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UniProtKB/Swiss-Prot entry P29726


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PURA_BACSU
Primary accession number P29726
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 75)
Name and origin of the protein
Protein name Adenylosuccinate synthetase
Synonyms EC 6.3.4.4
IMP--aspartate ligase
AdSS
AMPSase
Gene name
Name: purA
OrderedLocusNames: BSU40420
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1312531 [NCBI, ExPASy, EBI, Israel, Japan]
Maentsaelae P., Zalkin H.;
"Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP.";
J. Bacteriol. 174:1883-1890(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
DOI=10.1093/dnares/1.1.1; PubMed=7584024 [NCBI, ExPASy, EBI, Israel, Japan]
Ogasawara N., Nakai S., Yoshikawa H.;
"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin.";
DNA Res. 1:1-14(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M83690; AAA22203.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26185; BAA05174.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99124; CAB16079.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S65968; A42280.
RefSeq NP_391922.1; -.
3D structure databases
HSSP P12283; 1ADE. [HSSP ENTRY / PDB]
ModBase P29726.
Enzyme and pathway databases
BioCyc BSUB224308:BSU4039-MON; -.
Organism-specific databases
SubtiList BG10002; purA. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004019; Molecular function: adenylosuccinate synthase activity (inferred from electronic annotation from HAMAP).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00011; -; 1.
PBIL [Tree]
InterPro IPR001114; AdlSucc_Synth.
Graphical view of domain structure.
PANTHER PTHR11846; Asucc_synthtase; 1.
Pfam PF00709; Adenylsucc_synt; 1.
Pfam graphical view of domain structure.
ProDom PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00184; purA; 1.
PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.
BLOCKS P29726.
ProtoNet P29726.
Genome annotation databases
GeneID 937805; -.
GenomeReviews AL009126_GR; BSU40420.
KEGG bsu:BSU40420; -.
Phylogenomic databases
HOGENOM P29726; -.
Genome annotation databases
CMR P29726; BSU40420.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   430  430     Adenylosuccinate synthetase. PRO_0000095146
NP_BIND   12    18  7     GTP (Potential). 
ACT_SITE   139   139        By similarity. 
ACT_SITE   146   146        By similarity. 
METAL   13    13        Magnesium (By similarity). 
METAL   40    40        Magnesium; via carbonyl oxygen (By similarity). 
CONFLICT   245   256        AVSQSVLVSARP -> GGVTIGSGVGPT (in Ref. 2; BAA05174). 
CONFLICT   304   304        P -> R (in Ref. 2; BAA05174/CAB16079). 
CONFLICT   345   345        R -> A (in Ref. 2; BAA05174/CAB16079). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 47910 Da [This is the MW of the unprocessed precursor] CRC64: 73FA687EBA35D13C [This is a checksum on the sequence]
        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 

P29726 in FASTA format

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