[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NTCC 6750; DOI=10.1016/0014-5793(95)00461-H; PubMed=7781769 [NCBI, ExPASy, EBI, Israel, Japan] Ridout C.J., James R., Greenwood C.; "Nucleotide sequence encoding the di-haem cytochrome c551 peroxidase from Pseudomonas aeruginosa."; FEBS Lett. 365:152-154(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan] Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."; Nature 406:959-964(2000).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-346. DOI=10.1016/0014-5793(95)01326-1; PubMed=8543038 [NCBI, ExPASy, EBI, Israel, Japan] Samyn B., van Craenenbroeck K., de Smet L., Vandenberghe I., Pettigrew G., van Beeumen J.; "A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase."; FEBS Lett. 377:145-149(1995).
[4]	PROTEIN SEQUENCE OF 24-346. DOI=10.1016/0014-5793(89)80714-8; PubMed=2546794 [NCBI, ExPASy, EBI, Israel, Japan] Roennberg M., Kalkkinen N., Ellfolk N.; "The primary structure of Pseudomonas cytochrome c peroxidase."; FEBS Lett. 250:175-178(1989).
[5]	PARTIAL PROTEIN SEQUENCE. PubMed=3030432 [NCBI, ExPASy, EBI, Israel, Japan] Roennberg M.; "Amino acid sequences of the two heme c-binding sites of Pseudomonas cytochrome-c peroxidase."; Biochim. Biophys. Acta 912:82-86(1987).
[6]	CHARACTERIZATION. DOI=10.1016/0167-4838(91)90113-E; PubMed=1657179 [NCBI, ExPASy, EBI, Israel, Japan] Ellfolk N., Roennberg M., Oesterlund K.; "Structural and functional features of Pseudomonas cytochrome c peroxidase."; Biochim. Biophys. Acta 1080:68-77(1991).
[7]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1016/S0969-2126(01)00258-1; PubMed=8591033 [NCBI, ExPASy, EBI, Israel, Japan] Fueloep V., Ridout C.J., Greenwood C., Hajdu J.; "Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa."; Structure 3:1225-1233(1995).

Comments

FUNCTION: Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
CATALYTIC ACTIVITY: 2 ferrocytochrome c + H₂O₂ = 2 ferricytochrome c + 2 H₂O.
COFACTOR: Binds 2 heme groups. Heme 1 is low-potential (-330 mV) with 2 His axial ligands and functions in the peroxidase reaction, while heme 2 is high potential (+320 mV) with His and Met axial ligands and functions to feed electrons from electron-shuttle proteins such as cytochrome c and azurin.
SUBCELLULAR LOCATION: Periplasm.
DOMAIN: Organized into two domains, each containing a covalent c-heme in a structure reminiscent of class 1 cytochromes c. The domains are related by a quasi-twofold axis. The domain interface contains a calcium-binding site with an unusual set of ligands.
PTM: Binds 2 heme groups per subunit.

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

U23766; AAC43378.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG07975.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I53515; I53515.

RefSeq

NP_253277.1; -.

3D structure databases

PDB

1EB7; X-ray; 2.40 A; A=24-346.	[ExPASy / RCSB / EBI]
2VHD; X-ray; 2.30 A; A/B=24-346.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EB7; -.
2VHD; -.

ModBase

P14532.

Protein family/group databases

PeroxiBase

3543; PaerDiHCcP.

Enzyme and pathway databases

BioCyc

PAER208964:PA4587-MON; -.

Organism-specific databases

PseudoCAP

PA4587; -.

Ontologies

GO:0004130;	Molecular function: cytochrome-c peroxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR009056; Cyt_c_monohaem.
IPR004852; CytCP_MauG.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.760.10; Cytochrome_c_R; 1.

Pfam

PF03150; CCP_MauG; 1.
Pfam graphical view of domain structure.

PROSITE

PS51007; CYTC; 2.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P14532.

Genome annotation databases

GeneID

881021; -.

GenomeReviews

AE004091_GR; PA4587.

KEGG

pae:PA4587; -.

Phylogenomic databases

HOGENOM

P14532; -.

Genome annotation databases

CMR

P14532; PA4587.

Other

ProtoNet

P14532.

