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Q9X0I0 (PUR8_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 lyase

Short name=ASL
EC=4.3.2.2
Alternative name(s):
Adenylosuccinase
Short name=ASase
Gene names
Name:purB
Ordered Locus Names:TM_1095
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.

Subunit structure

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. Ref.2

Sequence similarities

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Adenylosuccinate lyase
PRO_0000137886

Regions

Region4 – 52Substrate binding By similarity
Region67 – 693Substrate binding By similarity
Region68 – 692Substrate binding By similarity

Sites

Active site1411Proton acceptor Ref.2
Active site1411Proton donor/acceptor By similarity
Active site2621Proton donor/acceptor By similarity
Binding site951Substrate By similarity
Binding site2121Substrate By similarity
Binding site3011Substrate By similarity
Binding site3061Substrate By similarity
Binding site3101Substrate By similarity

Secondary structure

............................................................ 431
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X0I0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: D3ACB25D87582869

FASTA43149,873
        10         20         30         40         50         60 
MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN NAKIDVELFK 

        70         80         90        100        110        120 
KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT ANSLALVEAG KILLESLKEF 

       130        140        150        160        170        180 
CDVLWEVANR YKHTPTIGRT HGVHAEPTSF GLKVLGWYSE MKRNVQRLER AIEEVSYGKI 

       190        200        210        220        230        240 
SGAVGNYANV PPEVEEKALS YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI 

       250        260        270        280        290        300 
RHLQRTEVLE VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE 

       310        320        330        340        350        360 
RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG LVFSQRVLLK 

       370        380        390        400        410        420 
LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK KLVTKEELEE LFDISYYLKH 

       430 
VDHIFERFEK E 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway."
Toth E.A., Yeates T.O.
Structure 8:163-174(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36171.1.
PIRA72294.
RefSeqNP_228901.1. NC_000853.1.
YP_007977450.1. NC_021214.1.
YP_008991807.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3CX-ray1.80A/B2-430[»]
1C3UX-ray2.30A/B1-431[»]
ProteinModelPortalQ9X0I0.
SMRQ9X0I0. Positions 2-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36171; AAD36171; TM_1095.
GeneID15494703.
18093621.
898670.
KEGGtma:TM1095.
tmm:Tmari_1101.
PATRIC23937125. VBITheMar51294_1111.

Phylogenomic databases

eggNOGCOG0015.
KOK01756.
OMAQRSEVYE.
OrthoDBEOG686NDB.
ProtClustDBCLSK875567.

Enzyme and pathway databases

UniPathwayUPA00074; UER00132.
UPA00075; UER00336.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
InterProIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF2. PTHR11444:SF2. 1 hit.
PfamPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SMARTSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00928. purB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9X0I0.

Entry information

Entry namePUR8_THEMA
AccessionPrimary (citable) accession number: Q9X0I0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 108 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways