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   03-AUG-2022, entry version 103.
DE   RecName: Full=Nitrate reductase;
DE            EC=1.7.-.-;
GN   Name=nasA;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; 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.MC52_25290; -.
DR   eggNOG; COG0243; Bacteria.
DR   BioCyc; MetaCyc:MON-13446; -.
DR   UniPathway; UPA00652; UER00706.
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: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   Gene3D; 1.10.10.1100; -; 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   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; SSF50692; 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