ID A0A399F3G8_9DEIN Unreviewed; 391 AA.
AC A0A399F3G8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN Name=aniA {ECO:0000313|EMBL:RIH89151.1};
GN ORFNames=Mrose_00536 {ECO:0000313|EMBL:RIH89151.1};
OS Calidithermus roseus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Calidithermus.
OX NCBI_TaxID=1644118 {ECO:0000313|EMBL:RIH89151.1, ECO:0000313|Proteomes:UP000265341};
RN [1] {ECO:0000313|EMBL:RIH89151.1, ECO:0000313|Proteomes:UP000265341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110900 {ECO:0000313|EMBL:RIH89151.1,
RC ECO:0000313|Proteomes:UP000265341};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus roseus NBRC 110900 genome sequencing project.";
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:RIH89151.1}.
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DR EMBL; QWLA01000005; RIH89151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399F3G8; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000265341; Unassembled WGS sequence.
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; cd11024; CuRO_1_2DMCO_NIR_like; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1};
KW Oxidoreductase {ECO:0000313|EMBL:RIH89151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265341}.
FT DOMAIN 110..223
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 246..355
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 35..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
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 160
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 200
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 201
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 209
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 214
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 339
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 391 AA; 43413 MW; 647F31AB6BA56EB1 CRC64;
MRSFLPKLFS RRQVLRSLGG VAGVAGAAAL GLGQGPKPAP QGEVGGHSGH YMGAADPKQM
GHGNNLTVGV VDHQANGFDP LRLLVDWDYG KVSMLPSGQT LREYEFVAQE KEIEIAPGVF
FPAWTYNGRV PGPTIRCTEG DRIRVRFTNS SSHPHTIHFH GIHPAEMDGT PLPGNGGLVQ
PGQSLTYEFT AEPFGCHLYH CHSLSLKRHI HKGMYGAFIV DPKGGRPPAR EFVMVMNAFD
TNFDGGNEVY AVNSVAFEYA RRAIPLKLGE LVRIYLINVL EFDPLNTFHL HANMFDYYDH
GTTLEPTLRR VDTISQVQGQ RGIIEFRYKF PGMYMFHPHV SEFTELGWMG HFNVVKPEDF
AQALQSVGLD AAWDQKSLQG SIVPWKRGEQ A
//
