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A7I467 (A7I467_METB6) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 35. 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:Mboo_0004
OrganismMethanoregula boonei (strain 6A8) [Complete proteome] [HAMAP]
Taxonomic identifier456442 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Genera incertae sedis › Methanoregula

Protein attributes

Sequence length337 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 binding281 – 2833GTP By similarity HAMAP MF_00011
Nucleotide binding321 – 3233GTP By similarity HAMAP MF_00011
Region13 – 164IMP binding By similarity HAMAP MF_00011
Region40 – 434IMP binding By similarity HAMAP MF_00011
Region249 – 2557Substrate 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 site1241IMP By similarity HAMAP MF_00011
Binding site1381IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site1761IMP By similarity HAMAP MF_00011
Binding site1911IMP By similarity HAMAP MF_00011
Binding site2531IMP By similarity HAMAP MF_00011
Binding site2551GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
A7I467 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: AA4EF3DE56D901B0

FASTA33736,166
        10         20         30         40         50         60 
MSCSIIVGGF FGDEGKGKIV AHIAHADEPV IISRGGVGPN AGHTVQIGDR EYGVRMVPSG 

        70         80         90        100        110        120 
FVYKKAKLCI GSGVLVDPRV LKHEVETLGV KGRVFVDKRC GIITEDHIAR DKGSAHLSKK 

       130        140        150        160        170        180 
IGSTGSGCGP ANSDRVMRIS PQAKDVPELK EYLLDVPKAI DDALKAGNEV LLEGTQGFGI 

       190        200        210        220        230        240 
SLYYGTYPFV TSKDTSASQI AADNGVGPTK IDDVIVVFKA YPTRVGEGPF STEMSAEKSD 

       250        260        270        280        290        300 
AMGIQEFGTV THRKRRIGGW DGEMARYSAM INGCTQAAIT GIDRVDKDCF GITEYSKLTR 

       310        320        330 
KAREFLKTAE DDIGSPVTLI STGPEMSQII DIRKEYA

« Hide

References

[1]"Complete sequence of Candidatus Methanoregula boonei 6A8."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Zinder S., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 6A8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000780 Genomic DNA. Translation: ABS54528.1.
RefSeqYP_001403171.1. NC_009712.1.

3D structure databases

ProteinModelPortalA7I467.
SMRA7I467. Positions 1-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7I467.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5412087.
GenomeReviewsGene locus Mboo_0004 in contig CP000780_GR.
KEGGmbn:Mboo_0004.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04146.
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. 2 hits.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA7I467_METB6
AccessionPrimary (citable) accession number: A7I467
Entry history
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 16, 2011
This is version 35 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