ID NASA_KLEOX Reviewed; 866 AA. AC Q06457; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 27-MAR-2024, entry version 109. DE RecName: Full=Nitrate reductase; DE EC=1.7.-.-; GN Name=nasA; OS Klebsiella oxytoca. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=571; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=M5a1; RX PubMed=8468296; DOI=10.1128/jb.175.8.2370-2378.1993; RA Lin J.T., Goldman B.S., Stewart V.; RT "Structures of genes nasA and nasB, encoding assimilatory nitrate and RT nitrite reductases in Klebsiella pneumoniae M5al."; RL J. Bacteriol. 175:2370-2378(1993). RN [2] RP SEQUENCE REVISION. RA Stewart V.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step CC of nitrate assimilation in plants, fungi and bacteria. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo- CC bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); CC dinitrogen from nitrate: step 1/4. CC -!- INDUCTION: By nitrate or nitrite during nitrogen-limited growth. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L06800; AAA25100.2; -; Genomic_DNA. DR AlphaFoldDB; Q06457; -. DR SMR; Q06457; -. DR STRING; 571.AB185_18740; -. DR eggNOG; COG0243; Bacteria. DR BioCyc; MetaCyc:MONOMER-13446; -. DR UniPathway; UPA00652; UER00706. 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:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway. 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 2: Evidence at transcript level; KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation; KW Oxidoreductase. FT CHAIN 1..866 FT /note="Nitrate reductase" FT /id="PRO_0000063235" FT DOMAIN 1..57 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 8 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 11 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 15 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" SQ SEQUENCE 866 AA; 93897 MW; 2B6B464578784DD5 CRC64; MTETRTTCPY CGVGCGVIAS RAPHGQVSVR GDEQHPANFG RLCVKGAALG ETVGLEGRML FPEVDGERAT WPQALAAAGS RLREIIDRHG PQAVAFYASG QLLTEDYYAA NKLMKGFIGA ANIDTNSRLC MSSAVTGYKR ALGADVVPCS YEDVENSDLV VLVGSNAAWA HPVLYQRLAQ AKRDNPQMRV VVIDPRRTAT CDIADRHLAL APGSDGGLFV GLLNAIAASG AISDDFNDAQ RALTIAQDWD LDKVAQFCGL PRQQIADFYR EFIAAPRAIT LYTMGINQSA SGSDKCNAII NVHLACGKYG RPGCGPFSLT GQPNAMGGRE VGGLATMLAA HMNFEPDDLR RLARFWGSER LAQTPGLTGV ELFAAIGRGE VKAVWIMGTN PVVSLPDSHA VSEALARCPL VIISDVVADT DTGRFAHIRF PALAWGEKSG TVTNSERRIS RQRAFMPPPG EARADWWIVA RVAEALGFGS AFAWQHPHEV FSEHAALSGY ENDGQRAFDI GGLADLSREA WDALEPVRWP VSRSEAAWSV HKGWHRDGKL RMVPVAPQPT RATTDAFYPL ILNSGRIRDQ WHTMTRTGAV PRLMQHINEP VVEVAPADAQ RYHLLEGELA RVRSPKGVMV AKVTIGDGQR PGSLFVPMHW NNQFARQGRV NNLLAAVTDP HSGQPESKQT AVAIATWLPA WKGELFSRQP VPLPASLHWR RRAAQGIIHL SLAGDTRSRD WLVEWCQRQG WQMQVAEGGK VWNLLAWRAG ELMLGWWSDA SEPAIDADWI HAAFRVPPQN AARRHALLSG RKGGVEMPRG RIICSCFSVG ERAIGEAIAG GCRTPGALGG KLKCGTNCGS CIPELKALLA AKLAQA //