ID A0A0X8G5N9_9FLAO Unreviewed; 775 AA.
AC A0A0X8G5N9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=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=Lupro_04255 {ECO:0000313|EMBL:AMC10504.1};
OS Lutibacter profundi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC10504.1, ECO:0000313|Proteomes:UP000059672};
RN [1] {ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT "Complete genome sequence of Lutibacter profundus strain LP1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC10504.1, ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|EMBL:AMC10504.1,
RC ECO:0000313|Proteomes:UP000059672};
RX PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT on the Arctic Mid-Ocean Ridge and emended description of the genus
RT Lutibacter.";
RL Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
CC -!- FUNCTION: Catalytic subunit of the nitrate reductase complex NapAB.
CC Receives electrons from NapB and catalyzes the reduction of nitrate to
CC 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 nitrate reductase NapAB complex composed of
CC NapA and NapB. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|HAMAP-Rule:MF_01630}.
CC Note=Membrane-associated. {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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01630}.
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DR EMBL; CP013355; AMC10504.1; -; Genomic_DNA.
DR RefSeq; WP_068206596.1; NZ_CP013355.1.
DR AlphaFoldDB; A0A0X8G5N9; -.
DR STRING; 1622118.Lupro_04255; -.
DR KEGG; lut:Lupro_04255; -.
DR PATRIC; fig|1622118.3.peg.896; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000059672; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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 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; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000059672};
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 47..103
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 91
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 151
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 176
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 180
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 262..264
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 364
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 368
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 473
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 498..499
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 521
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 548
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 665..674
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 741
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 749
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 766
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
SQ SEQUENCE 775 AA; 86875 MW; 30BE1244A2DF451C CRC64;
MIQESIDRRS FIKKMAAVAA MTTAATMFPG IIFASEQIEN LPSGGNLEWK KGPCRFCGVG
CGILVGVEKG KAVAVKGDPN SSVNKGLLCV KGYHQTMCIQ AKDRLTHALV KKNGSYIKIP
IDEALDIVAN KMKETIEKHG KDAVAMYTSG QSTIPEGYVA SKLMKGAIGT NNLDCNARLC
MASAVAGFLT TFGADEPMGC YEDINHADYF ITWGNNMAEM HPVLFSRMLE QKNNRGAKII
DFATRTTRSS MASNKSILFE PQTDLAVANA ICYEIINNGW VNKLFVEKHC NFSKGSTNIG
YGIEDNFKFK DKPVGINFEE FKKFLEDYTP EKVAKYSKVS VKDIKYLANI YGDPNKKVVS
YWCMGMNQHT RGTWINNLVY NIHLLTGKIS QPGNGPFSLT GQPSACGTAR EVGTFTHKLP
KGVVMNEKHR RLAAKIWKVP YENIPSKPTY HATEMFRAVD RGDIKFIWTQ VTNPLVSLPK
TSRYRSGMEK NSCFVVVSDV FPTPTSDVAD VILPASWHIE KSGLYGNSER RTQHWDKMIE
GPGDTTPDAW MTIEVAKRMG YGDLFPYSEE NHVEEIYNEY IQFHEGAKHG MAPLEVLKKE
SGAIWPYVNG KSTQWRFNAV YDPACSNGED FHFYGKPDGK AVIWQRPYEP AAEYPDQEFP
FWLNTGRVIE HWHTGSMTRR IPVLHKAMPH AYVEFHPEDA KTLGIRNGEK VKVTSRRGSC
TLPASINQRG LPTRGQVFVP FFDESMLIND VTLDAFCPIS KEPDYKKCAV KVERV
//
