[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Serotype A1; Roehrig S.C., Tran H.Q., Spehr V., Gunkel N., Selzer P.M., Ullrich H.J.; Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Plays a role in nitrite reduction (By similarity).
CATALYTIC ACTIVITY: NH₃ + 2 H₂O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H⁺.
COFACTOR: Binds 1 calcium ion per monomer (By similarity).
COFACTOR: Binds 5 heme groups covalently per monomer (By similarity).
PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
SUBCELLULAR LOCATION: Periplasm (By similarity).
SIMILARITY: Belongs to the cytochrome c-552 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

DQ680244; ABG89201.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q06PW6.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0042279;	Molecular function: nitrite reductase (cytochrome, ammonia-forming) activity (inferred from electronic annotation from HAMAP).
GO:0006807;	Biological process: nitrogen compound metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01182; -; 1.
PBIL [Tree]

InterPro

IPR003321; Cyt_c552.
IPR017570; Cytc_552_NO2Rdtase_formate-dep.
IPR011031; Multihaem_cyt.
Graphical view of domain structure.

Pfam

PF02335; Cytochrom_C552; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000243; Cyt_c552; 1.

PROSITE

PS51008; MULTIHEME_CYTC; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`CHAIN`	`25 500`	`476`	`Cytochrome c-552.`	`PRO_0000268969`
`METAL`	`102 102`		`Iron (heme 3 axial ligand) (By similarity).`
`METAL`	`134 134`		`Iron (heme 1 axial ligand) (By similarity).`
`METAL`	`172 172`		`Iron (heme 2 axial ligand) (By similarity).`
`METAL`	`221 221`		`Iron (heme 3 axial ligand) (By similarity).`
`METAL`	`223 223`		`Calcium (By similarity).`
`METAL`	`224 224`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`268 268`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`270 270`		`Calcium (By similarity).`
`METAL`	`282 282`		`Iron (heme 5 axial ligand) (By similarity).`
`METAL`	`293 293`		`Iron (heme 4 axial ligand) (By similarity).`
`METAL`	`308 308`		`Iron (heme 2 axial ligand) (By similarity).`
`METAL`	`325 325`		`Iron (heme 5 axial ligand) (By similarity).`
`METAL`	`400 400`		`Iron (heme 4 axial ligand) (By similarity).`
`BINDING`	`130 130`		`Heme 1 (covalent) (By similarity).`
`BINDING`	`133 133`		`Heme 1 (covalent) (By similarity).`
`BINDING`	`168 168`		`Heme 2 (covalent) (By similarity).`
`BINDING`	`171 171`		`Heme 2 (covalent) (By similarity).`
`BINDING`	`217 217`		`Heme 3 (covalent) (By similarity).`
`BINDING`	`220 220`		`Heme 3 (covalent) (By similarity).`
`BINDING`	`224 224`		`Substrate (By similarity).`
`BINDING`	`271 271`		`Substrate (By similarity).`
`BINDING`	`289 289`		`Heme 4 (covalent) (By similarity).`
`BINDING`	`292 292`		`Heme 4 (covalent) (By similarity).`
`BINDING`	`321 321`		`Heme 5 (covalent) (By similarity).`
`BINDING`	`324 324`		`Heme 5 (covalent) (By similarity).`

Sequence information

Length: 500 AA [This is the length of the unprocessed precursor]

Molecular weight: 56129 Da [This is the MW of the unprocessed precursor]

CRC64: 83F4D8702BC3D7DD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFLIKSLAV ATISILGCLQ TALAEEAKTE SLTDKAVKHE KLGVKIESAN HLFAEKYPLQ 

        70         80         90        100        110        120 
YDSWKSTAKS TDRGSALEAD PRYVILWAGY AFAKDYNKPR GHFYAVTDVR DILRTGAPKD 

       130        140        150        160        170        180 
ENDGPQPMAC WTCKGPDVPR LIEEKGERGY FDPKWAKYGA EIVNSIGCAD CHDTTSEEFK 

       190        200        210        220        230        240 
QGKPALRVAR PHVLRALNTV GWKFEDLDKH GKRPAVCANC HVEYYFKNKT DVTFPWDKGV 

       250        260        270        280        290        300 
DVDSIEKYYD EINFTDWTHA LSKAPMLKTQ HPDFEVWSQG THGKNGVTCI DCHMPKVKDK 

       310        320        330        340        350        360 
DGKVYTDHKI GNPFDQFEAT CKTCHEQSKE TLEKRVKEYK HEVKEAMIRL EDQLVKAHFE 

       370        380        390        400        410        420 
AKAAWEAGAT QEEMKEILMA IRHAQWRWDY SAAGHGNHFH APDVMLRTIA TGIDRAADAR 

       430        440        450        460        470        480 
AKLGVVLAKH GVTTPVAIPD ISTKEKAQLA IGLDIPKEQA AKDEFLKTVV PQWEKEARAK 

       490        500 
GLLPAEEADK PVAAPKAEAK

Q06PW6 in FASTA format

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View entry in raw text format (no links)
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	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