ID A0A1Q5PGZ1_9BACT Unreviewed; 491 AA.
AC A0A1Q5PGZ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN ORFNames=A3841_10640 {ECO:0000313|EMBL:OKL41500.1};
OS Pontibacter flavimaris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL41500.1, ECO:0000313|Proteomes:UP000186551};
RN [1] {ECO:0000313|EMBL:OKL41500.1, ECO:0000313|Proteomes:UP000186551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S10-8 {ECO:0000313|EMBL:OKL41500.1,
RC ECO:0000313|Proteomes:UP000186551};
RA Zhang G., Zhang R.;
RT "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT isolated from marine sediment of the Yellow Sea, China.";
RL Submitted (MAR-2016) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:OKL41500.1}.
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DR EMBL; LVWA01000003; OKL41500.1; -; Genomic_DNA.
DR RefSeq; WP_073850912.1; NZ_LVWA01000003.1.
DR AlphaFoldDB; A0A1Q5PGZ1; -.
DR STRING; 1797110.A3841_10640; -.
DR OrthoDB; 9811395at2; -.
DR Proteomes; UP000186551; 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 4: Predicted;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..491
FT /note="Copper-containing nitrite reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012140597"
FT DOMAIN 382..470
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 127
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 132
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 168
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 176
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 181
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 322
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 491 AA; 52773 MW; 3F0C9BF71B109109 CRC64;
MKRSTLKKTV VLLGLGLYSM GILSSCSTQS SHAETAAKTD DAIPKELPTV EAELTDAPKV
PAPITRSHAA KVVVRLEVTE VVKKMADGVD YTFWTFGGSV PGKFIRIRQN DEVEFHLMNH
PDSKNPHNID LHAVTGPGGG AASTFTAPGH ETVFKFKALN PGLYVYHCAT APVGMHIANG
MYGLILVEPE EGLPKVDKEY YVMQGDFYTK GDFGAPGLQP FDMQKALDEN PSYVVFNGSV
GALTGDNALT AKVGETVRLF VGNGGPNLIS SFHVIGEIFD KVYDEGGSTA IENIQTTLVP
AGGTAITEFK ADVPGNYVLV DHSIFRAFNK GALGMLKVEG TEDKKIYSGQ IVQKIYQPEG
STVQEMPSAG APKAAIASSK DMRLELGKTL YAQNCQACHQ AEGQGIKGAF PPLAKSDYLN
ADVDRAIGVV AHGLEGQIKV NGELYNSTMP KLKLSDEEIA NVMTFVMNNW SNKGGEVTPD
QVKKAKDNYK H
//
