ID A4G5N2_HERAR Unreviewed; 1242 AA.
AC A4G5N2;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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:CAL61819.1};
GN OrderedLocusNames=HEAR1662 {ECO:0000313|EMBL:CAL61819.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61819.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL61819.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL61819.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G5N2; -.
DR STRING; 204773.HEAR1662; -.
DR KEGG; har:HEAR1662; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_4; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000006697; 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; 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:CAL61819.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1242 AA; 138936 MW; E09BF460FB11D39D CRC64;
MSHFLDRLKF FNKPQESFSN GHGTVVDEDR SWEKSYRQRW QHDKIVRSTH GVNCTGSCSW
KVYVKNGLIT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYVYSAQRVK YPMVRGRLME
MWRAARVLMS PVAAWEYISQ NPERAQQYKS VRGQGGFVRA KWDEVNEIIA AANAYTVKKF
GPDRIIGFSP IPAMSMVSYA AGTRYLSLIG GVALSFYDWY CDLPPASPQV WGEQTDVPES
ADWYNSTYLM VWGSNVPMTR TPDAHFYTEV RYKGTKTVAV SSDFGEMAKF GDIWLAPKQG
TDAALAMAMG HVILKEYHAS GKSAYFRSYA KQYTDFPMLV LLKEKNGTLV PDYFLRASHL
ANNLDETNNP DWKTLVIDET SGDISAPAGS IGFRWGEFGK WNLEQKAGTS GKPIDPLLSL
IDCSDEVTAV GFPYFGGKDA EDMLLRNIPV KKIQLADGSI ATVATVYDLT MANYGVDRGL
GGGNVAKDLD DDVPYTPAWQ VKHTGVKAAD VITVAREFAD NADKTKGKSM VIVGAALNHW
YHMDMTYRGI INMLMMCGCV GQSGGGWAHY VGQEKLRPQT GWTPLAFALD WNRPMRQMNG
TSFFYAHTSQ WRHEKLHTEE IQSPSADSNV AQMSLLDYNA KAERMGWLPS APQLETNPLE
VTRAAEAAGQ DVQQYAVDQI KAGKLNFSCD DPDNPANFPR NMFVWRSNIL GSSGKGHEYF
LKYLLGTQNA LMSDEDSCIK PRDVKVRPAA EGKLDLLVVL DFRMSTTCLY GDIVLPTATW
YEKDDLNTSD MHPFIHPLSE AVQPLWQSKT DWEIYKGIAE KFSEIGGEYL GTQKDLVLTP
LMHDTPGELG QPFDPKDWRA GECEPIPGKT MPNFTVVERN YRDIYKKFTS VGPLLESLGN
GGKGIGWKTG HEVEVLRGIN RTVLEEGVSK GQPRLDTAID AAEMILSLAP ETNGHVAVKA
WDALSKMTGR DHTHLALPRE HDTIRFRDVQ AQPRKIISSP TWSGLESEEV SYNAGYTNVH
EMIPWRTLTG RQQFYQDHLW MRDFGEGLCV YKPAINTKTT AAMLGAQPNG NKEIALNFIT
PHQKWGIHST YSDNLRMLTL SRGGPHVWLS ETDAKNAGIV DNDWIEVFNV NGTLTARAVV
SQRVPAGMTL MYHAQEKIIN VPGAEMSGKR GGIHNSVTRA VTKPTHMIGG YAQLSYGFNY
YGTVGSNRDE FVLVRKMKKV DWLEGPLEEH GQEQGQKQGS AA
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