ID NAPA2_PHOPR Reviewed; 830 AA. AC Q6LQJ3; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 27-MAR-2024, entry version 110. DE RecName: Full=Periplasmic nitrate reductase 2 {ECO:0000255|HAMAP-Rule:MF_01630}; DE EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630}; DE Flags: Precursor; GN Name=napA2 {ECO:0000255|HAMAP-Rule:MF_01630}; GN OrderedLocusNames=PBPRA2030; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=298386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). 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 -!- SEQUENCE CAUTION: CC Sequence=CAG20433.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CR378669; CAG20433.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041394329.1; NC_006370.1. DR AlphaFoldDB; Q6LQJ3; -. DR SMR; Q6LQJ3; -. DR STRING; 298386.PBPRA2030; -. DR KEGG; ppr:PBPRA2030; -. DR eggNOG; COG0243; Bacteria. DR HOGENOM; CLU_000422_13_4_6; -. DR Proteomes; UP000000593; Chromosome 1. 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..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT CHAIN 32..830 FT /note="Periplasmic nitrate reductase 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT /id="PRO_0000045994" 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 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 374 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 378 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 484 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 510..511 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 533 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 560 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 720..729 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 796 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 804 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" FT BINDING 821 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630" SQ SEQUENCE 830 AA; 92868 MW; 80887A70897D1EDD CRC64; MKVSRRKFIK AQAVASAAAA AGISIPISAS NVVTDSSLTK ITWEKAPCRF CGTGCSVNVG TKEGKVVATH GDIKSPVNRG LNCVKGYFLS KIMYGKDRLT QPLLRMTDGK FDKNGEFSPI SWDQAFDIMA EKWKKTLKEK GPEAIGMFGS GQWTIYDGYA ASKLMKAGFR SNNLEPNARH CMASAVVGFI RTFGIDEPMG CYDDIEAADA FVLWGSNMVE MHPILWTRVT DRRLSVPGVK VSVLSTFEHR SFELADIPII FTPQSDLAIL NFIANYIITN DKVNKDFTSK HVNFRRGTTD IGYGLRPEHP LQQAAKNPDS GDSTPMTFEE FKAFVSEYTV EKASEISGVK PDKLIELAEL YANPETKVVS FWTMGFNQHT RGVWCNNLVY NIHLLTGKIS TPGNSPFSLT GQPSACGTAR EVGTFAHRLP ADLVVTNPEH RKIAEKIWKL PDGTIPGKVG AHAVLQSRML KDGKINAYWI QVNNNLQAGA NINEETLPGY RNPDNFIVVS EAYPTVTSQA ADLVLPTAMW VEKEGGFGNA ERRTQLWHQM VEAPGESKPD LWQLMEFSKR FKTDEVWPKE LLDSNPDYKG KTLFDVLFIN GNVNKYPLDD LAEGTLNDES NYYGFYVHKG LFEEYAEFGR GHGHDLAPFD MYHETRGLRW PVVDGKETLW RYREGSDPYV KEGAGFEFYG KPDGKAIIFA LPYEPAAESP DEEYDMWLST GRVIEHWHSG SMTQRVPELY KAYPDAQVFM HPDDAKSRGL RRGDAVKVMS RRGEIITRVE TRGRNKPPIG LVFVPWFDAS QLINKVTLDA TDPLSKQTDF KKCAVKIVKA //