ID   B2UHR8_RALPJ            Unreviewed;       499 AA.
AC   B2UHR8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290, ECO:0000256|RuleBase:RU365025};
DE            EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882, ECO:0000256|RuleBase:RU365025};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rpic_4015 {ECO:0000313|EMBL:ACD29119.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29119.1};
RN   [1] {ECO:0000313|EMBL:ACD29119.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=12J {ECO:0000313|EMBL:ACD29119.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM}
RP   X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) OF 32-499 IN COMPLEX WITH COPPER AND
RP   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 transfer.";
RL   Nature 496:123-126(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-
CC         [cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-
CC         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|ARBA:ARBA00029301,
CC         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|ARBA:ARBA00011233,
CC       ECO:0000256|RuleBase:RU365025}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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   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   AlphaFoldDB; B2UHR8; -.
DR   SMR; B2UHR8; -.
DR   STRING; 402626.Rpic_4015; -.
DR   KEGG; rpi:Rpic_4015; -.
DR   PATRIC; fig|402626.5.peg.259; -.
DR   eggNOG; COG2010; Bacteria.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_031740_1_1_4; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   CDD; cd11020; CuRO_1_CuNIR; 1.
DR   CDD; cd04208; CuRO_2_CuNIR; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
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   NCBIfam; TIGR02376; Cu_nitrite_red; 1.
DR   PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR   PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00695; CUNO2RDTASE.
DR   SUPFAM; SSF49503; Cupredoxins; 2.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM};
KW   Copper {ECO:0000256|PIRSR:PIRSR601287-1, ECO:0000256|RuleBase:RU365025};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601287-1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU365025,
KW   ECO:0000313|EMBL:ACD29119.1}; Signal {ECO:0000256|RuleBase:RU365025}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|RuleBase:RU365025"
FT   CHAIN           32..499
FT                   /note="Copper-containing nitrite reductase"
FT                   /evidence="ECO:0000256|RuleBase:RU365025"
FT                   /id="PRO_5015213072"
FT   DOMAIN          382..471
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         125
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         125
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         128
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         130
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         165
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         165
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         166
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         166
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         174
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         174
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         179
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         179
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         320
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         320
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         395
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         398
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         399
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         416
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         447
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
FT   BINDING         449
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:2YQB, ECO:0007829|PDB:3ZBM"
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
//