ID A0A371NRV1_9MICO Unreviewed; 862 AA.
AC A0A371NRV1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN ORFNames=DY023_11585 {ECO:0000313|EMBL:REJ04894.1};
OS Microbacterium bovistercoris.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2293570 {ECO:0000313|EMBL:REJ04894.1, ECO:0000313|Proteomes:UP000262172};
RN [1] {ECO:0000313|EMBL:REJ04894.1, ECO:0000313|Proteomes:UP000262172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-LLE {ECO:0000313|EMBL:REJ04894.1,
RC ECO:0000313|Proteomes:UP000262172};
RA Ling L.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from cow
RT dung.";
RL Submitted (AUG-2018) 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 -!- 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|ARBA:ARBA00001973,
CC ECO:0000256|PIRSR:PIRSR601287-1};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
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:REJ04894.1}.
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DR EMBL; QUAB01000044; REJ04894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371NRV1; -.
DR OrthoDB; 345021at2; -.
DR Proteomes; UP000262172; 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; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF13473; Cupredoxin_1; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 4: Predicted;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262172};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..517
FT /note="EfeO-type cupredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF13473"
FT DOMAIN 610..715
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT REGION 546..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 653
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 658
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 692
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 693
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 701
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 706
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 845
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 862 AA; 89848 MW; 758147BC0936C34A CRC64;
MRDIPTAVWL LLTIVAAVAH RALPAPGWLM IHLLLVGAVT HAILTWSQYF SWALLRGRPT
PTDARTQTIR LILSNAGAAL VIAGVLSSIW PITLVGATSL IVAVGWHGAS LIRRARRSMP
GRFGRTVRYY IVSAALLMVG AAIGAVLARG GDLPNLVLAH ALINVLGWIG LTVAGTVVTL
WPTVLRTRAD AHAADGAARA LPWLAAGVSV AALGAALAWL PVLALGLAAY LGGLVVIGIS
LWRVARSKPP RSFAAMSVGM ALIWWAGAVA MLIAGTVIAF ADGSGFAAVS ALLDGIVPYL
AAGFAAQVLL GALSYLVPVV LGGGPTPVRI GTAAFDRGAA WRVTVANAAL AVCALPVSSL
SRVVASVLYL IAMASFLPIM FLAMRAQRRA KAVGMTLSGT HTGPIVPEGE RPRGRRAGQA
VTGLLAVVLA VAVPAAADPA GFGWSAAPTG DADAPVKTVQ VEAADMRFTP SRIEVPAGTR
LVIELTNTDE EQVHDLVFAN GVAGGRLAPG ESQTIDVGVI AKDLDGWCSI IGHRQMGMTM
SIVATGASGS SSDAGTSDAG GHGEHAASAP IDLMADPGED FTPFDAGLPA LPASAGPAHR
RLTLTARDVE TEVAPGVTQT LWAYDGTAPG PVLHGRVGDT FEITLVNDGT MGHSIDFHAG
SLAPDRPMRT IVPGESLTYT FTATRAGIWM YHCSTMPMTA HIANGMYGAV VIEPDDRPAV
DRSYVLVQGE YYLGDHDGGE VDLDRIATRN PDLVVFNGYA NQYDHAPLPA TVGERVRVWV
LDAGIERSSS FHVIGGQFDT VWAEGRYLLN RSADTGSQAL GLMPAQGGFV ELTFPEAGHY
PFVSHFMIDA ERGAHGVFDV TG
//
