ID NAPA_SERP5 Reviewed; 828 AA. AC A8GHJ4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=Spro_3486; OS Serratia proteamaculans (strain 568). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Serratia proteamaculans 568."; RL Submitted (SEP-2007) 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; CP000826; ABV42584.1; -; Genomic_DNA. DR AlphaFoldDB; A8GHJ4; -. DR SMR; A8GHJ4; -. DR STRING; 399741.Spro_3486; -. DR KEGG; spe:Spro_3486; -. DR eggNOG; COG0243; Bacteria. DR HOGENOM; CLU_000422_13_4_6; -. DR OrthoDB; 9816402at2; -. 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 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; Signal; Transport. FT SIGNAL 1..33 FT /note="Tat-type signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT CHAIN 34..828 FT /note="Periplasmic nitrate reductase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT /id="PRO_5000279603" 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; 92599 MW; 46B8C60CD80539E9 CRC64; MKLSRRDFMK ANAAVAAAAA AGLTIPTVVQ AAAGSADSIK WDKAPCRFCG TGCGVLVGTQ NGRIVASQGD PEAAVNRGLS CIKGYFLPKI MYGKDRLNQP LLRMKDGQYH KEGEFTPVSW QQAFDIMAEK FKQALKEKGP EAVGMFGSGQ WTVWEGYAAA KLLKAGLRSN NLDPNARHCM ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITDR RLSNEKVNVS VLSTFEHRSF ELADNGMVFT PQTDLAIMNY IANYIIQNNA VDQDFLNRHV NFRRGATDIG YGLRPTDPLE KAAKNPGSDA SDPMSFEEYK AFVADYTLEK TAKMSGVPED QLEALAKLYA DPNIKVVSYW TMGFNQHTRG VWANNLCYNL HLLTGKISKP GCGPFSLTGQ PSACGTAREV GTFAHRLPAD MVVTNEKHRQ TAEQKWQLPA GTIPAKVGLH AVAQDRALKD GTLNAYWVMC NNNMQAGPNI NEDRMPGWRD ARNFVVVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER RTQFWRQQVK APGEAKSDLW QLVEFSKRFT VEEVWPAELL AQKPEYRGKT LYDVLFANGE VNKYPLTEIP ADQLNDEARD FGFYLQKGLF EEYAGFGRGH GHDLAPFDSY HQARGLRWPV VEGKETLWRY REGTDPYVKA GEEVRFYGKP DGKAVIFALP FEPAAESPDK EYDLWLSTGR VLEHWHTGSM TRRVPELHRA FPQAVVFIHP LDAKSRNLRR GEKVRVLSRR GELISTVETR GRNRPPRGLV YMPFFDAAQL VNNLTLDATD PLSKEVDFKK CAVKLEKV //