ID A0A1G9GW75_9PSED Unreviewed; 1251 AA.
AC A0A1G9GW75;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SAMN05216186_11427 {ECO:0000313|EMBL:SDL04916.1};
OS Pseudomonas indica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=137658 {ECO:0000313|EMBL:SDL04916.1, ECO:0000313|Proteomes:UP000198706};
RN [1] {ECO:0000313|EMBL:SDL04916.1, ECO:0000313|Proteomes:UP000198706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21544 {ECO:0000313|EMBL:SDL04916.1,
RC ECO:0000313|Proteomes:UP000198706};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFD01000014; SDL04916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9GW75; -.
DR STRING; 137658.SAMN05216186_11427; -.
DR Proteomes; UP000198706; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198706}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1251 AA; 140508 MW; 04353CFB049479D3 CRC64;
MSHLLDQLRF FKRKQGEFAD GHGETRIESR DWENVYRSRW QYDKIVRSTH GVNCTGSCSW
KIYVKNGLIT WETQQTDYPR TRNDLPNHEP RGCPRGASYS WYIYSANRLK YPKVRKPLLK
LWREARRTLA PVEAWARIVE DKAKAESYKS KRGMGGFIRS SWDEVNEIIA AANVYTVKQY
GPDRVVGFSP IPAMSMVSYA AGSRYLSLIG GVCLSFYDWY CDLPPASPQV WGEQTDVPES
ADWYNSNYII AWGSNVPQTR TPDAHFFTEV RYKGTKTVAI TPDYSEVAKL TDLWLNPKQG
TDAALAQAFA HVIFKEFHLE KPSAYFTDYA KRYTDLPVLV RLVEKDGAFV ADRFLRASDL
ADNLGQANNP EWKTIAVDAS GELVSPLGSI GYRWGEKGKW NIEAKEGGEG REVDLKLSQI
DGGEVAEVAF PYFGGIHHEH FQHAEGEAIQ LRRVPVRTIT LADGSSAKVA TVFDLMAGNL
AIDRGLGGSN VAKSYDDASV PGTPAWQEKI TGVAREKAIQ IAREFADNAD KTHGRSMIIV
GAAMNHWYHM DMNYRGLINM LMLCGCVGQT GGGWAHYVGQ EKLRPQCGWL PLAFGLDWSR
PSRQMNGTSF FYNHSSQWRH EKMSIHEVLS PLADKSQFPE HMLDYNIRAE RAGWLPSAPQ
LNRNPLQITR DAAAAGMSPV DYVVKSLKDG SLRFACEQPD NPDNFPRNMF VWRSNLLGSS
GKGHEYMLKY LLGTKNGVMN EDLGKRGGFK PNEAEWVDEG AIGKLDLVTT LDFRMSSTCV
YSDIVLPTAT WYEKDDMNTS DMHPFIHPLS AAIDPAWEAR SDWEIYKGIA KAFSAMARGH
LGVEQDLVTV PLLHDSPGEL AQPFGGSDWK SAGVDPQPGK NCPNITVVER DYPNTYKKFT
SLGPLLDKLG NGGKGINWNT QHEVEFLGEL NYKVREEGVS EGRPKIESAI DAAEVILSLA
PETNGHVAVK AWAALSEFTG RDHSHLALPK EHEAIRFRDI QAQPRKIISS PTWSGLEDEH
VSYNAGYTNV HEYIPWRTLT GRQQFFQDHP WMQAFGEQMM SYRPPINTRT IDYVKGKKSN
GNPEIVLNWI TPHQKWGIHS TYTDNLIMLT LSRGGPIVWM SEIDAKRAGI EDNDWIECFN
ANGALTARAV VSQRVKEGMV MMYHAQERIV NVPGSETTKT RGGHHNSVTR VVLKPTHMIG
GYAQQAYGFN YYGTVGCNRD EFVVVRKMAK VDWLDGPNGN DLPQPLPTEI E
//
