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UniProtKB/Swiss-Prot entry O31158


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

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Entry information
Entry name PRXC_PSEFL
Primary accession number O31158
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 55)
Name and origin of the protein
Protein name Non-heme chloroperoxidase
Synonyms EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase F
CPO-F
Gene name
Name: cpo
Synonyms: cpoF
From
Pseudomonas fluorescens [TaxID: 294] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BL914;
PubMed=8760926 [NCBI, ExPASy, EBI, Israel, Japan]
Kirner S., Krauss S., Sury G., Lam S.T., Ligon J.M., van Pee K.-H.;
"The non-haem chloroperoxidase from Pseudomonas fluorescens and its relationship to pyrrolnitrin biosynthesis.";
Microbiology 142:2129-2135(1996).
[2]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
STRAIN=BL914;
DOI=10.1006/jmbi.1998.1802; PubMed=9642069 [NCBI, ExPASy, EBI, Israel, Japan]
Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H., Hecht H.-J.;
"Structural investigation of the cofactor-free chloroperoxidases.";
J. Mol. Biol. 279:889-900(1998).
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
AF031153; AAB86577.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1A8S; X-ray; 1.80 A; A=1-274.[ExPASy / RCSB / EBI]
PDBsum 1A8S; -.
ModBase O31158.
Protein family/group databases
PeroxiBase 5914; PfHalNPrx03_BL914.
Ontologies
GO
GO:0031404; Molecular function: chloride ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016691; Molecular function: chloride peroxidase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003089; AB_hydrolase.
IPR000073; AB_hydrolase_1.
IPR000639; Epox_hydrolase-like.
Graphical view of domain structure.
Pfam PF00561; Abhydrolase_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00111; ABHYDROLASE.
PR00412; EPOXHYDRLASE.
Other
LinkHub O31158; -.
ProtoNet O31158.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chloride; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   274  273     Non-heme chloroperoxidase. PRO_0000207060
ACT_SITE   95    95        By similarity. 
ACT_SITE   225   225        By similarity. 
ACT_SITE   254   254        By similarity. 
STRAND   3     5  3      
STRAND   11    18  8      
STRAND   20    26  7      
HELIX   33    36  4      
HELIX   37    45  9      
STRAND   49    53  5      
HELIX   70    83  14      
STRAND   88    94  7      
HELIX   97   108  12      
STRAND   113   120  8      
HELIX   138   161  24      
STRAND   164   166  3      
HELIX   176   188  13      
HELIX   191   203  13      
HELIX   207   211  5      
STRAND   217   222  6      
STRAND   226   228  3      
TURN   231   233  3      
HELIX   234   240  7      
STRAND   245   249  5      
HELIX   256   259  4      
HELIX   261   273  13      
Sequence information
Length: 274 AA [This is the length of the unprocessed precursor] Molecular weight: 29651 Da [This is the MW of the unprocessed precursor] CRC64: 00E2CF31A99E460F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTTFTTRDGT QIYYKDWGSG QPIVFSHGWP LNADSWESQM IFLAAQGYRV IAHDRRGHGR 

        70         80         90        100        110        120 
SSQPWSGNDM DTYADDLAQL IEHLDLRDAV LFGFSTGGGE VARYIGRHGT ARVAKAGLIS 

       130        140        150        160        170        180 
AVPPLMLKTE ANPGGLPMEV FDGIRQASLA DRSQLYKDLA SGPFFGFNQP GAKSSAGMVD 

       190        200        210        220        230        240 
WFWLQGMAAG HKNAYDCIKA FSETDFTEDL KKIDVPTLVV HGDADQVVPI EASGIASAAL 

       250        260        270 
VKGSTLKIYS GAPHGLTDTH KDQLNADLLA FIKG 

O31158 in FASTA format

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