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A0ZZG5 (PURA_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BAD_0067
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length428 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 – 428428Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000783

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Nucleotide binding412 – 4143GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region298 – 3047Substrate 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 site1281IMP By similarity
Binding site1421IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3021IMP By similarity
Binding site3041GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0ZZG5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: A39661BC6C24BA83

FASTA42846,638
        10         20         30         40         50         60 
MPGIVLIGAQ WGDEGKGKAT DLIGTKVDYV ARFNGGNNAG HTVVVGDESY ALHLLPSGII 

        70         80         90        100        110        120 
SPNTTPVIGN GVVVDPEVLF QEIDGLESRG VDCSRLLVSE SAHIIAPYHR VLDKVTERFL 

       130        140        150        160        170        180 
GKHKIGTTGR GIGPAYADKI NRVGIRVHDL FNAEHLHDKV EASLHQKNQM LVKLYNRRPI 

       190        200        210        220        230        240 
DVDETTDELL KLGERLKPYV ANTSLVLNKA LDEGKTVLFE GGQATMLDVD HGTYPFVTSS 

       250        260        270        280        290        300 
NPTAGGACTG TGVGPTKITR VVGVSKAYVT RVGEGPFPTE LFGEEGEWLR AQGHEYGVTT 

       310        320        330        340        350        360 
GRPRRCGWFD AVVNRYAAQV NGLTDIVLTK LDVLTGLKEI PLCVAYDVNG ERRDDMPTDQ 

       370        380        390        400        410        420 
AEFAAAKPIY ESMPGWDEDI SQVHDFNDLP KTCQDYVKRL EELSGCRISV IGTGPQRDHI 


IQINSLID

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References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009256 Genomic DNA. Translation: BAF38848.1.
RefSeqYP_908930.1. NC_008618.1.

3D structure databases

ProteinModelPortalA0ZZG5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0ZZG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4556691.
GenomeReviewsGene locus BAD_0067 in contig AP009256_GR.
KEGGbad:BAD_0067.
NMPDRfig|1680.3.peg.331.
PATRIC21099311. VBIBifAdo27973_0060.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMADYVVRYQ.
ProtClustDBPRK01117.

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_BIFAA
AccessionPrimary (citable) accession number: A0ZZG5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 36 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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