ID A0A3N1J4T8_9ENTR Unreviewed; 1248 AA.
AC A0A3N1J4T8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=EDF81_0952 {ECO:0000313|EMBL:ROP62459.1};
OS Enterobacter sp. BIGb0383.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=2485118 {ECO:0000313|EMBL:ROP62459.1, ECO:0000313|Proteomes:UP000280899};
RN [1] {ECO:0000313|EMBL:ROP62459.1, ECO:0000313|Proteomes:UP000280899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0383 {ECO:0000313|EMBL:ROP62459.1,
RC ECO:0000313|Proteomes:UP000280899};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROP62459.1}.
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DR EMBL; RJKQ01000001; ROP62459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1J4T8; -.
DR Proteomes; UP000280899; 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: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; 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:SF8; RESPIRATORY NITRATE REDUCTASE 1 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000280899}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1248 AA; 140374 MW; DDEA6C9C2F1D8DCF CRC64;
MSKFLDRFRY FKQKGETFAD GHGQLLETNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDMPNHEP RGCPRGASYS WYLYSANRLK YPLMRKRLIK
LWREAKAQHS DPVLAWASIM EDSEKTKSYK QARGRGGFVR SSWQEVNELI AASNVYTVKT
YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPM TWGEQTDVPE
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA ITPDYAEIAK LCDLWLAPKQ
GTDSAMALAM GHVMLKEFHI DNPSPYFTDY VRRYTDMPML VMLEEREGFY AAGRMLRASD
LVDGLGQENN PEWKTVAIDD NSGAPMAPNG SIGFRWGEKG KWNLEQRDGT SGDEAGLRLS
LLGSHDEVAN VGFPYFGADT TEHFTPVKLD NVLLHKLPVK RMTLADGSSA LVATVYDLTM
ANYGIDRGLQ DENCATSYSE IKAYTPGWAE QVTGVSQAQI VRIAREFAAN ADKTHGRSMI
IVGAGLNHWY HLDMNYRGLI NMLIFCGCIG QSGGGWAHYV GQEKLRPQTG WQPLAFGLDW
QRPARHMNST SYFYNHSSQW RYETVTAQEF LSPMADKSRY SGHLLDFNVR AERMGWLPSA
PQLGTNPLYI AAEAEKAGMS PVDYTVKSLK DGSIRFAAEQ PENGKNHPRN LFIWRSNLLG
SSGKGHEYML KYLLGTEHGI QGKDLGQQGA MKPEEVEWHD NGLDGKLDLV VTLDFRLSST
CLYSDIVLPT ATWYEKDDMN TSDMHPFIHP LSAAVDPAWE SKSDWEIYKG IAKKFSEVCV
GHLGKETDIV TLPIQHDSAA ELAQPLDVKD WKKGECDLIP GKTAPHIIPV ERDYPATYER
FTSIGPLMEK IGNGGKGIAW NTQSEMDLLR KLNYTKADGP AKGQPMLNTA IDAAEMILTL
APETNGHVAV KAWAALSEFT GRDHTHLAVN KEEEKIRFRD IQAQPRKIIS SPTWSGLEDE
HVSYNACYTN VHELIPWRTL SGRQQLYQDH QWMRDFGESL LVYRPPIDTR SVKEVMGVKS
NGYPEKALNF LTPHQKWGIH STYSDNLLML TLGRGGPVVW ISDVDAKEIG IEDNDWIEVF
NSNGALTARA VVSQRVPSGM TMMYHAQERI VNLPGSEITG QRGGIHNSVT RITPKPTHMI
GGYAHLAYGF NYYGTVGSNR DEFVVVRKMK NINWLDGEGN DQVQESAK
//
