Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8TYQ7 (Q8TYQ7_METKA) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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 AAM01452.1
Ordered Locus Names:MK0235
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length346 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 binding16 – 227GTP By similarity HAMAP MF_00011
Nucleotide binding46 – 483GTP By similarity HAMAP MF_00011
Nucleotide binding294 – 2963GTP By similarity HAMAP MF_00011
Nucleotide binding334 – 3363GTP By similarity HAMAP MF_00011
Region17 – 204IMP binding By similarity HAMAP MF_00011
Region44 – 474IMP binding By similarity HAMAP MF_00011
Region262 – 2687Substrate binding By similarity HAMAP MF_00011

Sites

Active site171Proton acceptor By similarity HAMAP MF_00011
Active site471Proton donor By similarity HAMAP MF_00011
Metal binding171Magnesium By similarity HAMAP MF_00011
Metal binding461Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1311IMP By similarity HAMAP MF_00011
Binding site1451IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site1831IMP By similarity HAMAP MF_00011
Binding site1991IMP By similarity HAMAP MF_00011
Binding site2661IMP By similarity HAMAP MF_00011
Binding site2681GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
Q8TYQ7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 73C8126BF0CF1196

FASTA34637,631
        10         20         30         40         50         60 
MRDRGHVSVV AGGQWGDEGK GKIVAYLAVQ DEPEVIARAG VGPNAGHTVR VNGEDYGLRQ 

        70         80         90        100        110        120 
IPCGFPHEEA ELAIGPGVLV NPEVLLDEVE RLSRFRVDDR LIVDERCAII EPKHIEAERA 

       130        140        150        160        170        180 
SKHLSDEIDT TGTGCGPANA DRALRKAKLA RDVDELSEFL GDVPGLVNEA IDAGEDVLIE 

       190        200        210        220        230        240 
GTQGFGLSLY HGIDYPYVTS KDTTASAFAS DVGVGPTRID DVYVVFKAYA TRVGEGPFPT 

       250        260        270        280        290        300 
ELSREEVIEK FGEEILEVER GTVTGRPRRI GEFDFEMAKR ACVINGATQV AITCIDRRFP 

       310        320        330        340 
DAAEAETWHE LPTEAKKFVE KVEEAVGVPV TIVSTGPELE HTVDLR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM01452.1.
RefSeqNP_613522.1. NC_003551.1.

3D structure databases

HSSPHSSP built from PDB template 1ADE based on UniProtKB P12283.
ProteinModelPortalQ8TYQ7.
SMRQ8TYQ7. Positions 7-346.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1477538.
GenomeReviewsGene locus MK0235 in contig AE009439_GR.
KEGGmka:MK0235.
NMPDRfig|190192.1.peg.235.

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK04293.

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. 3 hits.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ8TYQ7_METKA
AccessionPrimary (citable) accession number: Q8TYQ7
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)