ID NAPA_NITSB Reviewed; 936 AA. AC A6Q604; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 94. 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=NIS_1808; OS Nitratiruptor sp. (strain SB155-2). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales; OC Nitratiruptoraceae; Nitratiruptor. OX NCBI_TaxID=387092; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB155-2; RX PubMed=17615243; DOI=10.1073/pnas.0700687104; RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., RA Horikoshi K.; RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into RT emergence of pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007). 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 --------------------------------------------------------------------------- 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; AP009178; BAF70913.1; -; Genomic_DNA. DR RefSeq; WP_012083176.1; NC_009662.1. DR AlphaFoldDB; A6Q604; -. DR SMR; A6Q604; -. DR STRING; 387092.NIS_1808; -. DR KEGG; nis:NIS_1808; -. DR eggNOG; COG0243; Bacteria. DR HOGENOM; CLU_000422_13_4_7; -. DR InParanoid; A6Q604; -. DR OrthoDB; 7376058at2; -. DR Proteomes; UP000001118; 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 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 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 Pfam; PF10518; TAT_signal; 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..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT CHAIN 32..936 FT /note="Periplasmic nitrate reductase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT /id="PRO_1000069721" 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 246..250 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 424 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 428 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 534 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 559..560 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 582 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 609 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 826..835 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 902 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 910 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 927 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" SQ SEQUENCE 936 AA; 106390 MW; 7171B3121E2C1E10 CRC64; MALSRRDFLK SSAAAAAASA VGLSVPKEVE AASKEAQKGW RWDKAVCRFC GTGCGIMIAT KDDRIVAVKG DPLAPVNRGL NCIKGYFTAK IMYGADRLKT PLLRMNDKGE FDKKGKFRPV SWKRAFDEME KQFRKAYNEL GPTGVAFFGS GQYTVMEGYA AAKLMKAGFR SNNIDPNARH CMASAVAGFI QTFGIDEPAG CYDDIELTDT IVLWGSNMAE MHPILWARCT DRKLSDPNKV KVVVLSTYTH RSCDLADDVI IFKPNTDLAI WNYIARSIVY DHPDAIDWNF VKEYCVFATG YPDIGYGMRN PKRAEELGYS KKEMQTVWHQ DHKKLSEDEK RALAPFGYGN ADVMKMKHVK AAGKHWAISF EEFKKSLEPY TLDYVAKVAK GDPDESLESF KAKLQRLKDL YVEKGRKVVS FWTMGMNQHT RGTWDNELSY VVHFLLGKQA LPGSGAFSLT GQPSACGTAR EVGTFAHRLP ADMVVFNPKH RAIAEKIWKL PKGTINPKVG SHIVKIMRDL EDGKIKFAWV HVCNPWQDTA NANHWIKAAR DMDNFIVVSD GYPGISAKVA DLILPSAMIY EKWGAYGNAE RRTQHWRQQV TPVGDAMPDI WQYTEFAKRF KLKDVWKEWK LPDGTVLPNV LDEAKKMGYS EDDTLFDVLF ANDYYRSFKW PDPIGEGFLN TEAEGDKRNV IGADGKPWKG YGFFIQKALW EEYRKFGEGR GHDYAPFDVY HKVRGLRWPV VNGKDTPWRF NVNYDPYAKR EKELGHVKGE FAFYGHALKV IPQGSLTGPD KNKPKIHLPN KAKIFARPYM EPPEVPDNEY DTWLCTGRVL EHWHSGTMTM RVPELYRAVP EALCYMHPED AKKRGVKRGD LVVIESRRGK CKARVETRGR NRPPRGLVFV PWFDERVYIN LVTLDATCPI SKQTDYKKCA VKIYKA //