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UniProtKB/Swiss-Prot entry P26901


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

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Entry information
Entry name CATA_BACSU
Primary accession number P26901
Secondary accession number P77838
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Vegetative catalase
Synonym EC 1.11.1.6
Gene name
Name: katA
Synonyms: kat, kat-19
OrderedLocusNames: BSU08820
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / YB886;
DOI=10.1016/0378-1119(91)90585-Y; PubMed=1756979 [NCBI, ExPASy, EBI, Israel, Japan]
Bol D.K., Yasbin R.E.;
"The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis.";
Gene 109:31-37(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9202460 [NCBI, ExPASy, EBI, Israel, Japan]
Cummings N.J., Connerton I.F.;
"The Bacillus subtilis 168 chromosome from sspE to katA.";
Microbiology 143:1855-1859(1997).
[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).
[4]
PROTEIN SEQUENCE OF 2-19.
STRAIN=168 / YB886;
PubMed=8180695 [NCBI, ExPASy, EBI, Israel, Japan]
Hartford O.M., Dowds B.C.A.;
"Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis.";
Microbiology 140:297-304(1994).
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
M80796; AAA22402.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82044; CAB04807.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99108; CAB12710.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JH0532; JH0532.
RefSeq NP_388762.1; -.
3D structure databases
HSSP P00432; 4BLC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P26901.
Protein family/group databases
PeroxiBase 4082; BsKat01_168.
Enzyme and pathway databases
BioCyc BSUB224308:BSU0881-MON; -.
Organism-specific databases
SubtiList BG10849; katA. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004096; Molecular function: catalase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26901.
ProtoNet P26901.
Genome annotation databases
GeneID 939240; -.
GenomeReviews AL009126_GR; BSU08820.
KEGG bsu:BSU08820; -.
NMPDR fig|224308.1.peg.881; -.
Phylogenomic databases
HOGENOM P26901; -.
Genome annotation databases
CMR P26901; BSU08820.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   483  482     Vegetative catalase. PRO_0000084975
ACT_SITE   54    54        By similarity. 
ACT_SITE   127   127        By similarity. 
METAL   337   337        Iron (heme axial ligand) (By similarity). 
CONFLICT   206   206        G -> P (in Ref. 1; AAA22402). 
CONFLICT   373   373        G -> D (in Ref. 1; AAA22402). 
Sequence information
Length: 483 AA [This is the length of the unprocessed precursor] Molecular weight: 54733 Da [This is the MW of the unprocessed precursor] CRC64: 456772956F870DE6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSNKLTTSW GAPVGDNQNS MTAGSRGPTL IQDVHLLEKL AHFNRERVPE RVVHAKGAGA 

        70         80         90        100        110        120 
HGYFEVTNDV TKYTKAAFLS EVGKRTPLFI RFSTVAGELG SADTVRDPRG FAVKFYTEEG 

       130        140        150        160        170        180 
NYDIVGNNTP VFFIRDAIKF PDFIHTQKRD PKTHLKNPTA VWDFWSLSPE SLHQVTILMS 

       190        200        210        220        230        240 
DRGIPATLRH MHGFGSHTFK WTNAEGEGVW IKYHFKTEQG VKNLDVNTAA KIAGENPDYH 

       250        260        270        280        290        300 
TEDLFNAIEN GDYPAWKLYV QIMPLEDANT YRFDPFDVTK VWSQKDYPLI EVGRMVLDRN 

       310        320        330        340        350        360 
PENYFAEVEQ ATFSPGTLVP GIDVSPDKML QGRLFAYHDA HRYRVGANHQ ALPINRARNK 

       370        380        390        400        410        420 
VNNYQRDGQM RFGDNGGGSV YYEPNSFGGP KESPEDKQAA YPVQGIADSV SYDHYDHYTQ 

       430        440        450        460        470        480 
AGDLYRLMSE DERTRLVENI VNAMKPVEKE EIKLRQIEHF YKADPEYGKR VAEGLGLPIK 


KDS 

P26901 in FASTA format

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View entry in raw text format (no links)
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