[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. STRAIN=TK64; PubMed=8157602 [NCBI, ExPASy, EBI, Israel, Japan] Bantleon R., Altenbuchner J., van Pee K.-H.; "Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene."; J. Bacteriol. 176:2339-2347(1994).
[2]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). STRAIN=TK64; 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

CATALYTIC ACTIVITY: 2 RH + 2 Cl^- + H₂O₂ = 2 RCl + 2 H₂O.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the bacterial non-heme bromo- and chloro-peroxidases family.

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

U02635; AAA18642.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55211; A55211.

3D structure databases

PDB

1A88; X-ray; 1.90 A; A/B/C=1-276.

[ExPASy / RCSB / EBI]

PDBsum

1A88; -.

ModBase

P49323.

Protein family/group databases

PeroxiBase

5557; SliHalNPrx.

Ontologies

GO:0016691;	Molecular function: chloride peroxidase activity (inferred from electronic annotation from EC).
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

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chloride; Direct protein sequencing; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 276`	`275`	`Non-heme chloroperoxidase.`	`PRO_0000207063`
`ACT_SITE`	`97 97`		`By similarity.`
`ACT_SITE`	`227 227`		`By similarity.`
`ACT_SITE`	`256 256`		`By similarity.`
`STRAND`	`3 5`	`3`
`STRAND`	`11 18`	`8`
`STRAND`	`24 28`	`5`
`HELIX`	`35 38`	`4`
`HELIX`	`39 47`	`9`
`STRAND`	`51 55`	`5`
`HELIX`	`72 86`	`15`
`STRAND`	`90 96`	`7`
`HELIX`	`99 109`	`11`
`STRAND`	`114 122`	`9`
`HELIX`	`140 152`	`13`
`HELIX`	`154 163`	`10`
`TURN`	`164 170`	`7`
`HELIX`	`178 190`	`13`
`HELIX`	`193 205`	`13`
`HELIX`	`209 214`	`6`
`STRAND`	`219 224`	`6`
`STRAND`	`228 230`	`3`
`TURN`	`233 235`	`3`
`HELIX`	`236 242`	`7`
`STRAND`	`246 251`	`6`
`HELIX`	`258 261`	`4`
`HELIX`	`263 275`	`13`

Sequence information

Length: 276 AA [This is the length of the unprocessed precursor]

Molecular weight: 29914 Da [This is the MW of the unprocessed precursor]

CRC64: CF8977B0C1FA53B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGTVTTSDGT NIFYKDWGPR DGLPVVFHHG WPLSADDWDN QMLFFLSHGY RVIAHDRRGH 

        70         80         90        100        110        120 
GRSDQPSTGH DMDTYAADVA ALTEALDLRG AVHIGHSTGG GEVARYVARA EPGRVAKAVL 

       130        140        150        160        170        180 
VSAVPPVMVK SDTNPDGLPL EVFDEFRAAL AANRAQFYID VPSGPFYGFN REGATVSQGL 

       190        200        210        220        230        240 
IDHWWLQGMM GAANAHYECI AAFSETDFTD DLKRIDVPVL VAHGTDDQVV PYADAAPKSA 

       250        260        270 
ELLANATLKS YEGLPHGMLS THPEVLNPDL LAFVKS

P49323 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools