ID E1VJB5_9GAMM Unreviewed; 1250 AA.
AC E1VJB5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narG {ECO:0000313|EMBL:CBL44907.1};
GN ORFNames=HDN1F_13240 {ECO:0000313|EMBL:CBL44907.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44907.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL44907.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL44907.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VJB5; -.
DR STRING; 83406.HDN1F_13240; -.
DR KEGG; gpb:HDN1F_13240; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_6; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000002677; 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: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 Oxidoreductase {ECO:0000313|EMBL:CBL44907.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1250 AA; 140968 MW; 3529523AF4DC5026 CRC64;
MSQFLDRLQF FKKNAGTFAE GHGVTSNESR AWENAYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASFS WYLYSANRVK YPMVRKRLLK
LWREERRTKN AVDAWQAIVE NPEKARSYKE VRGLGGFVRS SWNEVNEIIA AANVYTAKQY
GPDRILGFSP IPAMSMVSYA SGSRYLSLIG GACLSFYDWY CDLPPSSPQV WGEQTDVPES
ADWYNSNYII AWGSNVPQTR TPDAHFFTEV RYKGTKTVSV TPDYSEVAKL TDLWLNPKQG
TDAALAMAFG HVILKEFHID KPSAYFVDYC RRYTDMPNLV VLEERADGSY EPAHYLRASD
LADGLGEQNN PDWKTLAIDS ATQQIFAPTG SIGFRWGEKG KWNLEQRNAA SAEEVELSLS
LLEKHDKVAG VAFPYFGGVE NEYFTASKHE DILVRNVPTR ELQLANGKTA LVATVYDLLM
ANYSIDRGLG GNWVAKSYDD DIPFTPAWQE KITGVARKRV IQVAREFAEN AHKTKGRSMI
IVGAAMNHWY HMDMNYRGLI NMLMMCGCIG QTGGGWSHYV GQEKLRPQTG WTALAFALDW
NRPPRHQNGT SCFYMHTSQW RHEKLGMEEI LSPLANPEDW KGSMVDYNVR AERMGWLPSA
PQLSRNPLQI TRDAKAAGMD VKDYVVKQLK SGELGFASED PDNPVNFPRN MFVWRSNLLG
SSGKGHEYFL KYLLGTTHGV QSKDLGEEGG VKPMEVKWRD AARGKLDLLV TLDFRMSTTC
LYSDIVLPTA TWYEKNDLNT SDMHPFIHPL TAATDPAWEA RSDWEIYKGI AKKFSETAEG
HLGVEQDLVT VPTLHDTPGE LAQAFNPKDW KKGEIDPIPG KTMPSMIVVE RDYVNTYKKF
TSLGPLMEKL GNGGKGISWN TQKEVDFLRE LNYVVTEEGV SKGQPRIDSD IDAAEVILSL
APETNGQVAV KAWEALGQAT GLDHTHLALP KEEEKIRFRD VVAQPRKIIS SPTWSGLEDE
HVSYNAGYTN VHELIPWRTL TGRQQFYLDH QWMRAFGEGF VSYRPPVNLK AVKPMLGKKP
NGQKEIVANW ITPHQKWGIH STYTDNLIML TLSRGGPIVW VGEVDAKKAG IVDNDWIEVF
NANGAIAARA VVSQRVPEGM VMMYHAQEKT VNTPGSEITG HRGGIHNSVT RAVLKPTHMI
GGYAQFSYGF NYYGTVGSNR DEFVIIRKMN KVDWLDGSRS DELPRPLESL
//
