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Q18JL8 (Q18JL8_HALWD) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 50. 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 EMBL CAJ51788.1
Ordered Locus Names:HQ1660A
OrganismHaloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloquadratum

Protein attributes

Sequence length443 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. HAMAP MF_00011 RuleBase RU004163

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding11 – 177GTP By similarity HAMAP MF_00011
Nucleotide binding39 – 413GTP By similarity HAMAP MF_00011
Nucleotide binding339 – 3413GTP By similarity HAMAP MF_00011
Nucleotide binding424 – 4263GTP By similarity HAMAP MF_00011
Region12 – 154IMP binding By similarity HAMAP MF_00011
Region37 – 404IMP binding By similarity HAMAP MF_00011
Region307 – 3137Substrate binding By similarity HAMAP MF_00011

Sites

Active site121Proton acceptor By similarity HAMAP MF_00011
Active site401Proton donor By similarity HAMAP MF_00011
Metal binding121Magnesium By similarity HAMAP MF_00011
Metal binding391Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1271IMP By similarity HAMAP MF_00011
Binding site1411IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site2271IMP By similarity HAMAP MF_00011
Binding site2421IMP By similarity HAMAP MF_00011
Binding site3111IMP By similarity HAMAP MF_00011
Binding site3131GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
Q18JL8 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 31E0561BDEE1FBA1

FASTA44347,855
        10         20         30         40         50         60 
MTVTIVGSQL GDEGKGALVD LWGGGADVVA RYQGGDNAGH TVVEDGDEYK LSLVPSGAVR 

        70         80         90        100        110        120 
DKIGVLGNGC VINLKTLFSE IDDLRERGLT PDVRVARRAH VIMPYHRVLD GIEEDAKSDS 

       130        140        150        160        170        180 
DLEAGTTGRG IGPTYEDKVG RRGVRVGDLL DPSVLRDRLE YVVPQKRALA ENIFGVDTSE 

       190        200        210        220        230        240 
AFDVESLFSE YRQLGKRLTE EDMTVNAGEF LNEHLNHDST ILFEGAQGTS IDIDHGIYPY 

       250        260        270        280        290        300 
VTSSNPTAGG AATGTGISPT VIGQGEVVGI IKAYLSRVGT GPLPTELTGT DEALADHIRE 

       310        320        330        340        350        360 
KGGEFGTVTG RPRRIGWLDI PMLRHATRSN GFTGLVINHI DVLAGLDEVC VGHSYDLNGE 

       370        380        390        400        410        420 
EQFTIPATTE RWAECEPNLR SFDPWDSVAW SNVATEGYEA IPANAQQYLE YLTNELDTPI 

       430        440 
YAIGVGPDRA ETIELVNPFD IDA

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References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180088 Genomic DNA. Translation: CAJ51788.1.
RefSeqYP_657428.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18JL8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ18JL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4194528.
GenomeReviewsGene locus HQ1660A in contig AM180088_GR.
KEGGhwa:HQ1660A.
NMPDRfig|362976.6.peg.667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04146.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ18JL8.
ProtClustDBPRK13785.

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 nameQ18JL8_HALWD
AccessionPrimary (citable) accession number: Q18JL8
Entry history
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info