ID A0A0W1G6C5_9SPHN Unreviewed; 865 AA.
AC A0A0W1G6C5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KTE50327.1};
GN ORFNames=ATE69_18395 {ECO:0000313|EMBL:KTE50327.1};
OS Sphingopyxis sp. H071.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE50327.1, ECO:0000313|Proteomes:UP000054127};
RN [1] {ECO:0000313|EMBL:KTE50327.1, ECO:0000313|Proteomes:UP000054127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H071 {ECO:0000313|EMBL:KTE50327.1,
RC ECO:0000313|Proteomes:UP000054127};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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}.
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:KTE50327.1}.
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DR EMBL; LNSF01000013; KTE50327.1; -; Genomic_DNA.
DR RefSeq; WP_058457376.1; NZ_LNSF01000013.1.
DR AlphaFoldDB; A0A0W1G6C5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000054127; Unassembled WGS sequence.
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}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 865 AA; 93112 MW; E59455B48F06FE28 CRC64;
MTEAVRTTCA YCGVGCGIRA TVTGERSVEI AGDPDHPANR GRLCSKGTHL GETVGLEGRL
LHPTIGAKRA SWDKALDLVA KRFKETIARH GPGSVAFYVS GQLLTEDYYV ANKLMKGFIG
TANIDTNSRL CMSSAVAGHM RAFGEDVVPA TYDDLDAADL FVLVGSNTAW CHPIVYQRIR
ARCEAGAKLV VIDPRRTETA EEADLHLAVR PGSDVALMNG LLQHCRETGI VDEDYLAAHV
AAPAEYWDQL GEGNDLWSVA RICDVPAADL RHFYELFAAN PRTVTLFSQG INQSTAGTDQ
VNAITNLHLA TGRIGKPGAA PFSITGQPNA MGGREVGGLA STLAAHMDFS PENRARVQRF
WAAPTIAEKP GLKAVDLFRA IGEGRIKALW VMATNPAVSM PDGNAVREAL AACPFVVVSD
VIEKTDTGSF AHVRLPAAAW GEKDGTVTNS DRTISRQRAL FALPREAMPD WWIVKEVGRR
MGWKTAFAYD RPADIWREHC RLSTYDNDGA RLFALPGAAQ GGTAAYDEME PFRWGGDHPF
ADGRFSTEDG RARLVPITQK PLPAPLTKWP LTLNTGRYRD QWHTMTRTGL APKLARHREE
PLVEIHPDDG SRLGLTDGGL ARVETPQGDS LYRVAFHSGQ RHGELFVPIH WTDRTASGGR
TGLLPRPLVD PVSGQPGFKR TPASIAAVVP RWRGFLLLSR ELASAPRCLW ATRVAVPAGV
MWELAGNGDL KAIEALLPKG ERIEAQDAAR GTKRIAIVAN GRLSGALFVT ETGELPSRDW
LIAQLSAPQV APTLLAGRAP GAQADRGPII CVCFDVGLRT IVAAIRDQKL ADVAAIGGAL
GAGTNCGSCR PALARILAEE TSNAA
//
