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World-2DPAGE Repository  Search by  [accession number]  [description, ID or gene]  [author names]  [spot ID / serial number]  [identification methods]  [pI / Mw range]  [combined fields]  Maps  [experimental info]  [protein list]  [graphical interface]      Databases 0001 0002 0003 0004 0005 0006 0007 0008 0009 0010 0011 0012 0014 0017 0018 0019 0020 0021 0022 0023 0024 0026 0027 0029 0030 0031 0032 0034 0035 0036 0037 0038 0039 0040 0042 0043 0044 0046 0047 0050 0051 0053 0054 0056 0059 0061 0062 0063 0066 0068 0069 0076 0077 0080 0084 0085 0088 use 'Ctrl' to select several databases Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal Exclude local DBs has only effect if a remote interface is selected

Searching in 'World-2DPAGE Repository [0002]' for entry matching: P63433 World-2DPAGE Repository (0002):  P63433 P63433 General information about the entry View entry in simple text format Entry name ACON_STAAM Primary accession number P63433 integrated into World-2DPAGE Repository (0002) on  December 7, 2005 (release 1) 2D Annotations were last modified on May 1, 2011 (version 2) General Annotations were last modified on  November 14, 2011 (version 2) Name and origin of the protein Description RecName: Full=Aconitate hydratase; Short=Aconitase; EC=4.2.1.3; AltName: Full=Citrate hydro-lyase;. Gene name Name=acnA Synonyms=citB OrderedLocusNames=SAV1350 Annotated species Staphylococcus aureus (strain Mu50 / ATCC 700699) [TaxID: 158878] Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus. References [1]   MAPPING ON GEL PubMed=17370256; DOI=10.1002/pmic.200600925; [NCBI, EBI, Israel, Japan] Plikat U., Voshol H., Dangendorf Y., Wiedmann B., Devay P., Mueller D., Wirth U., Szustakowski J., Chirn G.W., Inverardi B., Puyang X., Brown K., Kamp H., Hoving S., Ruchti A., Brendlen N., Peterson R., Buco J., Oostrum J., Peitsch M.C. ''From proteomics to systems biology of bacterial pathogens: approaches, tools, and applications'' Proteomics 7(6):992-1003 (2007) 2D PAGE maps for identified proteins How to interpret a protein STAPHY4-7 {Staphylococcus aureus, pH 4-7} Staphylococcus aureus (strain Mu50 / ATCC 700699)   map experimental info   STAPHY4-7 MAP LOCATIONS: SPOT 299: pI=5.02; Mw=115000   [identification data] SPOT 326: pI=5.06; Mw=114000   [identification data] SPOT 345: pI=5.08; Mw=113000   [identification data] AREA: SPOT 299: 650 [1] SPOT 326: 878 [1]; SPOT 345: 244 [1]. PEAK HEIGHT: SPOT 299: 13212.512 [1] SPOT 326: 26883.466 [1]; SPOT 345: 16627.384 [1]. STAPH_LSI: SPOT 299: stapha_lsi_1350 [1] SPOT 326: stapha_lsi_1350 [1]; SPOT 345: stapha_lsi_1350 [1]. MAPPING (identification): SPOT 299: Peptide mass fingerprinting [1]; SPOT 326: Peptide mass fingerprinting [1]; SPOT 345: Peptide mass fingerprinting [1]. Copyright Data from Dr. Hans Voshol, Novartis Institutes for BioMedical Research, Basel, Switzerland Cross-references UniProtKB/Swiss-Prot P63433; ACON_STAAM. World-2DPAGE Repository P63433; ACON_STAAM. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 2011_10 Entry name ACON_STAAM Primary accession number P63433 Secondary accession number(s) Q99UC8 Sequence was last modified on  October 11, 2004 (version 1) Annotations were last modified on  October 19, 2011 (version 46) Name and origin of the protein Description RecName: Full=Aconitate hydratase; Short=Aconitase; EC=4.2.1.3; AltName: Full=Citrate hydro-lyase; Gene name Name=acnA Synonyms=citB OrderedLocusNames=SAV1350 Encoded on Name=acnA; Synonyms=citB; OrderedLocusNames=SAV1350 Keywords Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; Tricarboxylic acid cycle. Copyright Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL BA000017; BAB57512.1; -; Genomic_DNA RefSeq NP_371874.1; NC_002758.2; . ProteinModelPortal P63433; -; . SMR P63433; 7-899; . STRING P63433; -; . World-2DPAGE 0002:P63433; -; . EnsemblBacteria EBSTAT00000007598; EBSTAP00000007416; EBSTAG00000007597; . GeneID 1121325; -; . GenomeReviews BA000017_GR; SAV1350; . KEGG sav:SAV1350; -; . eggNOG COG1048; -; . GeneTree EBGT00050000024545; -; . HOGENOM HBG289738; -; . OMA YSKAQGM; -; . ProtClustDB PRK09277; -; . BioCyc SAUR158878:SAV1350-MONOMER; -; . GO GO:0051539; F:4 iron; 4 sulfur cluster binding; IEA:InterPro GO GO:0003994; F:aconitate hydratase activity; IEA:EC; . GO GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC; . GO GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC; . GO GO:0046872; F:metal ion binding; IEA:UniProtKB-KW; . GO GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW; . InterPro IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3; . InterPro IPR015937; Acoase/IPM_deHydtase; . InterPro IPR001030; Acoase/IPM_deHydtase_lsu_aba; . InterPro IPR015928; Aconitase/3IPM_dehydase_swvl; . InterPro IPR006249; Aconitase/Fe_reg_prot_2; . InterPro IPR015934; Aconitase/Fe_reg_prot_2/AcnD; . InterPro IPR015932; Aconitase/IPMdHydase_lsu_aba_2; . InterPro IPR018136; Aconitase_4Fe-4S_BS; . InterPro IPR000573; AconitaseA/IPMdHydase_ssu_swvl; . Gene3D G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 3; . Gene3D G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1; . Gene3D G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1; . PANTHER PTHR11670; Aconitase-like_core; 1; . PANTHER PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1; . Pfam PF00330; Aconitase; 1; . Pfam PF00694; Aconitase_C; 1; . PRINTS PR00415; ACONITASE; . SUPFAM SSF52016; Aconitase/3IPM_dehydase_swvl; 1; . SUPFAM SSF53732; Aconitase_N; 1; . TIGRFAMs TIGR01341; Aconitase_1; 1; . PROSITE PS00450; ACONITASE_1; 1; . PROSITE PS01244; ACONITASE_2; 1; . World-2DPAGE Repository (search AC)