[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Tu24; Pelletier I., Altenbuchner J., van Pee K.-H.; Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[2]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). STRAIN=Tu24; 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: RH + Cl^- + H₂O₂ = 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

AF031242; AAB86626.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1A7U; X-ray; 1.75 A; A/B=2-278.	[ExPASy / RCSB / EBI]
1A8U; X-ray; 1.60 A; A/B=2-278.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1A7U; -.
1A8U; -.

ModBase

O31168.

Protein family/group databases

PeroxiBase

5908; STaHalNPrx02.

Ontologies

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

O31168; -.

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

Keywords

3D-structure; Chloride; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 278`	`278`	`Non-heme chloroperoxidase.`	`PRO_0000207062`
`ACT_SITE`	`99 99`		`By similarity.`
`ACT_SITE`	`229 229`		`By similarity.`
`ACT_SITE`	`258 258`		`By similarity.`
`STRAND`	`3 9`	`7`
`STRAND`	`12 30`	`19`
`HELIX`	`37 40`	`4`
`HELIX`	`41 49`	`9`
`STRAND`	`53 57`	`5`
`HELIX`	`74 88`	`15`
`STRAND`	`92 98`	`7`
`HELIX`	`101 112`	`12`
`STRAND`	`117 124`	`8`
`STRAND`	`139 141`	`3`
`HELIX`	`143 155`	`13`
`HELIX`	`157 168`	`12`
`HELIX`	`171 174`	`4`
`TURN`	`176 178`	`3`
`HELIX`	`181 193`	`13`
`HELIX`	`196 205`	`10`
`TURN`	`211 213`	`3`
`HELIX`	`214 216`	`3`
`STRAND`	`221 226`	`6`
`STRAND`	`230 232`	`3`
`HELIX`	`234 236`	`3`
`HELIX`	`238 244`	`7`
`STRAND`	`248 253`	`6`
`HELIX`	`260 263`	`4`
`HELIX`	`265 277`	`13`

Sequence information

Length: 278 AA [This is the length of the unprocessed precursor]

Molecular weight: 30355 Da [This is the MW of the unprocessed precursor]

CRC64: 8C97A87251FBEDE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPFITVGQEN STSIDLYYED HGAGQPVVLI HGFPLSGHSW ERQSAALLDA GYRVITYDRR 

        70         80         90        100        110        120 
GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM GTGEVARYVS SYGTARIAKV 

       130        140        150        160        170        180 
AFLASLEPFL LKTDDNPDGA APKEFFDGIV AAVKADRYAF YTGFFNDFYN LDENLGTRIS 

       190        200        210        220        230        240 
EEAVRNSWNT AASGGFFAAA AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV 

       250        260        270 
FHKALPSAEY VEVEGAPHGL LWTHAEEVNT ALLAFLAK

O31168 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