ID A0A0S3EWP6_9SPHN Unreviewed; 869 AA.
AC A0A0S3EWP6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:ALR19861.1};
GN ORFNames=ATN00_05595 {ECO:0000313|EMBL:ALR19861.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR19861.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR19861.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR19861.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
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}.
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DR EMBL; CP013264; ALR19861.1; -; Genomic_DNA.
DR RefSeq; WP_062063077.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3EWP6; -.
DR STRING; 1332080.ATN00_05595; -.
DR KEGG; sbd:ATN00_05595; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000056968; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 869 AA; 93977 MW; B2334BA772DF5777 CRC64;
MGQPIRTTCA YCGVGCGISA TPTGPRSVQI KGDEAHPANA GRLCSKGTHL GETVSLQGRL
LHPMIGQRRA SWDKALDLVA KRFRETIDRH GPDSVAFYVS GQLLTEDYYV ANKLMKGFIG
SANIDTNSRL CMSSAVAGHT RAFGEDVVPA SYGDLAEADL IVLVGSNTAW CHPIVYQRIQ
AARAARGTKL VVIDPRRTET CEGADLHLPV KPGTDVALMN GLLAWVDQAG VTDPAFLAGH
VNAPEDFWEH IRTGHDLWTV AKTCDIAPAL LQQFFELFAA TPRTVTLFSQ GINQSIRGTD
QVNAIINVHL ATGRIGKPGA APFSITGQPN AMGGREVGGL ASTLAAHMDF APENVERVGR
FWAAPAMAAK PGLKAVDLFR AMGEGRIKAL WVMATNPAVS LPDAGRVREA LESCPFVVVS
DVIADTDTSA YADVRLPAAG WGEKDGTVTN SDRTISRQRP FLTLPGEARP DWWIIKEVAR
RMGWRNAFAY DRPAEIWREH ARLTAYQNDG ARVLNLRSHA TIGNDAYEAM EPFRWGGAAF
ADGRFPTTDG KARLVPVRQM DVQAPLKDWP MTLNTGRYRD QWHTMTRTGL SPKLARHREE
PLVEIHPQDA RALALEEGDL ARVSTPQGDS LFRVMFNEGQ RPGEIFTPIH WTDQTSTGGR
TGLLPRPLTD PHSGQPGFKS TPARVERQAV EWKGFLILRG TDPVRLPCLW ATRVTVPSGA
LYEVAGNGDP SRLEACLPKG DRVEAIDVTR GTRRVAIISD GQLTGVLFVT RSGILPSRDW
LIDQLQAPAV GASVLAARGP GNQPDKGATI CVCFDIGLNQ IVAAIREKQL VDVPAIGKAL
GAGTNCGSCR PALASILAQS KQETLHAAE
//