UniRef

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

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Peroxidase; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 346`	`323`	`Cytochrome c551 peroxidase.`	`PRO_0000006598`
`METAL`	`78 78`		`Iron (heme 1 axial ligand).`
`METAL`	`224 224`		`Iron (heme 2 axial ligand).`
`METAL`	`284 284`		`Iron (heme 1 axial ligand).`
`METAL`	`298 298`		`Iron (heme 2 axial ligand).`
`BINDING`	`74 74`		`Heme 1 (covalent).`
`BINDING`	`77 77`		`Heme 1 (covalent).`
`BINDING`	`220 220`		`Heme 2 (covalent).`
`BINDING`	`223 223`		`Heme 2 (covalent).`
`VARIANT`	`81 81`	`1`	`G -> D.`
`VARIANT`	`83 83`	`1`	`G -> D.`
`VARIANT`	`152 152`	`1`	`I -> V.`
`VARIANT`	`164 164`	`1`	`P -> A.`
`VARIANT`	`198 198`	`1`	`K -> I.`
`VARIANT`	`334 334`	`1`	`L -> W.`
`CONFLICT`	`86 86`		`D -> G (in Ref. 3).`
`CONFLICT`	`93 93`		`Missing (in Ref. 3).`
`CONFLICT`	`96 96`		`W -> G (in Ref. 3).`
`CONFLICT`	`102 120`		`Missing (in Ref. 3).`
`CONFLICT`	`137 137`		`E -> Q (in Ref. 3).`
`CONFLICT`	`175 175`		`M -> V (in Ref. 2).`
`CONFLICT`	`228 228`		`Missing (in Ref. 3).`
`CONFLICT`	`286 287`		`GQ -> QG (in Ref. 3).`
`CONFLICT`	`290 290`		`E -> Q (in Ref. 3).`
`HELIX`	`25 33`	`9`
`HELIX`	`51 62`	`12`
`HELIX`	`64 66`	`3`
`HELIX`	`74 77`	`4`
`TURN`	`80 84`	`5`
`HELIX`	`109 111`	`3`
`STRAND`	`116 120`	`5`
`HELIX`	`123 125`	`3`
`HELIX`	`131 139`	`9`
`HELIX`	`142 150`	`9`
`HELIX`	`153 162`	`10`
`STRAND`	`167 171`	`5`
`HELIX`	`172 185`	`14`
`HELIX`	`192 197`	`6`
`HELIX`	`206 217`	`12`
`HELIX`	`220 222`	`3`
`TURN`	`227 229`	`3`
`STRAND`	`234 241`	`8`
`TURN`	`253 255`	`3`
`STRAND`	`256 260`	`5`
`STRAND`	`266 269`	`4`
`HELIX`	`276 278`	`3`
`TURN`	`283 286`	`4`
`HELIX`	`291 298`	`8`
`STRAND`	`301 305`	`5`
`HELIX`	`309 320`	`12`

Sequence information

Length: 346 AA [This is the length of the unprocessed precursor]

Molecular weight: 37403 Da [This is the MW of the unprocessed precursor]

CRC64: 8B402E5BA149EA44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQSSQLLPLG SLLLSFATPL AQADALHDQA SALFKPIPEQ VTELRGQPIS EQQRELGKKL 

        70         80         90        100        110        120 
FFDPRLSRSH VLSCNTCHNV GTGGADNVPT SVGHGWQKGP RNSPTVFNAV FNAAQFWDGR 

       130        140        150        160        170        180 
AKDLGEQAKG PIQNSVEMHS TPQLVEQTLG SIPEYVDAFR KAFPKAGKPV SFDNMALAIE 

       190        200        210        220        230        240 
AYEATLVTPD SPFDLYLKGD DKALDAQQKK GLKAFMDSGC SACHNGINLG GQAYFPFGLV 

       250        260        270        280        290        300 
KKPDASVLPS GDKGRFAVTK TQSDEYVFRA APLRNVALTA PYFHSGQVWE LKDAVAIMGN 

       310        320        330        340 
AQLGKQLAPD DVENIVAFLH SLSGKQPRVE YPLLPASTET TPRPAE

P14532 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