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Q7WHP1 (PURA_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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
Synonyms:adeK
Ordered Locus Names:BB3165
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length435 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 – 435435Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095149

Regions

Nucleotide binding17 – 237GTP By similarity
Nucleotide binding45 – 473GTP By similarity
Nucleotide binding336 – 3383GTP By similarity
Nucleotide binding418 – 4203GTP By similarity
Region18 – 214IMP binding By similarity
Region43 – 464IMP binding By similarity
Region304 – 3107Substrate binding By similarity

Sites

Active site181Proton acceptor By similarity
Active site461Proton donor By similarity
Metal binding181Magnesium By similarity
Metal binding451Magnesium; via carbonyl oxygen By similarity
Binding site1341IMP By similarity
Binding site1481IMP; shared with dimeric partner By similarity
Binding site2291IMP By similarity
Binding site2441IMP By similarity
Binding site3081IMP By similarity
Binding site3101GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WHP1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 19BBF6EEF321A2C2

FASTA43546,841
        10         20         30         40         50         60 
MIRKMSKNVV VIGTQWGDEG KGKIVDWLAE SVQGVVRFQG GHNAGHTLWI NGKKTILRLI 

        70         80         90        100        110        120 
PSGIMHDGVT CFIGNGVVLS PEALLREIEE LEAAGLDVRS RLQVSEICTL ILPYHVAVDK 

       130        140        150        160        170        180 
AREARKGEGK IGTTGRGIGP AYEDKVARRA LRVQDLFNPA LFDEKLAEVL DYHNFVLTQY 

       190        200        210        220        230        240 
LGAEPVSANE VRDQAMALAP ALAPMVRDVS SNLFALQQEG KNLLFEGAQG ALLDVDHGTY 

       250        260        270        280        290        300 
PFVTSSNCVA GAASAGAGVG PQALQYVLGI TKAYTTRVGS GPFPTELVDE IGTRLATIGK 

       310        320        330        340        350        360 
EFGSVTGRPR RCGWFDGAAL KRSVRLNGIS GLCITKLDVL DGLETIQLGV GYRVNGEFRD 

       370        380        390        400        410        420 
VLPYGAHAVA QAQAVLEELP GWTESTVGIT EYSKLPVNAR RYLERVAEVC GVPIDLVSTG 

       430 
PDRNETIVLR HPFKG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640446 Genomic DNA. Translation: CAE33657.1.
RefSeqNP_889701.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WHP1.
SMRQ7WHP1. Positions 6-434.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2660561.
GenomeReviewsGene locus BB3165 in contig BX470250_GR.
KEGGbbr:BB3165.
NMPDRfig|257310.1.peg.3148.
PATRIC21139717. VBIBorBro124907_3226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ7WHP1.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBBRO257310:BB3165-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_BORBR
AccessionPrimary (citable) accession number: Q7WHP1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 54 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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