ID   A0A7X6NEF0_9MICO        Unreviewed;       885 AA.
AC   A0A7X6NEF0;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   02-OCT-2024, entry version 13.
DE   RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE            EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN   ORFNames=GX871_02945 {ECO:0000313|EMBL:NLA09153.1};
OS   Microbacteriaceae bacterium.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX   NCBI_TaxID=1873462 {ECO:0000313|EMBL:NLA09153.1, ECO:0000313|Proteomes:UP000535309};
RN   [1] {ECO:0000313|EMBL:NLA09153.1, ECO:0000313|Proteomes:UP000535309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS16jrsBPLL_32 {ECO:0000313|EMBL:NLA09153.1};
RX   PubMed=32123542;
RA   Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M.,
RA   Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A.,
RA   Konstantinidis K.T., Angelidaki I.;
RT   "New insights from the biogas microbiome by comprehensive genome-resolved
RT   metagenomics of nearly 1600 species originating from multiple anaerobic
RT   digesters.";
RL   Biotechnol. Biofuels 13:25-20(2020).
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:NLA09153.1}.
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DR   EMBL; JAAZHU010000135; NLA09153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7X6NEF0; -.
DR   Proteomes; UP000535309; 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: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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          467..529
FT                   /note="EfeO-type cupredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF13473"
FT   DOMAIN          636..734
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   REGION          559..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         672
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         677
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         711
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         712
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         720
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         725
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         863
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   885 AA;  91427 MW;  E15AA09BB6115C71 CRC64;
     MSRRNWYLLT NSLVLLWIAL AIVATIIHRF VAQPLWLMVH VPLLGAATAA ILVWSQHFAD
     TVLRRTGPSG RIGLGIRLAL HTVGVSLVIA GMLGSGLLLT LAGALLVGCA IVAHAVILML
     QIRGALPTRF APMVWYAVAA SIVFLAGIAA AIAMVLAVDP ALVERLAMSH LVLGVFGWIG
     LTALGILSLL WPTVLRTQLS AGAGASVRFA LPVLLVGLAV AAAGPLLGIP AVLALGLVLW
     LVGAVRLAVE AWREARTAPP RSFAAWSLAA AFVWALLSAV ALGATALLAE DWGSLKDDTL
     LVLGPLGAGF VMQLVMGALS HLVPVVIIGS PSSSAAAAAV LDRGAAFRVF AFNGAIALYV
     LPMPSIVRVL LAALAAGVVT AFVVLAIRAI VASRRMLREE LAAGAAGRAE RIAARRAEPP
     RATPRRAGGV TAAFTVLALC VAGGVAADPV AAGISAVSPG EGVAASGQVT RVTVQVTGMR
     FDTDVIEVPY GNRLEVTFEN TGTDVHDLTF ENGARTQRLA PGESETIDVG VIGADMAGWC
     TVAGHRQMGM ELSVVVTGAP DGGGEASTGG AGTAGEHAGG HEAAGAGDAA ADIDWQREPA
     AGFTAWPALL APAPEGTVHA ITLRAEESVE EVAPGITQAR WTFGGSAPGP TLRGKIGDVF
     EITLINDGTI GHSIDFHAGA LAPDEPMRTI APGESLVYRF TATRAGIWMY HCSTMPMSMH
     IANGMFGAVI IDPPGLAPVA AEYVLVQGEL YLGAQGDVAN AEKIAEERPD LVAFNGYADQ
     YLHQPLTATA GERVRVWVLD AGPNRPSSFH VIGGQFDTVY LEGAYRLLPD DPGGSQALGL
     QPAQGGFVEL VFPEAGNYPF VTHRMSDAEK GARGVFRVGD PGAAG
//