ID   NAPA_ECO5E              Reviewed;         828 AA.
AC   B5YWZ7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
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};
GN   OrderedLocusNames=ECH74115_3343;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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}.
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DR   EMBL; CP001164; ACI38621.1; -; Genomic_DNA.
DR   RefSeq; WP_000778047.1; NC_011353.1.
DR   AlphaFoldDB; B5YWZ7; -.
DR   SMR; B5YWZ7; -.
DR   KEGG; ecf:ECH74115_3343; -.
DR   HOGENOM; CLU_000422_13_4_6; -.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
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   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01706; NAPA; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 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; Signal; Transport.
FT   SIGNAL          1..31
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   CHAIN           32..828
FT                   /note="Periplasmic nitrate reductase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT                   /id="PRO_1000186356"
FT   DOMAIN          39..95
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         49
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         81
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         83
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         150
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         175
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         179
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         212..219
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         243..247
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         262..264
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         372
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         376
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         482
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         508..509
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         531
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         558
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         718..727
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         794
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         802
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         819
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
SQ   SEQUENCE   828 AA;  93057 MW;  967121CB05C59323 CRC64;
     MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
     QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW
     DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM
     ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQDVTVA
     VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG
     YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA
     DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
     GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC
     TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER
     RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEELL AKKPELRGKT LYEVLYATPE
     VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV
     VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR
     VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR
     GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV
//