(data stored in ACNUC7421 zone)

SWISSPROT: B2UHR8_RALPJ

ID   B2UHR8_RALPJ            Unreviewed;       499 AA.
AC   B2UHR8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Copper-containing nitrite reductase {ECO:0000256|RuleBase:RU365025};
DE            EC=1.7.2.1 {ECO:0000256|RuleBase:RU365025};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rpic_4015 {ECO:0000313|EMBL:ACD29119.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29119.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:3ZIY}
RP   X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) OF 32-499 IN COMPLEX WITH
RP   COPPER AND HEME.
RX   PubMed=23535590; DOI=10.1038/NATURE11996;
RA   Antonyuk S.V., Han C., Eady R.R., Hasnain S.S.;
RT   "Structures of protein-protein complexes involved in electron
RT   transfer.";
RL   Nature 496:123-126(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[Fe(III)cytochrome c] + H2O + nitric oxide =
CC         [Fe(II)cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU365025};
CC   -!- COFACTOR:
CC       Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC         Evidence={ECO:0000256|RuleBase:RU365025};
CC       Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|RuleBase:RU365025};
CC       Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU365025}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|RuleBase:RU365025}.
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DR   EMBL; CP001069; ACD29119.1; -; Genomic_DNA.
DR   RefSeq; WP_012430128.1; NC_010678.1.
DR   PDB; 2YQB; X-ray; 1.41 A; A=32-499.
DR   PDB; 3ZBM; X-ray; 1.87 A; A=32-499.
DR   PDB; 3ZIY; X-ray; 1.01 A; A=32-499.
DR   PDB; 4AX3; X-ray; 1.60 A; A/B/C/D=32-499.
DR   PDBsum; 2YQB; -.
DR   PDBsum; 3ZBM; -.
DR   PDBsum; 3ZIY; -.
DR   PDBsum; 4AX3; -.
DR   SMR; B2UHR8; -.
DR   STRING; 402626.Rpic_4015; -.
DR   EnsemblBacteria; ACD29119; ACD29119; Rpic_4015.
DR   GeneID; 6285310; -.
DR   KEGG; rpi:Rpic_4015; -.
DR   PATRIC; fig|402626.5.peg.259; -.
DR   eggNOG; ENOG4105CEI; Bacteria.
DR   eggNOG; COG2010; LUCA.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000217143; -.
DR   KO; K00368; -.
DR   OMA; CVGCKLH; -.
DR   OrthoDB; 971126at2; -.
DR   BioCyc; RPIC402626:GH94-4015-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 1.
DR   Gene3D; 2.60.40.420; -; 2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR001287; NO2-reductase_Cu.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00695; CUNO2RDTASE.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   SUPFAM; SSF49503; SSF49503; 2.
DR   TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
DR   PRODOM; B2UHR8.
DR   SWISS-2DPAGE; B2UHR8.
KW   3D-structure {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM,
KW   ECO:0000213|PDB:3ZIY, ECO:0000213|PDB:4AX3};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Copper {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM,
KW   ECO:0000213|PDB:3ZIY, ECO:0000256|RuleBase:RU365025};
KW   Heme {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM,
KW   ECO:0000213|PDB:3ZIY, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM,
KW   ECO:0000213|PDB:3ZIY, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:3ZBM,
KW   ECO:0000256|PROSITE-ProRule:PRU00433, ECO:0000256|RuleBase:RU365025};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU365025,
KW   ECO:0000313|EMBL:ACD29119.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Signal {ECO:0000256|RuleBase:RU365025}.
FT   SIGNAL        1     31       {ECO:0000256|RuleBase:RU365025}.
FT   CHAIN        32    499       Copper-containing nitrite reductase.
FT                                {ECO:0000256|RuleBase:RU365025}.
FT                                /FTId=PRO_5015213072.
FT   DOMAIN      382    471       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   METAL       125    125       Copper 1; via pros nitrogen.
FT                                {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:
FT                                3ZBM, ECO:0000213|PDB:3ZIY}.
FT   METAL       130    130       Copper 2; via tele nitrogen.
FT                                {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:
FT                                3ZBM, ECO:0000213|PDB:3ZIY}.
FT   METAL       165    165       Copper 2; via tele nitrogen.
FT                                {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:
FT                                3ZBM, ECO:0000213|PDB:3ZIY}.
FT   METAL       166    166       Copper 1. {ECO:0000213|PDB:2YQB,
FT                                ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:
FT                                3ZIY}.
FT   METAL       174    174       Copper 1; via pros nitrogen.
FT                                {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:
FT                                3ZBM, ECO:0000213|PDB:3ZIY}.
FT   METAL       179    179       Copper 1. {ECO:0000213|PDB:2YQB,
FT                                ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:
FT                                3ZIY}.
FT   METAL       320    320       Copper 2; via tele nitrogen.
FT                                {ECO:0000213|PDB:2YQB, ECO:0000213|PDB:
FT                                3ZBM, ECO:0000213|PDB:3ZIY}.
FT   METAL       399    399       Iron (heme axial ligand); via tele
FT                                nitrogen. {ECO:0000213|PDB:2YQB,
FT                                ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:
FT                                4AX3}.
FT   METAL       449    449       Iron (heme axial ligand).
FT                                {ECO:0000213|PDB:4AX3}.
FT   BINDING     395    395       Heme (covalent). {ECO:0000213|PDB:2YQB,
FT                                ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:
FT                                3ZIY}.
FT   BINDING     398    398       Heme (covalent). {ECO:0000213|PDB:2YQB,
FT                                ECO:0000213|PDB:3ZBM, ECO:0000213|PDB:
FT                                3ZIY}.
SQ   SEQUENCE   499 AA;  53086 MW;  78D55A8E6C864B2C CRC64;
     MSRLHTVRSL MRAGLISVVL GALLAGTAAR AASAKLPGDF GPPRGEPIHA VLTSPPLVPP
     PVHRNYPAKV IVELEVVEKE MQISEGVSYT FWTFGGTVPG SFIRVRQGDT VEFHLKNHPS
     SKMPHNIDLH GVTGPGGGAA SSFTAPGHES QFTFKALNEG IYVYHCATAP VGMHIANGMY
     GLILVEPPEG LPKVDHEYYV MQGDFYTAGK YREKGLQPFD MEKAIDERPS YVLFNGAEGA
     LTGDKALHAK VGETVRIFVG NGGPNLVSSF HVIGAIFDQV RYEGGTNVQK NVQTTLIPAG
     GAAVVKFTAR VPGSYVLVDH SIFRAFNKGA LAILKIDGPE SKLVYSGKEL DSVYLGDRAA
     PNMSAVTKAT EASVSGTLTV QDQVQAGRAL FAGTCSVCHQ GNGAGLPGVF PPLAKSDFLA
     ADPKRAMNIV LHGLNGKIKV NGQEYDSVMP PMTQLNDDEV ANILTYVLNS WDNPGGRVSA
     EDVKKVRAQP APAKAVAEH
//

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