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Protein

Non-heme chloroperoxidase

Gene

cpo

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei97By similarity1
Active sitei227By similarity1
Active sitei256By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Chloride

Protein family/group databases

ESTHERistrli-cpoL. Haloperoxidase.
MEROPSiS33.992.
PeroxiBasei5557. SliHalNPrx.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-heme chloroperoxidase (EC:1.11.1.10)
Alternative name(s):
Chloride peroxidase
Chloroperoxidase L
Short name:
CPO-L
Gene namesi
Name:cpo
Synonyms:cpoL
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002070632 – 276Non-heme chloroperoxidaseAdd BLAST275

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi11 – 18Combined sources8
Beta strandi24 – 28Combined sources5
Helixi35 – 38Combined sources4
Helixi39 – 47Combined sources9
Beta strandi51 – 55Combined sources5
Helixi72 – 86Combined sources15
Beta strandi90 – 96Combined sources7
Helixi99 – 109Combined sources11
Beta strandi114 – 122Combined sources9
Helixi140 – 152Combined sources13
Helixi154 – 163Combined sources10
Turni164 – 170Combined sources7
Helixi178 – 190Combined sources13
Helixi193 – 205Combined sources13
Helixi209 – 214Combined sources6
Beta strandi219 – 224Combined sources6
Beta strandi228 – 230Combined sources3
Turni233 – 235Combined sources3
Helixi236 – 242Combined sources7
Beta strandi246 – 251Combined sources6
Helixi258 – 261Combined sources4
Helixi263 – 275Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A88X-ray1.90A/B/C2-276[»]
ProteinModelPortaliP49323.
SMRiP49323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 254AB hydrolase-1Sequence analysisAdd BLAST231

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]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTVTTSDGT NIFYKDWGPR DGLPVVFHHG WPLSADDWDN QMLFFLSHGY
60 70 80 90 100
RVIAHDRRGH GRSDQPSTGH DMDTYAADVA ALTEALDLRG AVHIGHSTGG
110 120 130 140 150
GEVARYVARA EPGRVAKAVL VSAVPPVMVK SDTNPDGLPL EVFDEFRAAL
160 170 180 190 200
AANRAQFYID VPSGPFYGFN REGATVSQGL IDHWWLQGMM GAANAHYECI
210 220 230 240 250
AAFSETDFTD DLKRIDVPVL VAHGTDDQVV PYADAAPKSA ELLANATLKS
260 270
YEGLPHGMLS THPEVLNPDL LAFVKS
Length:276
Mass (Da):29,914
Last modified:January 23, 2007 - v2
Checksum:iCF8977B0C1FA53B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02635 Unassigned DNA. Translation: AAA18642.1.
PIRiA55211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02635 Unassigned DNA. Translation: AAA18642.1.
PIRiA55211.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A88X-ray1.90A/B/C2-276[»]
ProteinModelPortaliP49323.
SMRiP49323.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERistrli-cpoL. Haloperoxidase.
MEROPSiS33.992.
PeroxiBasei5557. SliHalNPrx.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP49323.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRXC_STRLI
AccessioniPrimary (citable) accession number: P49323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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 one 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.