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Q81JI9 (PURA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 68. 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

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:BA_5716, GBAA_5716, BAS5320
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length429 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
Reference 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 – 429429Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095143

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
Q81JI9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0E44D5BA065649D5

FASTA42947,424
        10         20         30         40         50         60 
MSSVVVVGTQ WGDEGKGKIT DFLSEHAEVV ARYQGGNNAG HTIVFGGVKY KLHLIPSGIF 

        70         80         90        100        110        120 
YKEKICVIGN GLVVDPKALL EELKYLHDRG VSTDNLRVSN RAHVILPYHL KQDELEEASK 

       130        140        150        160        170        180 
GDNKIGTTKK GIGPAYMDKA ARIGIRMADL LDREAFKEKL EQNLAQKNRL FEKMYDTEGF 

       190        200        210        220        230        240 
SVDEIFEEYF EYGQQIAQYV CDTSVVLNDA LDNNHRVLFE GAQGVMLDID HGTYPFVTSS 

       250        260        270        280        290        300 
NPIAGGVTVG TGVGPAKVTR VVGVCKAYTS RVGDGPFPTE LHDEIGHQIR EVGREYGTTT 

       310        320        330        340        350        360 
GRPRRVGWFD SVVVRHARRV SGLTDLSLNS IDVLTGIPTL KICVAYKCDG KVIDEVPANL 

       370        380        390        400        410        420 
NILAKCEPVY EELPGWTEDI TGVRSLDELP ENARKYVERV SELTGIQLSM FSVGPDRNQT 


NIVRNVYEA 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP29348.1.
AE017334 Genomic DNA. Translation: AAT34877.1.
AE017225 Genomic DNA. Translation: AAT57607.1.
RefSeqNP_847862.1. NC_003997.3.
YP_022402.1. NC_007530.2.
YP_031557.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81JI9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81JI9. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000010316; EBBACP00000010072; EBBACG00000010308.
EBBACT00000015895; EBBACP00000015516; EBBACG00000015887.
EBBACT00000020874; EBBACP00000020359; EBBACG00000020865.
GeneID1085481.
2816054.
2852842.
GenomeReviewsGene locus BA_5716 in contig AE016879_GR.
Gene locus BAS5320 in contig AE017225_GR.
Gene locus GBAA_5716 in contig AE017334_GR.
KEGGban:BA_5716.
bar:GBAA_5716.
bat:BAS5320.
TIGRBA_5716.
GBAA_5716.

Phylogenomic databases

GeneTreeEBGT00050000001253.
HOGENOMHBG658237.
OMADYVVRYQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBANT260799:BAS5320-MONOMER.
BANT261594:GBAA5716-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_BACAN
AccessionPrimary (citable) accession number: Q81JI9
Secondary accession number(s): Q6HQ31, Q6KJH5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 68 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