Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9PG47 (PURA_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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:XF_0455
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

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 AAF83265.1 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_0000095264

Regions

Nucleotide binding13 – 197GTP By similarity
Nucleotide binding41 – 433GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding414 – 4163GTP By similarity
Region14 – 174IMP binding By similarity
Region39 – 424IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site141Proton acceptor By similarity
Active site421Proton donor By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity
Binding site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PG47 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: EAF0CEE854B24119

FASTA43046,671
        10         20         30         40         50         60 
MGQSVVVLGA QWGDEGKGKI VDLLTEEIGA VVRFQGGHNA GHTLVINGKK TVLHLIPSGI 

        70         80         90        100        110        120 
LRNGVLCLIG NGVVISPAAL RKEIEELEDT GLEIRSRLKI SPAAPLIMEY HIALDQAREK 

       130        140        150        160        170        180 
AAGGRAIGTT GRGIGPAYED KVGRRGIRVA DLHYPDQLAE KLRDALDYHN FVLTRYFGVD 

       190        200        210        220        230        240 
GMDFQRIYDE MLVFAEYVEP MKSDVAGILH DLRKQGKRVL FEGAQGTLLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSSTTVGGAL SGAGVGVQDI DYVLGIAKAY ATRVGGGPFP TELDDEIGQG IRDRGVEYGA 

       310        320        330        340        350        360 
STGRPRRCGW MDIVALKRAV AINGITGLCI TKLDVLDGMD KLKICIAYEY HDKRSEYAPL 

       370        380        390        400        410        420 
DAQGWEECTP VYLEFPGWNE STHGITSWEK LPPAARAYLC ALEELAGCPI GIVSTGPDRE 

       430 
HTIMLHDPFA

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF83265.1. Different initiation.
PIRB82803.
RefSeqNP_297745.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PG47.
SMRQ9PG47. Positions 2-430.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125985.
GenomeReviewsGene locus XF_0455 in contig AE003849_GR.
KEGGxfa:XF0455.
NMPDRfig|160492.1.peg.452.
PATRIC24130877. VBIXylFas578_0483.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycXFAS160492:XF0455-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_XYLFA
AccessionPrimary (citable) accession number: Q9PG47
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 27, 2002
Last modified: January 25, 2012
This is version 74 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents