ID NAPA_CAMFF Reviewed; 925 AA. AC A0RQ36; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 108. 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=CFF8240_1161; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=82-40; RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000487; ABK82549.1; -; Genomic_DNA. DR RefSeq; WP_011732100.1; NC_008599.1. DR AlphaFoldDB; A0RQ36; -. DR SMR; A0RQ36; -. DR GeneID; 61064986; -. DR KEGG; cff:CFF8240_1161; -. DR eggNOG; COG0243; Bacteria. DR HOGENOM; CLU_000422_13_4_7; -. DR Proteomes; UP000000760; 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 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..30 FT /note="Tat-type signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT CHAIN 31..925 FT /note="Periplasmic nitrate reductase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT /id="PRO_1000069712" FT DOMAIN 36..92 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" 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 50 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 78 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 80 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 148 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 173 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 210..217 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 418 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 528 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 553..554 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 576 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 603 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 815..824 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 891 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 899 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 916 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" SQ SEQUENCE 925 AA; 104255 MW; 6421C720F2CE60BB CRC64; MDRREFIKSS AAAAACSAAG IAVPSSLSAA ENQDGWRWDK SACRFCGTGC GIMVATKNGK IVAVKGDPLA PVNRGLNCIK GYFNAKIMYG EDRITKPLLR VNANGEFDKK GKFQEVSWKR AFDEMEKQFR KTYAELGPTG IGVFGSGQYT IQEGYAISKL IKGGFRSHNI DPNARHCMAS AVVGFMQTFG IDEPAGCYDD IELTDTIVTW GANMAEMHPI LWSRVSDRKL QNSDKVKVVN LSTYSTRTSN IADIEIIFTP HTDLAIWNYI AREIVYNHPE AIDEEFVKAN CVFTTGPVDI GYGMRANIKH PKYLPSELDT AAKEKSTVLS ENEGVTLAYL GMKAGDTLEN KSTGAPDKHW IIQYEDFKKA LAPYTLDFVA KLAKGDPNED LEEFKKKLKA LADLYIEKNR KVVSFWTMGM NQHTRGVWVN EQSYMVHFLL GKQAKPGSGA FSLTGQPSAC GTAREVGTFS HRLPADMVVA NPKHREITEK IWKIPAGTIN PKPGAPYMKI MRDLEDGKVK FVWVHVNNPW QNSANANHWI KAAREMDNFI VVSDPYPGIS AKVGDLILPT AMIYEKWGAY GNAERRTQHW RQQVLPVGDA MSDTWQYMEF AKRFKLKDFW GEVKVDGKLT LPNVLDKAVA MGYNPENTLF EVLFANKSAM KFSSDDKIMA GYDNTEVFGD SRNVVGSDGN VFKGYGFFVQ KYLWEEYREF GLGHGHDLAD FDTYHKVRGL RWPVVDGKET LWRFNTKYDV YAKKDNPNGD FSFYGNKNGA LVTGDLAKAT SKEKEALKSR AKIFFRPYMD PPEMPSKDYP LWLCTGRVLE HWHSGTMTMR VPELYRAVPE ALCFMNEIDG NKFGIKQNDI IWVESRRGKV KARVDFRGRN KPAEGLIYVP WFDENVFINK VCLDATDPLS KQTDFKKCAV KIYKA //