ID A0A1B3LPQ0_9PROT Unreviewed; 1264 AA.
AC A0A1B3LPQ0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Nitrate reductase, alpha subunit {ECO:0000313|EMBL:AOF82827.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AOF82827.1};
GN ORFNames=BSY238_1272 {ECO:0000313|EMBL:AOF82827.1};
OS Methyloversatilis sp. RAC08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF82827.1, ECO:0000313|Proteomes:UP000094168};
RN [1] {ECO:0000313|Proteomes:UP000094168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; CP016448; AOF82827.1; -; Genomic_DNA.
DR RefSeq; WP_069038382.1; NZ_CP016448.1.
DR AlphaFoldDB; A0A1B3LPQ0; -.
DR STRING; 1842540.BSY238_1272; -.
DR KEGG; metr:BSY238_1272; -.
DR PATRIC; fig|1842540.3.peg.1285; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000094168; Chromosome.
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:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
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; 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; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AOF82827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094168}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1264 AA; 141828 MW; CF7EC7ABA3204DE8 CRC64;
MSHFLDRLSH FSNPKEAFSG DHGITTGEDR SWEDAYRNRW AHDKIVRSTH GVNCTGSCSW
KIYVKGGIVT WETQQTDYPR TRWDMPNHEP RGCARGASYS WYLYSANRVK YPMVRGRLLK
SWREARLAHG PVEAWASIVE NDAKRRDYQQ VRGLGGFVRS SWDEVNEIVA AANVYTIKKH
GPDRVIGFSP IPAMSMISYA AGSRYLSLIG GVCMSFYDWY CDLPPSSPQI WGEQTDVPES
ADWYNSTYII AWGSNVPQTR TPDAHFFTEV RYKGAKTVAV TPDYSEVAKL SDIWMKPKQG
TDAAVAMAMG HVILKEFYFP DSGERSAYFD DYVRRYTDMP MLVMLKEHKL PNGDMILVPD
RYVRASDFNG KLGQANNPEW KTVAFDDSGK VVLPNGAIGF RWGADGRADE GQWNLEAKEA
RHGANVKLKL SLLEGEAPSS ETARVGFPYF GGIVSEHFPN NAQTDVLVRT VPVQRIALGK
AGEKRDALVA TVFDLQVANY GIARGLPGEL AAKDFNDDTP YTPAWQECIT GTPREQLITV
ARQFAENAHK TKGKSMVIIG AAMNHWYHSD MNYRGVINML MMCGCIGQSG GGWAHYVGQE
KLRPQTGWTA LAFALDWIRP PRQMNSTSFF YAHTDQWRYE KLGMEEVISP LADKKMYGGS
MIDYNVRAER MGWLPSAPQL QTNPLQVVRD AASAGMDPKD YAVRGLKDGS LKMSCTDPDH
PDNWPRNMFV WRSNILGSSG KGHEYFLKHL LGTSNGVQGK DLGKEEAKPT EVVWHDTAPE
GKLDLLVTLD FRMSTTCLYS DIVLPTATWY EKNDLNTSDM HPFIHPLSTA VDPAWQSRSD
WDIYKGFARK FSEVCVGHLG VERELVLSPL MHDSPSELAQ PFDVKDWKRG ECELIPGKTA
PNLVVVERDY PNVYKRFTAL GPLMNKVGNG GKGISWNTQT EVKQLGELNG LVTAEGVTCG
MPKIDTDIDA CEVVLQLAPE TNGHVAVKAW QALGKQTGLK HEHLALYRED EKIRFRDIQA
QPRKIISSPT WSGIESETVS YNAGYTNVHE LIPWRTLTGR QQFYMDHPWM IAFGEGFTSY
RPPVDLKTTA GIHNIKPNGN PEIALNFITP HQKWGIHSTY TDNLLMLTLS RGGPCVWMSE
DDAKRADIID NDWIELFNIN GAIAARAVVS QRVKPGMVMM YHAQEKIVNT PGSEITGARG
GIHNSVTRIV LKPTHMIGGY AQFSYGFNYY GTIGTNRDEF VVVRKMKRID WLDNEKSAAD
TSHA
//