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Q5F9J5 (PURA_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 60. 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:NGO0398
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length434 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 committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00011

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_00011

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00011

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000224296

Regions

Nucleotide binding15 – 217GTP By similarity
Nucleotide binding43 – 453GTP By similarity
Nucleotide binding335 – 3373GTP By similarity
Nucleotide binding418 – 4203GTP By similarity
Region16 – 194IMP binding By similarity
Region41 – 444IMP binding By similarity
Region303 – 3097Substrate binding By similarity

Sites

Active site161Proton acceptor By similarity
Active site441Proton donor By similarity
Metal binding161Magnesium By similarity
Metal binding431Magnesium; via carbonyl oxygen By similarity
Binding site1331IMP By similarity
Binding site1471IMP; shared with dimeric partner By similarity
Binding site2281IMP By similarity
Binding site2431IMP By similarity
Binding site3071IMP By similarity
Binding site3091GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5F9J5 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 9E02DE741966037B

FASTA43445,982
        10         20         30         40         50         60 
MAMAKNVVVI GAQWGDEGKG KIVDWLAEEA GGVVRFQGGH NAGHTLVVGG KKTILRLIPS 

        70         80         90        100        110        120 
GILHEGLDCF IGSGVVVSPE ALLGEIDELN AAGVKNVEGR LKIAPTCPLI LPYHIALDQA 

       130        140        150        160        170        180 
REASRGKGKI GTTGRGIGPA YEDKVARRAI RAADLLHPEK LREKLDAVLA YYNVQLQYLH 

       190        200        210        220        230        240 
NAGPVKAEDV MAVIEKVAPR IAPMIADVSR VLNEKNKNGE KLLFEGAQGA LLDIDYGTYP 

       250        260        270        280        290        300 
FVTSSNCLAG AASAGAGVGP QMLDYVLGIV KAYTTRVGSG PFPTELFDEV GAGLAERGHE 

       310        320        330        340        350        360 
FGSVTGRARR CGWFDAAALK RSIQINGISG MCITKLDVMD GVETINICVG YELPGGGKTD 

       370        380        390        400        410        420 
ILPCGSDAVE TCKPIYETMP GWRESTVGVK SYDALPANAK AYLKRIEEVC GAPVAIVSTG 

       430 
PDREETIVLH HPFA

« Hide

References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004969 Genomic DNA. Translation: AAW89142.1.
RefSeqYP_207554.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5F9J5.
SMRQ5F9J5. Positions 4-434.
ModBaseSearch...

Protein-protein interaction databases

STRING242231.NGO0398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW89142; AAW89142; NGO0398.
GeneID3283011.
KEGGngo:NGO0398.
PATRIC20333803. VBINeiGon24812_0479.

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMALDYYNFQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycNGON242231:GI2G-377-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_NEIG1
AccessionPrimary (citable) accession number: Q5F9J5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 15, 2005
Last modified: May 29, 2013
This is version 60 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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