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Q8XH63 (PURA_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:CPE2622
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00011

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_00011

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00011

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095168

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding331 – 3333GTP By similarity
Nucleotide binding413 – 4153GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region299 – 3057Substrate 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 site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2241IMP By similarity
Binding site2391IMP By similarity
Binding site3031IMP By similarity
Binding site3051GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XH63 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7323E7092EF0462B

FASTA42847,590
        10         20         30         40         50         60 
MSAFVVLGAQ WGDEGKGKMT DYLAEEAEVV VRFQGGNNAG HTVEVEDKQY KLHLIPSGIL 

        70         80         90        100        110        120 
HDEKLNVIGN GVVVDPKALF TEIDYLEGLG VKVTPEKLIV SDRAHLIMPY HITLDKLKEK 

       130        140        150        160        170        180 
ARGKNDIGTT CKGIGPCYTD KYERSGIRVC DLMHKDSFAE KLRINIEMKN GYIKLLGGEE 

       190        200        210        220        230        240 
LNFDEIYNEY MAFAERLRPY VKDTSVEIYN AIQADKNVLF EGAQGMLLDI DYGTYPYVTS 

       250        260        270        280        290        300 
SNTTSCGVAS GAGIGPNMVT NAVGIAKAYT TRVGKGPFPT ELENETGDWI REKGHEYGVT 

       310        320        330        340        350        360 
TGRSRRCGWL DLVILKTTTR VCGLTSLVVT KIDTLAGLDK IQMCVGYELD GKVIDYFPAS 

       370        380        390        400        410        420 
LEDLARCKPV YEEFEGWGEE VADARSYEEL PENAKTYLRR IEEFTGTKVS IVGVGPKRNQ 


TIRVREEL 

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References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB82328.1.
RefSeqNP_563538.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XH63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE2622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB82328; BAB82328; BAB82328.
GeneID989276.
KEGGcpe:CPE2622.
PATRIC19499357. VBICloPer59675_2693.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMAISEACPI.
OrthoDBEOG68Q0QG.

Enzyme and pathway databases

BioCycCPER195102:GJFM-2753-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_CLOPE
AccessionPrimary (citable) accession number: Q8XH63
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: March 1, 2002
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways