ID C6WVM1_METML Unreviewed; 480 AA.
AC C6WVM1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Mmol_1061 {ECO:0000313|EMBL:ACT47970.1};
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT47970.1, ECO:0000313|Proteomes:UP000002742};
RN [1] {ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT47970.1, ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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 -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|RuleBase:RU365025}.
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DR EMBL; CP001672; ACT47970.1; -; Genomic_DNA.
DR RefSeq; WP_015832005.1; NC_012968.1.
DR AlphaFoldDB; C6WVM1; -.
DR STRING; 583345.Mmol_1061; -.
DR KEGG; mmb:Mmol_1061; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_031740_1_1_4; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000002742; Chromosome.
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:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 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.
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 ECO:0000313|EMBL:ACT47970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002742};
KW Signal {ECO:0000256|RuleBase:RU365025}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU365025"
FT CHAIN 22..480
FT /note="Copper-containing nitrite reductase"
FT /evidence="ECO:0000256|RuleBase:RU365025"
FT /id="PRO_5015212160"
FT DOMAIN 368..456
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 460..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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 118
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 153
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 154
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 162
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 167
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 309
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 480 AA; 51173 MW; C7415D17BEEE628C CRC64;
MKKIPLLVLG AALCMANIAV AATVTKSNSD KVIGQETAVL TDAPAVPPRI TRKHATKVIV
NLEVKELEGR LADGVSYTFW TFGGKVPGKF IRIREGDDVE FHLNNHPDNK MPHNIDLHAV
TGPGGGAAAS LTAPGHSSVF SFKALNPGLY VYHCATAPVA MHVANGMYGL ILVEPKAGMS
KVDHEFYVMQ GDFYTQGKNG EQGLQAFSMA KAIDEKPEYV VFNGAAGALT GDNALKAKKG
DTVRLFVGVG GPNLTSSFHV IGEIFDKVNH EGNTAAPAKN IQTTMIPAGG AAYMEFKVNV
PGTYIMVDHS LTRAFNKGAL GMLKVSGDED KTIYSGKMTD EVYLPEGTSM RNAERSQAQA
PTAKTKADRV KLGEAIYNNN CAACHQTTGV GVPQAFPPLA KSDYLLNGKA PTIKAVTGGL
QGKLVVNGNE YNGVMPAWTL SDEEVANVLT YIYSSWGNSG DEVTPEEVKQ HRVAPVKHVE
//
