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B4S195 (PURA_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase
Short name=AMPSase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:purA
Ordered Locus Names:MADE_1002935
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas

Protein attributes

Sequence length432 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 MF_00011

Catalytic activity

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089266

Regions

Nucleotide binding13 – 197GTP By similarity
Nucleotide binding41 – 433GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding415 – 4173GTP By similarity
Region14 – 174IMP binding By similarity
Region39 – 424IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site141Proton acceptor By similarity
Active site421Proton donor By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity
Binding site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S195 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: D376ED938E150E5E

FASTA43246,717
        10         20         30         40         50         60 
MAKNVVVLGT QWGDEGKGKV VDLLTDRAKY VVRYQGGHNA GHTLVIDGEK TVLHLIPSGI 

        70         80         90        100        110        120 
LRDNVTCIIG NGVVLSPDAL MKEMTMLEER GVPVRERLKI SEACPLILPY HIALDVAREK 

       130        140        150        160        170        180 
ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFNAEDFAA KLKEVLDVHN FTLTQYYGEE 

       190        200        210        220        230        240 
AVDFEETLNG AMEVADILKA MVVDVTDELD KAHKAGLPIM FEGAQGTLLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSNTTVGGVA TGAGFGPLKL DYVLGIVKAY TTRVGSGPFP TELDCEVGQH LGVKGHEFGA 

       310        320        330        340        350        360 
TTGRKRRTGW FDAVAMKRAV QINSITGFCL TKLDVLDGLE SLQICVGYKD ADGNVKDVPP 

       370        380        390        400        410        420 
MAADGYDKVT PVYEEMPGWT DNTFGVTEFE GLPQAAKNYI KRLEELTGVP VDIVSTGPDR 

       430 
NETIVLRSPY DA

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001103 Genomic DNA. Translation: AEA96735.1.
RefSeqYP_004425733.1. NC_011138.2.

3D structure databases

ProteinModelPortalB4S195.
SMRB4S195. Positions 4-432.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4S195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10555932.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK01117.

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. 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 namePURA_ALTMD
AccessionPrimary (citable) accession number: B4S195
Secondary accession number(s): F2G7F5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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