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A0RXL8 (A0RXL8_CENSY) Unreviewed, UniProtKB/TrEMBL

Last modified September 21, 2011. Version 37. Feed History...

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

Protein namesRecommended name:
Adenylosuccinate synthetase HAMAP MF_00011
Short name=AMPSase HAMAP MF_00011
Short name=AdSS HAMAP MF_00011
EC=6.3.4.4 HAMAP MF_00011
Alternative name(s):
IMP--aspartate ligase HAMAP MF_00011
Gene names
Name:purA HAMAP MF_00011
Ordered Locus Names:CENSYa_1463
OrganismCenarchaeum symbiosum (strain A)
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaea › Thaumarchaeota › Cenarchaeales › Cenarchaeaceae › Cenarchaeum

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis By similarity. RuleBase RU000520

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 RuleBase RU000520

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 RuleBase RU000520

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family. RuleBase RU004163 HAMAP MF_00011

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 187GTP By similarity HAMAP MF_00011
Nucleotide binding42 – 443GTP By similarity HAMAP MF_00011
Nucleotide binding280 – 2823GTP By similarity HAMAP MF_00011
Nucleotide binding320 – 3223GTP By similarity HAMAP MF_00011
Region13 – 164IMP binding By similarity HAMAP MF_00011
Region40 – 434IMP binding By similarity HAMAP MF_00011
Region248 – 2547Substrate binding By similarity HAMAP MF_00011

Sites

Active site131Proton acceptor By similarity HAMAP MF_00011
Active site431Proton donor By similarity HAMAP MF_00011
Metal binding131Magnesium By similarity HAMAP MF_00011
Metal binding421Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1231IMP By similarity HAMAP MF_00011
Binding site1371IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site1751IMP By similarity HAMAP MF_00011
Binding site1901IMP By similarity HAMAP MF_00011
Binding site2521IMP By similarity HAMAP MF_00011
Binding site2541GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
A0RXL8 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: C94527D0D1CB0E86

FASTA33835,809
        10         20         30         40         50         60 
MPCTVVVGGF FGDEGKGKII SHMAQNDGPS IIVRGGAGPN AGHTIRDGDK VYKVRMLPSG 

        70         80         90        100        110        120 
FLNKDAKVMI GPGVVIDPVV LKAEIEEFGV RGRAFVDANC GIIEEEHKKL DSGGDLKGRI 

       130        140        150        160        170        180 
GSTGSGTGPA NAARAMRTLR LAGDEPRLLR LLKDVPRAVN TALDDGETIL AEGTQGTFLS 

       190        200        210        220        230        240 
LWHGTYPYVT TKDVTASGIC ADIGIGPRRV DEVVVVFKSY VTRVGTGPLE GELDDKEVEK 

       250        260        270        280        290        300 
RGWGEFGTVT GRPRRAADFD FELAGRAVML NGATQAAITK LDVRFPACKG ITSYGELPME 

       310        320        330 
ARTFVASVEE RLGVPVTMLG TGPDKAEIVD RRVGAAQG

« Hide

References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed: 17114289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DP000238 Genomic DNA. Translation: ABK78085.1.

3D structure databases

ProteinModelPortalA0RXL8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA0RXL8_CENSY
AccessionPrimary (citable) accession number: A0RXL8
Entry history
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: September 21, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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