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A5N4D3 (PURA_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:CKL_0087
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [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 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 – 428428Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000073942

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding414 – 4163GTP 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 site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5N4D3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 156FBA57074AABC6

FASTA42847,362
        10         20         30         40         50         60 
MSAFIVLGSQ WGDEGKGKMT DYLAKDVDVV VRFQGGNNAG HTVRVGDKEY KLHIIPSGIL 

        70         80         90        100        110        120 
YKDKVNVIGN GVVLDPEALF QEIDYLEKAG VDIQPDNLMI SDRAQLIMPY HKVLDGIKER 

       130        140        150        160        170        180 
SRGKKDIGTT GKGIGPCYTD KMERSGIRVC DLINQDVFKE NLKENLKIKN DIITKVYGEE 

       190        200        210        220        230        240 
ALDFDSICDQ YIEYRKKLAP YVKDISVEVY NSIKNDKKVL FEGAQGTLLD IDYGTYPYVT 

       250        260        270        280        290        300 
SSSTIAGGVC IGAGIGPTLI TGAIGVAKAY TTRVGKGPFP TELFDDTGDW IRKSGREYGV 

       310        320        330        340        350        360 
TTGRARRCGW LDLVILKTSS RVSGLTNFAI TKIDTLGGLE KVKVCTGYKF NGKIIDYVPA 

       370        380        390        400        410        420 
SLQDLAKCEP VYEEFDGWDK DIENAKTYDE LPENAKIYLN KIEEFTNTKI SIVSVGPGRD 


QTINLNNM 

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed: 18218779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000673 Genomic DNA. Translation: EDK32164.1.
RefSeqYP_001393512.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N4D3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5N4D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5390836.
GenomeReviewsGene locus CKL_0087 in contig CP000673_GR.
KEGGckl:CKL_0087.
NMPDRfig|431943.4.peg.145.
PATRIC19461575. VBICloKlu111549_0157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMADYVQPMK.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycCKLU431943:CKL_0087-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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_CLOK5
AccessionPrimary (citable) accession number: A5N4D3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
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