ID A0A1N7MU14_9GAMM Unreviewed; 1249 AA.
AC A0A1N7MU14;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SAMN05421760_1076 {ECO:0000313|EMBL:SIS89570.1};
OS Neptunomonas antarctica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Neptunomonas.
OX NCBI_TaxID=619304 {ECO:0000313|EMBL:SIS89570.1, ECO:0000313|Proteomes:UP000185999};
RN [1] {ECO:0000313|Proteomes:UP000185999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22306 {ECO:0000313|Proteomes:UP000185999};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001854};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FTOE01000007; SIS89570.1; -; Genomic_DNA.
DR RefSeq; WP_054340699.1; NZ_LJSI01000027.1.
DR AlphaFoldDB; A0A1N7MU14; -.
DR STRING; 619304.SAMN05421760_1076; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000185999; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1249 AA; 140789 MW; EA9F1BC5888A1757 CRC64;
MSHLLDRLRF LKKKQSTFAN GHGETVKESR EWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLIT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYIYSANRLK YPTVRKRLIK
LWREARTTKD PVDAWASIVE DSAKATSYKS MRGQGGFVRS TWDEVNEIIA AANTYTIKEY
GPDRVIGFSP IPAMSMVSYA AGARYLSLIG GVCLSFYDWY CDLPPASPMT WGEQTDVPES
ADWYNSNYII AWGSNVPQTR TPDAHFFTEV RYKGTKTVSI TPDYAEVAKL CDQWLSPKQG
TDAALAMAFG HVILKEFHVD NPSAYFTEYC RDYTDMPFLV QLDQREDGSY AAGRFIRASD
FDGNMGQDNN PKWKTVAYDE ATDSYVVPNG SIGFRWGEKG KWNIEQKEGL EGRSTTLKMS
LLDSHDEIAS VGFPYFGGVE NEYFTHNTFT DIIHHNLPAK RVKLADGSES LLVTVYDLMM
ANYGIDRGLG GDFVATSYDD NAPYTPAWQE QITGVDRKVA IQIAREFADT ANKTKGRSMI
IVGAGMNHWY HMDMNYRGLM NMLIMCGCVG QSGGGWAHYV GQEKLRPQTG WTPLAFGLDW
QRPPRHMNGT SFFYNHSSQW RYEKLDVTEI LSPLADKSKW TGSLIDYNVR AERMGWLPSA
PQLDCNPLHI TKAAEAAGKT AQEYTVDQLK SGAMNFACED PDNPKNFPRN MFIWRSNLLG
SSGKGHEYLL KYLLGTNHGL MNKDLGEDGI KKPEDVVWHD KGAEGKVDLL VTLDFRMSTT
CLYSDIVLPT ATWYEKDDLN TSDMHPFIHP LSAATDPAWE ARSDWDIYKG IAEKFSEVCV
GHLGVEQDLV TIPMQHDSPG ELAQPLGVMD WKKGECDPVP GISMPNLVVV ERDYPNTYRR
FSSIGPLLES AGNGGKGIGW DTKDEVKFLK ELNWTHTEEG IHKGRAKLDT AIDACEMILS
LAPETNGQVA IKAWAALGEI TGLEHTHLAR PKADEKIRFR DVQAQPRKII SSPTWSGLED
EHVSYNACYT NVHELIPWRT VTGRQQFYQD HEWMRDFGEG FVSYRPPINT KSVAPLMNKK
PNGNPEIALN FITPHQKWGI HSTYSDNLLM LTLSRGGPII WMSEGDATTT GIEDNDWVEV
FNANGAIACR VVVSQRVPDG MTMMYHAQER IVNVPGAETT GTRGGIHNSC TRVCPKPTHM
IGGYAQQSYG FNYYGTVGSN RDEFVIVRKM KNIDWLDGED NDYTQEAAK
//