ID A0A514WN95_9SPHN Unreviewed; 877 AA.
AC A0A514WN95;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:QDK34961.1};
GN ORFNames=DM450_19570 {ECO:0000313|EMBL:QDK34961.1};
OS Sphingomonas sp. IC081.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=304378 {ECO:0000313|EMBL:QDK34961.1, ECO:0000313|Proteomes:UP000319092};
RN [1] {ECO:0000313|EMBL:QDK34961.1, ECO:0000313|Proteomes:UP000319092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IC081 {ECO:0000313|EMBL:QDK34961.1,
RC ECO:0000313|Proteomes:UP000319092};
RA Vejarano F., Suzuki-Minakuchi C., Ohtsubo Y., Tsuda M., Okada K.,
RA Nojiri H.;
RT "Draft Genome Sequence of the Carbazole-Degrading Bacterium Sphingomonas
RT sp. IC081.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP029762; QDK34961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A514WN95; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000319092; Chromosome c2.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0045333; P:cellular respiration; IEA:UniProt.
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; 3.40.50.740; -; 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 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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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 SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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:UP000319092}.
FT DOMAIN 2..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 877 AA; 94265 MW; 1F8045B7E3E135D0 CRC64;
MRAAVRTTCA YCGVGCGIAA TPNPNGAGER SVEIRGDEAH PANAGRLCSK GTHLGETVAL
TGRLLTPMIG DRRASWDKAL DLVARRFAET IARHGPDSVA FYVSGQLLTE DYYVANKLMK
GFIGSANIDT NSRLCMSSAV AGHMRAFGED VVPARYDDLE AADLVVLVGS NTAWCHPIVY
QRIQAARAAR GSKLVVIDPR RTETCEGADL HLALRPGSDV ALMKGLLAWL AAEDALDRDY
LAAHVEVPGG FWEELEATSD LWTTAKTCDL DPQALLRFFE LFRDNPRTVT VFSQGINQSI
RGTDQVNAIL NLHLATGRIG KPGAAPFSIT GQPNAMGGRE VGGLASTLAS HMDFAPENVA
RVGRFWAAPN MATRPGLKAV DLFRAMGEGR IKAVWIMATN PAVSLPDAAR VREALAKCPF
VVVSDVMAET DTGAHAHVRL PAAAWGEKDG TVTNSERVVS RQRRFMALPG EAMPDWWIIK
EVGRRMGWKG EFAYDHPADI WREHARLTAY QNDGPASGGR VLNLADKAAI GNQAYEDMAP
FRWGGTPFAD GRFSTPSGKA RMLPVVQMEL QDPLRDWPLT LNTGRYRDQW HTMTRTGLAP
KLARHREEPL VEVNPGDAEV MGLRSGDLAR VATPQGDSLF RVALSDGQRP GEIFTPIHWT
DQTSTGGRTG LLPRPLVDPH SGQPGFKSTP ARLAKVATEW KGFLILRGEH PVKVPCLWAT
KVAVPGGALY EIAGNGDPAR IEACLPRGER VEAIDQARGS RRVAVIVEGR LAGVLFLTRT
GLLPSRDWLI GQLAAEGVGA AVLAARGPGS QPDKGATICV CFDIGLNQIV AAIREQALVD
VPAIGKALGA GTNCGSCRPA LAKILVQTNE EVLDAAE
//
