ID A0A1H0VVP3_9RALS Unreviewed; 831 AA.
AC A0A1H0VVP3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000256|HAMAP-Rule:MF_01630};
DE EC=1.9.6.1 {ECO:0000256|HAMAP-Rule:MF_01630};
GN Name=napA {ECO:0000256|HAMAP-Rule:MF_01630};
GN ORFNames=SAMN04488595_1317 {ECO:0000313|EMBL:SDP82311.1};
OS Ralstonia sp. 25mfcol4.1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1761899 {ECO:0000313|EMBL:SDP82311.1, ECO:0000313|Proteomes:UP000199332};
RN [1] {ECO:0000313|EMBL:SDP82311.1, ECO:0000313|Proteomes:UP000199332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25MFCol4.1 {ECO:0000313|EMBL:SDP82311.1,
RC ECO:0000313|Proteomes:UP000199332};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01630};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000256|HAMAP-Rule:MF_01630};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01630};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01630}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747, ECO:0000256|HAMAP-Rule:MF_01630}.
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DR EMBL; FNJO01000031; SDP82311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0VVP3; -.
DR STRING; 1761899.SAMN04488595_1317; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000199332; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01630};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01630};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01630};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01630};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01630}.
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 85
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 152
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 177
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 181
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 214..221
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 245..249
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 264..266
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 375
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 379
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 485
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 511..512
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 534
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 561
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 721..730
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 797
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 805
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 822
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
SQ SEQUENCE 831 AA; 93538 MW; A75E2E2F9EAE680D CRC64;
MSVTRRDFIK QTAIAATASV AGIPLPGEAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA
VRDNKVVATQ GDPQCEVNKG LNCVKGYFLS KIMYGQDRLT KPLLRMKNGK YDKNGEFAPV
SWDRAFDEME QQFKRVLKEK GPTAVGMFGS GQWTVWEGYA ASKLMKAGFR TNNIDPNARH
CMASAVTGFI RTFGMDEPMG CYDDFENADA FVLWGSNMAE MHPILWTRIT DRRLSHPKTR
VAVLSTFTHR SFDLADLPII FTPQTDLAML NYVANHIIQT NRVNKDFVNK YTVFKEGVTD
IGYGLRPDNP LQKAAKNAGN PTDAKPITFD EFARFVSKYD ANYVSKLSGV PKDKLQQLAE
LYADPNVKIM SLWTMGFNQH TRGTWVNNMV YNVHLLTGKI ATPGNSPFSL TGQPSACGTA
REVGTFSHRL PADMVVTNPK HREEAERIWK LPAGTIPDKV GYHAVLQNRM LKDGKLNAYW
VQVNNNMQAA ANMMQEGLPG YRNPDNFIVV SDVYPTVTAL SADLILPSAM WVEKEGAYGN
AERRTQFWHQ LVDAPGDARS DLWQLMEFSK RFKVEDVWPA DLIAKKPEVR GKTLFDVLYR
NGNVDKFPIK EVNGEYQNAE AKAFGFYVQK GLFEEYASFG RGHGHDLAPF DTYHEVRGLR
WPVVNGKETR WRYREGSDPY VKAGAGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPFWLA
TGRVLEHWHS GSMTRRVPEL YKAFPNAVCF MHPEDARAMG LRRGVEVEVV SRRGRMRTRI
ETRGRDTPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V
//
