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A8I1V7 (PURA_AZOC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:AZC_4670
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Azorhizobium

Protein attributes

Sequence length430 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.

Sequence caution

The sequence BAF90668.1 differs from that shown. Reason: Erroneous initiation.

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 – 430430Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000336999

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding331 – 3333GTP By similarity
Nucleotide binding413 – 4153GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region299 – 3057Substrate 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 site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2241IMP By similarity
Binding site2391IMP By similarity
Binding site3031IMP By similarity
Binding site3051GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8I1V7 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 189F74955F4F19FC

FASTA43046,513
        10         20         30         40         50         60 
MANVVVVGSQ WGDEGKGKIV DWLSEQADVV VRFQGGHNAG HTLVVDGVTY KLSLLPSGVV 

        70         80         90        100        110        120 
RPGKLSVIGN GVVLDPQALV DELARLESQG VHVGPDRLRI AENTPLILPL HRELDALREN 

       130        140        150        160        170        180 
ASEGTRIGTT KRGIGPAYED KVGRRAIRLV DLVDPKALPA KVERLLTHHN LIRRGLGVEE 

       190        200        210        220        230        240 
VNPQALVDEL LALAPKVLPY MDRVWELLDK ARKDGKKILF EGAQGALLDI DHGTYPYVTS 

       250        260        270        280        290        300 
SNTVASSAAG GSGVGPGALD YVLGITKAYT TRVGEGPFPT ELTDEVGKTL GTKGREFGVV 

       310        320        330        340        350        360 
TGRPRRCGWF DAVLVRQTVR TCGIHGIALT KLDVLDGFDE IKVCVGYKLD GKEIDYFPSE 

       370        380        390        400        410        420 
MGAQARVEPI YETIEGWTDS TAGARSWADL PAEAVKYVRW LEELIGCPVA VLSTSPERND 

       430 
TILVHNPFQA

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43989 / DSM 5975 / ORS 571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009384 Genomic DNA. Translation: BAF90668.1. Different initiation.
RefSeqYP_001527586.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8I1V7.
SMRA8I1V7. Positions 2-430.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8I1V7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5687884.
GenomeReviewsGene locus AZC_4670 in contig AP009384_GR.
KEGGazc:AZC_4670.
PATRIC21026289. VBIAzoCau17976_4867.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycACAU438753:AZC_4670-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_AZOC5
AccessionPrimary (citable) accession number: A8I1V7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 30 of the entry and version 2 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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