ID   Q9WX89_CLOPF            Unreviewed;       692 AA.
AC   Q9WX89;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Nitrate reductase catalytic subunit {ECO:0000313|EMBL:BAA74791.1};
GN   Name=narA {ECO:0000313|EMBL:BAA74791.1};
OS   Clostridium perfringens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502 {ECO:0000313|EMBL:BAA74791.1};
RN   [1] {ECO:0000313|EMBL:BAA74791.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PB6K {ECO:0000313|EMBL:BAA74791.1};
RX   PubMed=10627036;
RA   Fujinaga K., Taniguchi Y., Sun Y., Katayama S., Minami J., Matsushita O.,
RA   Okabe A.;
RT   "Analysis of genes involved in nitrate reduction in Clostridium
RT   perfringens.";
RL   Microbiology 145:3377-3387(1999).
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; AB017192; BAA74791.1; -; Genomic_DNA.
DR   RefSeq; WP_003481844.1; NZ_UFWR01000001.1.
DR   PATRIC; fig|1502.176.peg.2158; -.
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: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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_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; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 2.
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}.
SQ   SEQUENCE   692 AA;  78437 MW;  A40857B3E0B94569 CRC64;
     MKRIQSTCNY CALACNLDFY TEDGKIKRVV PTPHYPVNKG FSCIKGLNLD KQCTKFNGSK
     KPLLKMKDGE RKAIEWKEAF DLFASKMTAI QEKYGKESVA YISTGQLPTE EMALLGHVGR
     SYMGINGDGN TRLCMASAVV AYKQSFGFDA PPYTLKDLEL SDTIFFIGAN PVIAHPIAWG
     RVRKNKDAKI ITIDPRKSET AMNSDMWIDI KTKGDLALFY TLANVLIEKG WINQDYINNY
     TEGFEDFKAH VKKYTLEDVE ERTGISKMRV LELAKIIHEG KRVSFWWTMG VNQSYEAVRT
     AQAIINLALI TGNMGREGTG ANSLTGQCNA MGSRMFSNTT ALYGGGEYNN KERRKVVADI
     LGMDENMLPT KPTLDYEQII KGINKGEIKG LWVVCTNPRH SFSNNEEFKK AMKNLDFFVV
     QDIYEDTDSS KECDLYLPSV PAIKKEGFLI NTERRLSALV PVLEKEEDEL SDYEILLGIG
     EALGMGSLLD KWRTPEDAFK LLRECSKGMP CDITGVSYER LRDSKGIQWP CRKGEELESD
     ERRLFEDGKY YTPSGKAKFI FEDVTENPNA TNEEFPFNLN TGRGTVGQWH THTRTREIQA
     VTNIVSQKAY VDINRKDAEK LDIKENDEVL IHSSNGHTSK FIARLTDNLK EKTLYAPIHY
     IETNLLTPSV FDPYSKEPSY KTVQVNIEKV RK
//