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Reviewed, UniProtKB/Swiss-Prot P29726 (PURA_BACSU)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase
Gene names
Name: purA
Ordered Locus Names: BSU40420
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. 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.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

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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: HAMAP

   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095146

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1391 By similarity
Active site1461 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Experimental info

Sequence conflict245 – 25612AVSQS…VSARP → GGVTIGSGVGPT in BAA05174. Ref.2
Sequence conflict3041P → R in BAA05174. Ref.2
Sequence conflict3041P → R in CAB16079. Ref.2
Sequence conflict3451R → A in BAA05174. Ref.2
Sequence conflict3451R → A in CAB16079. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P29726-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 73FA687EBA35D13C

FASTA43047,910
        10         20         30         40         50         60 
MSSVVVVGTQ WGDEGKGKIT DFLSENAEVI ARYQGGNNAG HTIKFDGITY KLHLIPSGIF 

        70         80         90        100        110        120 
YKDKTCVIGN GMVVDPKALV TELAYLHERN VSTDNLRISN RAHVILPYHL KLDEVEEERK 

       130        140        150        160        170        180 
GANKIGTTKK GIGPAYMDKA ARIGIRIADL LDRDAFAEKL ERNLEEKNRL LEKMYETEGF 

       190        200        210        220        230        240 
KLEDILDEYY EYGQQIKKYV CDTSVVLNDA LDEGRRVLFE GAQGVMLDID QGTYPFVTSS 

       250        260        270        280        290        300 
NPVAAVSQSV LVSARPKIKH VVGVSKAYTT RVGDGPFPTE LKDEIGDQIR EVGREYGTTT 

       310        320        330        340        350        360 
GRPPRVGWFD SVVVRHARRV SGITDLSLNS IDVLAGIETL KICVRYRYKG EIIEEFPASL 

       370        380        390        400        410        420 
KALAECEPVY EEMPGWTEDI TGAKSLSELP ENARHYLERV SQLTGIPLSI FSVGPDRSQT 

       430 
NVLRSVYRAN

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References

« Hide 'large scale' references
[1]"Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP."
Maentsaelae P., Zalkin H.
J. Bacteriol. 174:1883-1890(1992) [PubMed: 1312531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / DE1.
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

M83690 Genomic DNA. Translation: AAA22203.1.
D26185 Genomic DNA. Translation: BAA05174.1.
AL009126 Genomic DNA. Translation: CAB16079.1.
PIRA42280. S65968.
RefSeqNP_391922.1.

3D structure databases

HSSPHSSP built from PDB template 1ADE based on UniProtKB P12283.
ModBaseSearch...

Genome annotation databases

GeneID937805.
GenomeReviewsGene locus BSU40420 in contig AL009126_GR.
KEGGbsu:BSU40420.

Organism-specific databases

SubtiListBG10002. purA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP29726.

Enzyme and pathway databases

BioCycBSUB224308:BSU4039-MON.
BRENDA6.3.4.4. 150.

Family and domain databases

HAMAPMF_00011.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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...

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Entry information

Entry namePURA_BACSU
AccessionPrimary (citable) accession number: P29726
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents