ID   NIR_PSECL               Reviewed;         363 AA.
AC   Q06006;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Copper-containing nitrite reductase;
DE            EC=1.7.2.1;
DE   AltName: Full=Cu-NIR;
DE   Flags: Precursor;
GN   Name=nirK;
OS   Pseudomonas chlororaphis (Pseudomonas aureofaciens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-41.
RC   STRAIN=ATCC 13985 / DSM 50082 / NRRL B-1576 / Stanier 38;
RX   MEDLINE=93356602; PubMed=8352648;
RA   Glockner A.B., Juengst A., Zumft W.G.;
RT   "Copper-containing nitrite reductase from Pseudomonas aureofaciens is
RT   functional in a mutationally cytochrome cd1-free background (NirS-) of
RT   Pseudomonas stutzeri.";
RL   Arch. Microbiol. 160:18-26(1993).
CC   -!- CATALYTIC ACTIVITY: Nitric oxide + H(2)O + ferricytochrome c =
CC       nitrite + ferrocytochrome c + 2 H(+).
CC   -!- COFACTOR: Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues
CC       from each of 2 monomers of the trimer. Nitrite is bound to the
CC       Cu(2+) ion site. Pseudoazurin is the physiological electron donor
CC       for the Cu-NIR in vitro.
CC   -!- COFACTOR: Binds 1 Cu(+) ion. The Cu(+) ion is bound within a
CC       single monomer.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC       dinitrogen from nitrate: step 2/4.
CC   -!- SUBUNIT: Homotrimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- DOMAIN: The type I copper site in NIR plays a crucial role for
CC       electron transfer from pseudoazurin to the type II copper site of
CC       NIR, which comprises the catalytic center of NIR for the reduction
CC       of nitrite.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 2 plastocyanin-like domains.
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DR   EMBL; Z21945; CAA79939.1; -; Genomic_DNA.
DR   PIR; S32112; S32112.
DR   HSSP; O68601; 1OE2.
DR   SMR; Q06006; 27-358.
DR   BRENDA; 1.7.2.1; 20327.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR001287; Cu_NO2-reductase_N.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR012746; Nitrite_red_Cu.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 2.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   PRINTS; PR00695; CUNO2RDTASE.
DR   ProDom; PD001235; Copper_blue_sub; 1.
DR   TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; FAD; Flavoprotein; Metal-binding;
KW   Nitrate assimilation; Oxidoreductase; Periplasm; Repeat; Signal.
FT   SIGNAL        1     24
FT   CHAIN        25    363       Copper-containing nitrite reductase.
FT                                /FTId=PRO_0000002988.
FT   DOMAIN       25    193       Plastocyanin-like 1.
FT   DOMAIN      194    363       Plastocyanin-like 2.
FT   METAL       113    113       Copper 1; type 1 (By similarity).
FT   METAL       118    118       Copper 2; type 2 (By similarity).
FT   METAL       153    153       Copper 2; type 2 (By similarity).
FT   METAL       154    154       Copper 1; type 1 (By similarity).
FT   METAL       163    163       Copper 1; type 1 (By similarity).
FT   METAL       168    168       Copper 1; type 1 (By similarity).
FT   METAL       324    324       Copper 2; type 2 (By similarity).
SQ   SEQUENCE   363 AA;  39248 MW;  50DDB60CC4DC3E00 CRC64;
     MSVFRSVLGA CVLLGSCASS LALAGGAEGL QRVKVDLVAP PLVHPHEQVV SGPPKVVQFR
     MSIEEKKMVI DDQGTTLQAM TFNGSMPGPT LVVHEGDYIE LTLVNPATNS MPHNVDFHAA
     TGALGGAGLT QVVPGQEVVL RFKADRSGTF VYHCAPQGMV PWHVVSGMNG ALMVLPRDGL
     RDPQGKLLHY DRVYTIGESD LYIPKDKDGH YKDYPDLASS YQDTRAVMRT LTPSHVVFNG
     RVGALTGANA LTSKVGESVL FIHSQANRDS RPHLIGGHGD WVWTTGKFAN PPQRNMETWF
     IPGGSAVAAL YTFKQPGTYV YLSHNLIEAM ELGALAQIKV EGQWDDDLMT QVKAPGPIVE
     PKQ
//