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A3MSE9 (A3MSE9_PYRCJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 45. 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-Rule MF_00011
Short name=AMPSase HAMAP-Rule MF_00011
Short name=AdSS HAMAP-Rule MF_00011
EC=6.3.4.4 HAMAP-Rule MF_00011
Alternative name(s):
IMP--aspartate ligase HAMAP-Rule MF_00011
Gene names
Name:purA HAMAP-Rule MF_00011
Ordered Locus Names:Pcal_0128
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP] EMBL ABO07566.1
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum ›

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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-Rule MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_00011

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00011

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_00011

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00011

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family. HAMAP-Rule MF_00011

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding40 – 423GTP By similarity HAMAP-Rule MF_00011
Nucleotide binding276 – 2783GTP By similarity HAMAP-Rule MF_00011
Nucleotide binding316 – 3183GTP By similarity HAMAP-Rule MF_00011
Region38 – 414IMP binding By similarity HAMAP-Rule MF_00011
Region244 – 2507Substrate binding By similarity HAMAP-Rule MF_00011

Sites

Active site121Proton acceptor By similarity HAMAP-Rule MF_00011
Active site411Proton donor By similarity HAMAP-Rule MF_00011
Metal binding121Magnesium By similarity HAMAP-Rule MF_00011
Metal binding401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_00011
Binding site1211IMP By similarity HAMAP-Rule MF_00011
Binding site1351IMP; shared with dimeric partner By similarity HAMAP-Rule MF_00011
Binding site1711IMP By similarity HAMAP-Rule MF_00011
Binding site1861IMP By similarity HAMAP-Rule MF_00011
Binding site2481IMP By similarity HAMAP-Rule MF_00011
Binding site2501GTP By similarity HAMAP-Rule MF_00011

Sequences

Sequence LengthMass (Da)Tools
A3MSE9 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 627EFAD8D2672E1F

FASTA33436,460
        10         20         30         40         50         60 
MLTVVVDGFF GDTGKGKVVA YLALADKPEL CVRTGAPNAG HTVVIGGEVH VLRTLPTCFV 

        70         80         90        100        110        120 
NPTSKLAVAP GALIKVDVFL SEVERYGKGK SYVDFNTGVI EDRHVEAERR DEFLMKTVGS 

       130        140        150        160        170        180 
TGQGVGAAMV DRVLRRLRLA KDVEELRPYL ADVPSMIHEA RERGVVIEGT QGTFLSLYHG 

       190        200        210        220        230        240 
TYPYVTSRDV TASGVLSEAG VGPKAVDEVV LVFKAYVTRV GGGPLPGELP PEEAERRGWV 

       250        260        270        280        290        300 
ERGAVTGRPR RAAPFNFELA KRAVLLNTPT QIALTKVDAL FKDAAGKTRW QDLPPEARRW 

       310        320        330 
VEEVEERLGV PVTLIGTGPE PWHMVDLRRE KGRL

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000561 Genomic DNA. Translation: ABO07566.1.
RefSeqYP_001055032.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MSE9.
ModBaseSearch...

Protein-protein interaction databases

STRING410359.Pcal_0128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO07566; ABO07566; Pcal_0128.
GeneID4908480.
KEGGpcl:Pcal_0128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMAAMINGCT.
ProtClustDBPRK04293.

Enzyme and pathway databases

BioCycPCAL410359:GIX2-129-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 3 hits.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA3MSE9_PYRCJ
AccessionPrimary (citable) accession number: A3MSE9
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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