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UniProtKB/Swiss-Prot entry P42321


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

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Entry information
Entry name CATA_PROMI
Primary accession number P42321
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Catalase
Synonym EC 1.11.1.6
Gene name
Name: katA
From
Proteus mirabilis [TaxID: 584] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Proteus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, AND MASS SPECTROMETRY.
STRAIN=PR;
DOI=10.1007/BF01888363; PubMed=7786407 [NCBI, ExPASy, EBI, Israel, Japan]
Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G.;
"Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site.";
J. Protein Chem. 14:59-72(1995).
[2]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
STRAIN=PR;
DOI=10.1006/jmbi.1995.0350; PubMed=7791219 [NCBI, ExPASy, EBI, Israel, Japan]
Gouet P., Jouve H.-M., Dideberg O.;
"Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH.";
J. Mol. Biol. 249:933-954(1995).
[3]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND ABSORPTION SPECTROSCOPY.
DOI=10.1038/nsb1196-951; PubMed=8901874 [NCBI, ExPASy, EBI, Israel, Japan]
Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J.;
"Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy.";
Nat. Struct. Biol. 3:951-956(1996).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND EPR SPECTROSCOPY.
DOI=10.1002/prot.10283; PubMed=12486720 [NCBI, ExPASy, EBI, Israel, Japan]
Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.;
"High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.";
Proteins 50:261-271(2003).
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
PIR A58663; A58663.
3D structure databases
PDB
1E93; X-ray; 2.00 A; A=1-484.[ExPASy / RCSB / EBI]
1H6N; X-ray; 2.11 A; A=1-484.[ExPASy / RCSB / EBI]
1H7K; X-ray; 2.40 A; A=2-484.[ExPASy / RCSB / EBI]
1M85; X-ray; 2.00 A; A=1-484.[ExPASy / RCSB / EBI]
1MQF; X-ray; 2.50 A; A=1-484.[ExPASy / RCSB / EBI]
1NM0; X-ray; 2.30 A; A=1-484.[ExPASy / RCSB / EBI]
2CAG; X-ray; 2.70 A; A=1-484.[ExPASy / RCSB / EBI]
2CAH; X-ray; 2.70 A; A=1-484.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E93; -.
1H6N; -.
1H7K; -.
1M85; -.
1MQF; -.
1NM0; -.
2CAG; -.
2CAH; -.
ModBase P42321.
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).
ProtoNet P42321.
Other
LinkHub P42321; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; NADP; Oxidation; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   484  484     Catalase. PRO_0000084992
ACT_SITE   54    54         
ACT_SITE   127   127         
METAL   337   337        Iron (heme axial ligand). 
MOD_RES   53    53        Methionine sulfone. 
STRAND   17    19  3      
STRAND   21    24  4      
HELIX   34    43  10      
STRAND   56    66  11      
TURN   71    73  3      
HELIX   77    79  3      
STRAND   85    93  9      
STRAND   95    97  3      
STRAND   103   107  5      
STRAND   110   117  8      
STRAND   120   130  11      
HELIX   137   139  3      
HELIX   140   147  8      
TURN   151   153  3      
HELIX   158   166  9      
HELIX   169   171  3      
HELIX   172   179  8      
HELIX   181   183  3      
STRAND   184   186  3      
HELIX   188   190  3      
STRAND   199   202  4      
STRAND   208   217  10      
HELIX   226   235  10      
HELIX   239   249  11      
STRAND   255   264  10      
HELIX   265   269  5      
STRAND   271   273  3      
TURN   284   286  3      
STRAND   290   299  10      
HELIX   304   307  4      
TURN   308   310  3      
HELIX   328   345  18      
HELIX   349   351  3      
TURN   353   355  3      
STRAND   386   388  3      
HELIX   394   396  3      
STRAND   407   409  3      
HELIX   412   414  3      
HELIX   420   428  9      
HELIX   431   445  15      
HELIX   450   463  14      
HELIX   465   478  14      
Sequence information
Length: 484 AA [This is the length of the unprocessed precursor] Molecular weight: 55614 Da [This is the MW of the unprocessed precursor] CRC64: ADC25F3CB41F5C50 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA 

        70         80         90        100        110        120 
FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG AADAERDIRG FALKFYTEEG 

       130        140        150        160        170        180 
NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS 

       190        200        210        220        230        240 
DRGLPLSYRF VHGFGSHTYS FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS 

       250        260        270        280        290        300 
QRDLFEAIER GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN 

       310        320        330        340        350        360 
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH QIPVNAPKCP 

       370        380        390        400        410        420 
FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP LSIEGAADHW NHREDEDYFS 

       430        440        450        460        470        480 
QPRALYELLS DDEHQRMFAR IAGELSQASK ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG 


KDAK 

P42321 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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