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O29417 (PURA_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. 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
Short name=AMPSase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:purA
Ordered Locus Names:AF_0841
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length337 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 – 337337Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095266

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding42 – 443GTP By similarity
Nucleotide binding281 – 2833GTP By similarity
Nucleotide binding321 – 3233GTP By similarity
Region13 – 164IMP binding By similarity
Region40 – 434IMP binding By similarity
Region249 – 2557Substrate 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 site1241IMP By similarity
Binding site1381IMP; shared with dimeric partner By similarity
Binding site1761IMP By similarity
Binding site1911IMP By similarity
Binding site2531IMP By similarity
Binding site2551GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
O29417 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C232E7D044DA3F9E

FASTA33736,563
        10         20         30         40         50         60 
MGATIIVGGF WGDEGKGKIV AHVAHSDKPV IIARGGVGPN AGHTVEIDGQ KFGVRMIPSG 

        70         80         90        100        110        120 
FVYKDAKLLI GAGVLVNPEV FLKEVELLKV GDRARVDYRC AIIEPKHIEA DKGSEHLSKK 

       130        140        150        160        170        180 
IGTTGTGCGP ANVDRVNRVA KQAKDIPELK DYLADVPLEV NQAIENGQFV LIEGSQGFGL 

       190        200        210        220        230        240 
SLYYGTYPYV TSKDTTASAI ASDVGVGPTR VDDVIVVFKC FPTRVGAGPF PTEMPQEEAE 

       250        260        270        280        290        300 
KLGIVEYGTV TGRRRRIGYW DGEFARYSAM VNGATQVAIT GVDKLDKECY GVTEWEKLTP 

       310        320        330 
KAKKFIEQVE EDVRVPVTLI STGPELKQII DLRKEKL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB90398.1.
PIRA69355.
RefSeqNP_069675.1. NC_000917.1.

3D structure databases

ProteinModelPortalO29417.
SMRO29417. Positions 1-333.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1484060.
GenomeReviewsGene locus AF_0841 in contig AE000782_GR.
KEGGafu:AF0841.
NMPDRfig|224325.1.peg.834.
TIGRAF_0841.

Phylogenomic databases

HOGENOMHBG658237.
OMAIDPHVGI.
ProtClustDBPRK04293.

Enzyme and pathway databases

BioCycAFUL224325:AF_0841-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_ARCFU
AccessionPrimary (citable) accession number: O29417
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 84 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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