ID A0A0J8RUQ5_COCIT Unreviewed; 456 AA.
AC A0A0J8RUQ5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN ORFNames=CIHG_05568 {ECO:0000313|EMBL:KMU87799.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU87799.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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 -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000256|ARBA:ARBA00001960,
CC ECO:0000256|PIRSR:PIRSR601287-1};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR601287-1};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; DS017000; KMU87799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RUQ5; -.
DR STRING; 396776.A0A0J8RUQ5; -.
DR VEuPathDB; FungiDB:CIHG_05568; -.
DR eggNOG; ENOG502S0TZ; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion 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 InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; Cupredoxins; 2.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601287-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..276
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 329..431
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213
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 218
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 253
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 254
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 262
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 267
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 416
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"
SQ SEQUENCE 456 AA; 49549 MW; 681C136D5AF99902 CRC64;
MNTCTRCLRT PLKAPWKAIQ STSLPREAFS SRGFVSTVSR STKIQSRRIS TDSSKSSGNK
YGNRTKLAFA LAVSGFTTAV ILLYGGHRDA VRMDWQPKRK PAVDPTPAPS SGKPVPPDPY
TVLGHEPIDV SKFPVEDAIL TTAPNVPPPI TRDHPALLRV PLTTTTKLSQ LTSVYKYDQW
TFNDSVPGPF IRARAGDVIE LTITNKDPSG NPHNIDCHAF IGPGGGAPLT TVGFNESKTA
RFQLLHPGLY VYHCSAAPVP VHIANGMYGM IYVQPAEGDL PPVDKEYFVL QSEFYHEPPE
VEDDGRPSSI VEFSYPNALR EEPNVVVFNG SESALTRDKP LTANTNETVR IFFGNAGPNL
TSSFHVIGSN FKKVYREGDV ISPPGQFIQT VSVPPGSATI VDMEMSVPGT YALVDHAIFR
MDKGAVGYLN VSGEQRPDIY GSTQPPAPCV GCKLHP
//
