ID NAPA_SACD2 Reviewed; 831 AA. AC Q21PN1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 107. 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=Sde_0084; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Saccharophagus. OX NCBI_TaxID=203122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024; RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087; RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., RA Richardson P.M., Borovok I., Hutcheson S.; RT "Complete genome sequence of the complex carbohydrate-degrading marine RT bacterium, Saccharophagus degradans strain 2-40 T."; RL PLoS Genet. 4:E1000087-E1000087(2008). 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; CP000282; ABD79348.1; -; Genomic_DNA. DR RefSeq; WP_011466572.1; NC_007912.1. DR AlphaFoldDB; Q21PN1; -. DR SMR; Q21PN1; -. DR STRING; 203122.Sde_0084; -. DR KEGG; sde:Sde_0084; -. DR eggNOG; COG0243; Bacteria. DR HOGENOM; CLU_000422_13_4_6; -. DR OrthoDB; 9816402at2; -. DR Proteomes; UP000001947; Chromosome. 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; Reference proteome; KW Signal; Transport. FT SIGNAL 1..29 FT /note="Tat-type signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT CHAIN 30..831 FT /note="Periplasmic nitrate reductase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT /id="PRO_0000256076" FT DOMAIN 41..97 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 48 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 51 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 55 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 83 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 85 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 245..249 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 264..266 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 375 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 379 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 485 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 511..512 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 561 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 721..730 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 797 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 805 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 822 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" SQ SEQUENCE 831 AA; 93164 MW; 8B6EA1C70B7AF770 CRC64; MTVTRRDFVR HQALATAAAA AGVAVPAAAT NIVTTAADNK LVWSKAPCRF CGTGCSVNVA TKEGRVVATH GDIKSPVNRG LNCVKGYFLS KVMYGEDRLT QPLLRKKNGV YAKDGEFEPV TWEEAFTIMA EKFKKTLKEK GPEGIGMFGS GQWTVWEGYA ASKLMKAGFR SNNIDPNARH CMASAVGGFM RTFGIDEPMG CYDDFEHADA FVLWGSNMAE MHPILWTRIA DRRLSYPHVQ VAVMSTYEHR SFDLADLGVV FTPQSDLAIA NFIANYIIQN KKVNWDFVKK HTNFRVGTTD IGYGLRPEHP LQKAAKNADS AGASEPIDFE TYAKFVADYT VEKASEISGV SEDKLIKLAK LYADPNIKVM SLWTMGVNQH TRGVWMNNLI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA REVGTFSHRL PADMVVTNPK HRAYAEKIWK LPEGSIPEKV GAHAVLQSRK LKDGEINAYW VQVNNNVQAG PNINEEVLPG YRNPQNFIVV SDAYPTVTAQ AADLILPSAM WVEKEGAYGN AERRTQFWHQ LVNAPGDARS DLWQLVEFSK YFKVEEVWPA DLIAKMPEAK GKTLFDILYK NGKVNKFPLA QVSKDYENKE ADAFGFYIQK GLFEEYAEFG RGHGHDLADF DRYHEERGLR WPVVNGEETL WRYREGSDPY VEKGKGVQFY GKPDGKAIIF ALPYEPPAES PNKEYPFWLC TGRVIEHWHS GSMTQRVPEL YKAFPDAVCF MHPEDARSAG LRRGDKVKLQ SIRGHIITRI ETRGRNKPPK GLVFVPWFDA RQLINKVTLD ATDPISKQTD FKKCAVKVER V //