NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00871635; PubMed=7747927 [NCBI, ExPASy, EBI, Israel, Japan]
de Boer A.P.N., Reijnders W.N.M., Kuenen J.G., Stouthamer A.H., van Spanning R.J.M.;
"Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans.";
Antonie Van Leeuwenhoek 66:111-127(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.;
"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Inactivation of this cytochrome oxidase results in the loss of nitrite and nitric oxide reductase activities, but not of nitrous oxide reductase activity.
CATALYTIC ACTIVITY: Nitric oxide + H₂O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H⁺.
CATALYTIC ACTIVITY: NH₃ + H₂O + acceptor = hydroxylamine + reduced acceptor.
COFACTOR: Binds 2 heme groups per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).
SIMILARITY: Contains 1 cytochrome c domain.

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

U05002; AAA93118.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000489; ABL70574.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_916270.1; -.

3D structure databases

HSSP

P72181; 1H9X. [HSSP ENTRY / PDB]

SMR

Q51700; 38-596.

ModBase

Q51700.

Family and domain databases

InterPro

IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR003143; Cyt_d1_haem.
Graphical view of domain structure.

Gene3D

G3DSA:2.140.10.20; Cyt_d1_haem; 1.
G3DSA:1.10.760.10; Cytochrome_c_R; 1.

Pfam

PF00034; Cytochrom_C; 1.
PF02239; Cytochrom_D1; 1.
Pfam graphical view of domain structure.

PROSITE

PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q51700.

Genome annotation databases

GeneID

4580125; -.

GenomeReviews

CP000489_GR; Pden_2487.

KEGG

pde:Pden_2487; -.

CMR

Q51700; Pden_2487.

Other

ProtoNet

Q51700.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`	`By similarity.`
`CHAIN`	`30 596`	`567`	`Nitrite reductase.`	`PRO_0000006574`
`DOMAIN`	`77 162`	`86`	`Cytochrome c.`
`REGION`	`30 76`	`47`	`N-terminal tail.`
`REGION`	`163 596`	`434`	`D1-heme domain.`
`METAL`	`46 46`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`98 98`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`229 229`		`Iron (heme D1 proximal ligand) (By similarity).`
`BINDING`	`94 94`		`Heme (covalent) (By similarity).`
`BINDING`	`97 97`		`Heme (covalent) (By similarity).`

Sequence information

Length: 596 AA [This is the length of the unprocessed precursor]

Molecular weight: 65440 Da [This is the MW of the unprocessed precursor]

CRC64: 90C981B688A74BD3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRQRTPFARP GLLASAALAL VLGPLAVAAQ EQAAPPKDPA AALEDHKTKT DNRYEPSLDN 

        70         80         90        100        110        120 
LAQQDVAALG APEGIPALSD AQYNEANKIY FERCAGCHGV LRKGATGKAL TPDLTRDLGF 

       130        140        150        160        170        180 
DYLQSFITYG SPAGMPNWGT SGELTAEQVD LMANYLLLDP AAPPEFGMKE MRESWQVHVA 

       190        200        210        220        230        240 
PEDRPTQQEN DWDLENLFSV TLRDAGQIAL IDGTTYEIKS VLDTGYAVHI SRMSASGRYL 

       250        260        270        280        290        300 
FVIGRDGKVN MIDLWMKEPA TVAEIKIGSE ARSIETSKME GWEDKYAIAG AYWPPQYVIM 

       310        320        330        340        350        360 
DGETLEPMKI QSTRGMIYDE QEYHPEPRVA AILASHYRPE FIVNVKETGK ILLVDYTDLK 

       370        380        390        400        410        420 
NLKTTEIEAE RFLHDGGLDG SHRYFITAAN ARNKLVVIDT KEGKLVAIED TGGQTPHPGR 

       430        440        450        460        470        480 
GANFVHPTFG PVWATSHMGD DSVALIGTDP EGHPDNAWKI LDSFPALGGG SLFIKTHPNS 

       490        500        510        520        530        540 
QYLYVDATLN PEAEISGSVA VFDTKAMTGD GSDPEFKTLP IAEWAGIAEG QPRVVQGEFN 

       550        560        570        580        590 
KDGTEVWFSV WNGKDQESAL VVVDDKTLEL KHVIKDERLV TPTGKFNVYN TMTDTY

Q51700 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