ID   NAPA_WOLSU              Reviewed;         928 AA.
AC   Q7M962; Q8GBG1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630}; OrderedLocusNames=WS1178;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 /
OS   NCTC 11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12823811; DOI=10.1046/j.1365-2958.2003.03544.x;
RA   Simon J., Saenger M., Schuster S.C., Gross R.;
RT   "Electron transport to periplasmic nitrate reductase (NapA) of Wolinella
RT   succinogenes is independent of a NapC protein.";
RL   Mol. Microbiol. 49:69-79(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC   NCTC 11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC       of nitrate to nitrite. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC         [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC         COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC       composed of NapA and NapB. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE10263.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ512686; CAD55547.1; -; Genomic_DNA.
DR   EMBL; BX571660; CAE10263.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041572131.1; NC_005090.1.
DR   AlphaFoldDB; Q7M962; -.
DR   SMR; Q7M962; -.
DR   STRING; 273121.WS1178; -.
DR   KEGG; wsu:WS1178; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_4_7; -.
DR   Proteomes; UP000000422; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
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; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 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   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR01706; NAPA; 1.
DR   PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 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   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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   Nitrate assimilation; Oxidoreductase; Periplasm; Reference proteome;
KW   Signal; Transport.
FT   SIGNAL          1..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   CHAIN           34..928
FT                   /note="Periplasmic nitrate reductase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT                   /id="PRO_0000046014"
FT   DOMAIN          40..96
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         47
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         84
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         152
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         177
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         181
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         214..221
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         265..267
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         422
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         426
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         532
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         557..558
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         580
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         607
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         818..827
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         894
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         902
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         919
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
SQ   SEQUENCE   928 AA;  104968 MW;  9D5A8D055AA6D451 CRC64;
     MAFSRREFLK SAAAASAASA VGMSVPSQLL AQAQEGEKGW RWDKSVCRFC GTGCGIMVAT
     KNDQIVAVKG DPAAPVNRGL NCIKGYFNAK IMYGADRLTD PLLRVNEKGE FDKQGKFKPV
     SWKKAFDVME AQFKRAYNEL GPTGIGVFGS GQYTIQEGYM AAKLIKGGFR SNNLDPNARH
     CMASAVAAFM ETFGIDEPAG CYDDIELTDT IITWGANMAE MHPILWARVT DKKLSNPDKV
     KVINLSTYTN RTSDLADIEI IFTPQTDLAI WNYIAREIVY NHPESIDMEF VKNHCIFTTG
     FTDIGYGMRT DIKHAKYDPK ELDIAAKERS KVLSEAEGVT LRYLGMKAGD VMEMKHNATA
     GNHWEITFED FKKALEPYTL DFVAKLAKGN SEESLESFKE KLQKLANLYI EKERKVVSFW
     TMGMNQHTRG TWVNEQSYMV HFLLGKQAKP GSGAFSLTGQ PSACGTAREV GTFSHRLPAD
     MVVANPKHRA VSEKIWKLPE GTLNPKMGAH YMNIMRDLED GKIKFAWIQV NNPWQNTANA
     NHWIKAAREM DNFIVCSDAY PGISAKVADL ILPTAMIYEK WGAYGNAERR TQHWRQQVVP
     VGNAMPDVWQ MAEFSKRFKL KEVWGAKKID DKLTLPDVLE KAKAMGYSPE DTLFEVLFAN
     SEAKSFKAKD PIGEGFENTE VFGDRRNVAG SDGEVFKGYG FFIHKYLWEE YRRFGNGHGH
     DLADFDTYHK VRGLKWPVVD GKETQWRFNA KYDPYARKAG SGEFAFYGDA MKELPRGDLL
     SPKTEEKFKL TNKAKIFFRP YMDPPEMPSS EYPLWLCTGR VLEHWHSGTM TMRVPELYRA
     VPEALCYMHP EDAKKLGVKQ NEAVWVESRR GKVKARVDTR GRNRTPLGLV YVPWFDEKVY
     INKVCLDATC PISKQTDFKK CAVKVYKA
//