

Nucleotide binding11 – 177GTP By similarity
Nucleotide binding39 – 413GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Nucleotide binding412 – 4143GTP By similarity
Region12 – 154IMP binding By similarity
Region37 – 404IMP binding By similarity
Region298 – 3047Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Active site401Proton donor By similarity
Metal binding121Magnesium By similarity
Metal binding391Magnesium; via carbonyl oxygen By similarity
Binding site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3021IMP By similarity
Binding site3041GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12ZI9 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 3EC11067A903B6BD

FASTA42346,094
        10         20         30         40         50         60 
MFTILTGSQF GDEGKGKIVD LLSKDYDLVV RFQGGDNAGH TVVVGDDVYK LHLIPSGFLL 

        70         80         90        100        110        120 
DSRVLIGPGT VLNPEVLAEE IDMLEKTGVE VSSDKLGIDA KTSIIMPYHV ELDSLRESLR 

       130        140        150        160        170        180 
KEKIGTTKKG IGFAYVDKIA RDEVRMSDLV DSEILMNRLT EMAASKEAAI RELGGDPSIV 

       190        200        210        220        230        240 
TDSELMDKYV KLGQRLAPYV TDVSYEINKA ISEGKNVLAE GAQGTFLDVI HGTQKFVTSS 

       250        260        270        280        290        300 
STIAGSACAN LGVGPTKVDE VLGIVKAYIT RVGEGPLPTE LHDEAGAHLH DVGHEFGTTT 

       310        320        330        340        350        360 
GRSRRCGWFD LPLLKKAINL NGYTSVALTK LDVLSDLDVV KVCVAYDLNG ERLDYPPEDT 

       370        380        390        400        410        420 
SLLSMCKPIY DELEGWSDDL TGVKRYEDIA RAAHDYVEKL EGMMGVPIKY VSVGPGREQT 


FEK 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51137.1.
RefSeqYP_564887.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12ZI9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12ZI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3998228.
GenomeReviewsGene locus Mbur_0119 in contig CP000300_GR.
KEGGmbu:Mbur_0119.
NMPDRfig|259564.8.peg.110.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04146.
HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK13786.

Enzyme and pathway databases

BioCycMBUR259564:MBUR_0119-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. 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_METBU
AccessionPrimary (citable) accession number: Q12ZI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 38 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