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Q8TPJ2 (PURA1_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase 1
Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase 1
Gene names
Name:purA1
Ordered Locus Names:MA_1919
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length424 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
Reference 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 – 424424Adenylosuccinate synthetase 1 HAMAP MF_00011
PRO_0000095269

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding413 – 4153GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site411Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity
Binding site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site2361IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TPJ2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: AFE917A824D8EB35

FASTA42446,812
        10         20         30         40         50         60 
MSVTVIVGAQ CGDEGKGKMV DLIAQDYDLV IRFQGGDNAG HTVVNQYGTF KMHLIPCGIF 

        70         80         90        100        110        120 
NQNAISLVGT GMVVNPDELQ KEMKQITSAG MSVDNLKIST RANILMPYHR DLDELNEQSG 

       130        140        150        160        170        180 
GMSIGTTKRG IGPAYAGRAT RTNIRFGDLA HQDYLKSHFE KVLPAINHQL SFFGAAQYTV 

       190        200        210        220        230        240 
DQLCEYCSNW YKLYNEHIVD AFTLIHNMMK ENKRILFEGQ LGVMKDIDLG IYPFVTSSNP 

       250        260        270        280        290        300 
IAAYAAVSSG IPARSITSVI GVAKAFSSQV GDGPFPTEVL DNCIVSLRGT GKNIDDEFGA 

       310        320        330        340        350        360 
RTGRPRRLGW LDIPVLRYAH TINGFDTLAI CKLDKMDSLP EIKICTSYRY QDQILSVFPD 

       370        380        390        400        410        420 
TEILGQVKAE YETLPGWECT TRGVNSFDDL PENAKSYIKR IEELVGVPVK YIGVGPARSD 


VIIR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE010299 Genomic DNA. Translation: AAM05323.1.
RefSeqNP_616843.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8TPJ2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1473808.
GenomeReviewsGene locus MA_1919 in contig AE010299_GR.
KEGGmac:MA1919.
NMPDRfig|188937.1.peg.1869.

Phylogenomic databases

HOGENOMHBG658237.
OMAMESWSED.

Enzyme and pathway databases

BioCycMACE188937:MA1919-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 namePURA1_METAC
AccessionPrimary (citable) accession number: Q8TPJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 59 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

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