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Q8UCN6 (PURA_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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:Atu2447
ORF Names:AGR_C_4442
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970)
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

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
Reference 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_0000095140

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding333 – 3353GTP By similarity
Nucleotide binding415 – 4173GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region301 – 3077Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site411Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity
Binding site1321IMP By similarity
Binding site1461IMP; shared with dimeric partner By similarity
Binding site2261IMP By similarity
Binding site2411IMP By similarity
Binding site3051IMP By similarity
Binding site3071GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8UCN6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 1B60F0FFBBA837DD

FASTA43246,513
        10         20         30         40         50         60 
MTNVVVVGSQ WGDEGKGKIV DWLSERADVV VRYQGGHNAG HTLVIDGISY KLSLLPSGVV 

        70         80         90        100        110        120 
RPGKLAVIGN GVVVDPHALI AEIGRLEVQG VKVTPENLRI ADNATLILSL HRELDGMRED 

       130        140        150        160        170        180 
AASNSGTKIG TTRRGIGPAY EDKVGRRAIR VMDLADMEAL SAKVDRILTH HNALRRGFGA 

       190        200        210        220        230        240 
TEVSHETIME ELGSIAERIL PFSETVWLLL DKKRRAGARI LFEGAQGSLL DIDHGTYPYV 

       250        260        270        280        290        300 
TSSNTVAGQA AAGSGMGPGS LGYILGITKA YTTRVGEGPF PTELHDEIGQ FLGEKGHEFG 

       310        320        330        340        350        360 
TVTGRKRRCG WFDAALVRQS VATNGITGIA LTKLDVLDGL DELKICVGYK LDGQEIDHLP 

       370        380        390        400        410        420 
ASQGAQARVE PIYVTLEGWK ESTVGARKWA DLPAQAIKYV RQVEELIGAP VALLSTSPER 

       430 
DDTILVTDPF ED

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE007869 Genomic DNA. Translation: AAK88184.1.
PIRAE2877.
G97653.
RefSeqNP_355399.1. NC_003062.2.

3D structure databases

ProteinModelPortalQ8UCN6.
SMRQ8UCN6. Positions 2-432.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8UCN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1134485.
GenomeReviewsGene locus Atu2447 in contig AE007869_GR.
KEGGatu:Atu2447.
PATRIC20814681. VBIAgrTum91616_2459.

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMADYVVRYQ.
PhylomeDBQ8UCN6.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycATUM176299-1:ATU2447-MONOMER.

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 namePURA_AGRT5
AccessionPrimary (citable) accession number: Q8UCN6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 68 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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