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Database: UniProt
Entry: A0A3N4PRC2_9BACT
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Original site: A0A3N4PRC2_9BACT 
ID   A0A3N4PRC2_9BACT        Unreviewed;      1179 AA.
AC   A0A3N4PRC2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=NAD(P)H-nitrite reductase {ECO:0000313|EMBL:RPE09299.1};
GN   ORFNames=EGT74_20075 {ECO:0000313|EMBL:RPE09299.1};
OS   Chitinophaga lutea.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=2488634 {ECO:0000313|EMBL:RPE09299.1, ECO:0000313|Proteomes:UP000278351};
RN   [1] {ECO:0000313|EMBL:RPE09299.1, ECO:0000313|Proteomes:UP000278351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZY74 {ECO:0000313|EMBL:RPE09299.1,
RC   ECO:0000313|Proteomes:UP000278351};
RA   Zong Y.;
RT   "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747}.
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:RPE09299.1}.
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DR   EMBL; RPDH01000002; RPE09299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4PRC2; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000278351; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278351}.
FT   DOMAIN          2..58
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1179 AA;  130072 MW;  002B62FF0ADFE0AF CRC64;
     MQDSFKTTCC YCGVGCGIVV HRDRLGKLTV EGDKDHPVNR GMLCSKGMNL HYTVMDTSDR
     LLHPEMRYNR NLPRQRVSWD QALGRTAAVF SQIIRRYGPE SVAFYASGQC LTEEYYVVNK
     LIKGFIGSNN IDTNSRLCMS SAVAAYKMAL GEDAVPGSYD DIEHTDCIFV AGANPAWCHP
     ILWRRVEAAR AANPRLKIIV SDPRVTQSCA MADVHLQLNP GTDIVLHHAL GRILIEKGKT
     DPAFIHQHTE GFEAYREAVM QRSIEEAALI CGIDAADIYA AAGHIAGAKG FMTMWTMGLN
     QSAVGVRKNL SLINLHLITG HIGKPGSGPF SLTGQPNAMG GREVGGLANL LPAHRVLDNP
     EHRREVAAFW GGGELSPKPG LTATQMFEAM HSGQLKAIWI MCSNPLVSLP DARFMEAALQ
     KAMFVVVQEI SNKPETLRYA DVVLPAAAWA EKEGTMTNAE RRISYLTKIT DAPGEALPDS
     EIICRFAQKM GYHGFDYPHV SAIYEEHCRL TAGTNIDITG LNYNVLREQR SVQWPYPAGA
     TGHGTPRLFT DHQFYTAHQK AVIHSFGDEN TSAPPDRDYP LILTTGRIRD QWHTMSKTGK
     VSKLKQHIDA AFLEIHPDDA RTRNIRQNDM VEVTSGNGMV RVKALLSTTI KKGVVFLPMH
     WGKILNNDLH RANNLTNNLV DPVSKQPDLK FTAVAVARYE KPVQKIVVIG AGAGAYGFVK
     SYRQLNQRDE ITVFSKEDLP FYNRVMLPDY ISGARQWAQL IKMSEAEERN FDITLHRGLS
     IEKIDRENKV LTDSKGITHT YDVLILATGS RAATLRDTPP LTGIFTMRSR MDADAFLRHI
     DPAGGKIVIA GGGLLGIELA ASLREMNMEV AVIQRTSRLM DRQLDALGAQ LLYEELKDRG
     IDIYFTDEIE QFAGTRKVEG VRLKSGRSIA CQAVVISIGT VPNIELAQAA QLECNRGVVV
     NEYLQTSDPG IYAIGEIASC NNILYGITAA AEQQAGVVAR HLGGDISGYY EGSLFMNILK
     MQGMELCSMG MVETPPDQAY EEVVFIDKSH RYYKKCIIHQ DRLVGAILIG DKSEFQEFCD
     LIRQKTELSE KRLQLLRSGR KGAALMGKLV CSCGNVGEGN IQEKIREGHT ELESLCRASG
     AGLGCGSCRP EVQNLLGACK PKIKTQLQTH GQAVTTHPH
//
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