ID G4F6Y5_9GAMM Unreviewed; 1265 AA.
AC G4F6Y5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=HAL1_10752 {ECO:0000313|EMBL:EHA15733.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA15733.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA15733.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA15733.1}.
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DR EMBL; AGIB01000045; EHA15733.1; -; Genomic_DNA.
DR RefSeq; WP_008958049.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F6Y5; -.
DR PATRIC; fig|550984.5.peg.2092; -.
DR Proteomes; UP000005692; 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.
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 1265 AA; 142138 MW; 1FC70AFA4BCF0918 CRC64;
MSHFIDRLNF FRKSREPFAN EHGELRSESR EWENSYRARW QHDKVVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPLVRKPLLA
LWREALKANP DPVDAWASIV EDPAKTKQYK RARGMGGFVR GNWDELNELV AASNVYTAKQ
YGPDRIIGFS PIPAMSMVSY AAGSRYLSLI GGVCMSFYDW YCDLPPASPM TWGEQTDVPE
SADWYNSGYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVS ITPDYAEVSK LTDEWLSAKQ
GTDAALAMAM GHVILKEFHL ENPSAYFTDY VRRYTDMPFL VELEAREDGS FAPGRQLRAS
DFDAALGQEN NPEWKTVAWD ETRDQLVVPR GSIGFRWGET GDEVGKWNLE SLDAAGTEIK
PLLSLVNHHD SVARVAFPYF GGIEHEHFEH VKGAGVGAAD DLLFHNLPAK RLKRADGSEM
LAVTVFDLMC ANYGIDRGFV GDGEDDGATS YDQIRPYTPA WQEKITGVSA EQCTRIAREF
ADNAHKTNGR SMIIVGAGMN HWYHMDMNYR GLINMLVMCG CIGQSGGGWA HYVGQEKLRP
QTGWTPLAFG LDWQRPPRHM NSTSFFYSHS SQWRYEKLEI KEILSPLVKV EDYPGSLIDF
NVRAERMGWL PSAPQLDTNP LRLAKKAEAA GMSTADYAVQ QLKSGELRFA AEDPDAPENF
PRNMFIWRSN LLGSSGKGHE YMLKYLLGTR HGIQGKDLGD FGGQKPEEVV WRDEAPEGKL
DLLVTLDFRM STTCLYSDIV LPTATWYEKD DLNTSDMHPF IHPLTAATDP AWESRSDWDI
YKGIAKAFSK VCVGHLGEET DLVTLPMQHD SPGELAQPAV MDWKKGECAP IPGKTMPSLI
EVKRNYPETY ERFTSIGPLL ESIGNGGKGI AWNTDAEVEL LGKLNHRKLD GPHKGRPLID
SAIDAAEMIL TLAPETNGAV AVKAWEALSK ITGRDHTHLA RPKHDEKIRF RDVVAQPRKI
ISSPTWSGLE DEHVSYNAGY TNVHELIPWR TVSGRQQFYQ DHAWMRAFGE SLLVYRPPID
TKAAKGFRLP ADNGFKSKAL NFLTPHQKWG IHSTYSDNLM MLTLNRGGPV VWLSEADAAE
IEIEDNDWIE VYNANGSIAA RAVVSQRVKA GMVMMYHAQE RNVNVPGSEV TGTRGGIHNS
VTRVCPKPTH MIGGYAQLSY SFNYYGTVGS NRDEFVLVRK MKHVDWLDGE GNDSVQKNSA
QEAVK
//
