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Protein

Non-heme chloroperoxidase

Gene

cpo

Organism
Streptomyces aureofaciens
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RH + Cl- + H2O2 = RCl + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991By similarity
Active sitei229 – 2291By similarity
Active sitei258 – 2581By similarity

GO - Molecular functioni

  1. chloride peroxidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Chloride

Protein family/group databases

MEROPSiS33.991.
PeroxiBasei5908. STaHalNPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-heme chloroperoxidase (EC:1.11.1.10)
Alternative name(s):
Chloride peroxidase
Chloroperoxidase T
Short name:
CPO-T
Gene namesi
Name:cpo
Synonyms:cpoT
OrganismiStreptomyces aureofaciens
Taxonomic identifieri1894 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Non-heme chloroperoxidasePRO_0000207062Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi12 – 2211Combined sources
Beta strandi24 – 307Combined sources
Helixi37 – 404Combined sources
Helixi41 – 499Combined sources
Beta strandi53 – 575Combined sources
Helixi74 – 8815Combined sources
Beta strandi92 – 987Combined sources
Helixi100 – 11213Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 15513Combined sources
Helixi157 – 16812Combined sources
Helixi171 – 1744Combined sources
Turni176 – 1783Combined sources
Helixi181 – 19313Combined sources
Helixi196 – 20510Combined sources
Turni211 – 2133Combined sources
Helixi214 – 2163Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi230 – 2323Combined sources
Helixi234 – 2363Combined sources
Helixi238 – 2447Combined sources
Beta strandi248 – 2536Combined sources
Helixi260 – 2634Combined sources
Helixi265 – 27713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7UX-ray1.75A/B2-278[»]
1A8UX-ray1.60A/B2-278[»]
ProteinModelPortaliO31168.
SMRiO31168. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31168.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

O31168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFITVGQEN STSIDLYYED HGAGQPVVLI HGFPLSGHSW ERQSAALLDA
60 70 80 90 100
GYRVITYDRR GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM
110 120 130 140 150
GTGEVARYVS SYGTARIAKV AFLASLEPFL LKTDDNPDGA APKEFFDGIV
160 170 180 190 200
AAVKADRYAF YTGFFNDFYN LDENLGTRIS EEAVRNSWNT AASGGFFAAA
210 220 230 240 250
AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV FHKALPSAEY
260 270
VEVEGAPHGL LWTHAEEVNT ALLAFLAK
Length:278
Mass (Da):30,355
Last modified:January 1, 1998 - v1
Checksum:i8C97A87251FBEDE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031242 Genomic DNA. Translation: AAB86626.1.
RefSeqiWP_033354363.1. NZ_JNWR01000048.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031242 Genomic DNA. Translation: AAB86626.1.
RefSeqiWP_033354363.1. NZ_JNWR01000048.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7UX-ray1.75A/B2-278[»]
1A8UX-ray1.60A/B2-278[»]
ProteinModelPortaliO31168.
SMRiO31168. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS33.991.
PeroxiBasei5908. STaHalNPrx02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO31168.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Pelletier I., Altenbuchner J., van Pee K.-H.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Tu24.
  2. "Structural investigation of the cofactor-free chloroperoxidases."
    Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H., Hecht H.-J.
    J. Mol. Biol. 279:889-900(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
    Strain: Tu24.

Entry informationi

Entry nameiPRXC_STRAU
AccessioniPrimary (citable) accession number: O31168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 1, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.