ID A0A0W1DNW9_9SPHN Unreviewed; 865 AA.
AC A0A0W1DNW9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KTE19807.1};
GN ORFNames=ATE67_14355 {ECO:0000313|EMBL:KTE19807.1};
OS Sphingopyxis sp. H050.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE19807.1, ECO:0000313|Proteomes:UP000053439};
RN [1] {ECO:0000313|Proteomes:UP000053439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA Gomez-Alvarez V., Revetta R.P.;
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:KTE19807.1}.
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DR EMBL; LNRZ01000006; KTE19807.1; -; Genomic_DNA.
DR RefSeq; WP_058817355.1; NZ_LNRZ01000006.1.
DR AlphaFoldDB; A0A0W1DNW9; -.
DR STRING; 1759072.ATE67_14355; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000053439; 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 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.
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; 92970 MW; 595FDDAC5932DACF CRC64;
MADAVRTTCA YCGVGCGIRA TVTGARSVEI AGDPDHPANR GRLCSKGTHL GETVGLEGRL
LHPMIGSKRA SWDKALDLVA KRFKETIARH GPGSVAFYVS GQLLTEDYYV ANKLMKGFIG
TANIDTNSRL CMSSAVAGHT RAFGEDIVPA TYDDLDAADL FVLVGSNTAW CHPIVYQRIR
ARCEAGAKLV VIDPRRTETA EEADLHLAIR PGSDVALMNG LLQHCRETGV VDEDYLAAHV
AVPQDFWDQL GEGNDLWSVA RICDVPAADL RHFYEMFAAN PRTVTLFSQG INQSAAGTDQ
VNAITNLHLA TGRLGKPGAA PFSITGQPNA MGGREVGGLA STLAAHMDFA PENRARVQRF
WAAPTMAEKA GLKAVDMFRA IGEGRIKALW VMATNPAVSM PDGNAVREAL KTCPFVVVSD
VIEKTDTGAF AHIRLPAAAW GEKDGTVTNS DRMISRQRAL FALPGEAMPD WWIVKEVGRR
MGWKNAFTYD RAADIWREHC RLSTYDNGGA RLFALPGAAR GGTAAYDAMQ PFRWGGDHPF
ANGRFSTEDG RARLVPVAQK LVPEPLAKWP LTLNTGRYRD QWHTMTRTGL APKLARHREE
PLVEVHPDDG ARLGLSDGGL ARVETPQGDS IYRVAFHAGQ RAGELFVPIH WTDRTSSGGR
TGLLPRPLVD PVSGQPGFKR TPASIASIAP KWRGFLLLAR ELASTPRCLW ATRVAVPSGV
MWELAGNGDL KAIEALLPKG ERIEAQDAAR GTKRIAIVAN GRLSGALFVT ETGELPPRDW
LIAQLSAPQT APTLLAGRAP GVQADRGPVI CVCFDIGLKT IVAAIRDRKL ADVAAIGGAL
GAGTNCGSCR PALARILTEE TSNAA
//
