ID A0A0Q9QG06_9GAMM Unreviewed; 471 AA.
AC A0A0Q9QG06;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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};
GN ORFNames=ASG87_09865 {ECO:0000313|EMBL:KRF01809.1};
OS Frateuria sp. Soil773.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRF01809.1, ECO:0000313|Proteomes:UP000051919};
RN [1] {ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|Proteomes:UP000051919};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF01809.1, ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|EMBL:KRF01809.1,
RC ECO:0000313|Proteomes:UP000051919};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|RuleBase:RU365025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRF01809.1}.
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DR EMBL; LMSL01000002; KRF01809.1; -; Genomic_DNA.
DR STRING; 1736407.ASG87_09865; -.
DR OrthoDB; 5290932at2; -.
DR Proteomes; UP000051919; Unassembled WGS sequence.
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; BLL4482 PROTEIN-RELATED; 1.
DR PANTHER; PTHR35008:SF4; SOXD PROTEIN; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
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 Signal {ECO:0000256|RuleBase:RU365025}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU365025"
FT CHAIN 19..471
FT /note="Copper-containing nitrite reductase"
FT /evidence="ECO:0000256|RuleBase:RU365025"
FT /id="PRO_5015213868"
FT DOMAIN 355..445
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 24..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
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 103
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 138
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 139
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 147
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 152
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 293
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 471 AA; 49493 MW; BF05A68B4998DB8E CRC64;
MKRLLCTMLA AAGMLAMAGC SDKPSAMAAT SAPAQGAPAG TAASGDFGPP QGDPVHAVLT
SPPNVXXXGT VPGSFIRVRQ GDTVEFHLKN APDSKMPHNI DLHGVTGPGG GAASSFTAPG
HESQFTFKAL NQGIYVYHCA TAPVGMHIAN GMYGLILVEP PEGLPKVDHE YYVMQGDFYT
TGKYREKGHQ PFDMDKAIAE QPTYVLFNGH EGALTGDKAL TAKVGDSVRL FVGNGGPNLV
SSFHVIGEIF DRVQPEGGTH PQENVQTTLI PAGGAAIVEF HTQVPGSYVL VDHSIFRAFN
KGAMAILKVD GPEDKAIYSG KEVDSVYLGD RAEPNLHAVS TAAKANASGT LSKDDQIAAG
KQLFTGTCSV CHQANGEGLA NVFPPLAKSD YLAKQDKEHL ISIPLHGLTG KVTVNGKDYD
SVMPPMGQLT DDEVANILTY VLNSWDNPGG QVSKDEVAKV RAQPAPAAPE H
//
