ID W5TII7_9NOCA Unreviewed; 1231 AA.
AC W5TII7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narG2 {ECO:0000313|EMBL:AHH18798.1};
GN ORFNames=NONO_c40140 {ECO:0000313|EMBL:AHH18798.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH18798.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH18798.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH18798.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH18798.1; -; Genomic_DNA.
DR RefSeq; WP_025350219.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TII7; -.
DR STRING; 1415166.NONO_c40140; -.
DR KEGG; nno:NONO_c40140; -.
DR PATRIC; fig|1415166.3.peg.4119; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000019150; 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: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 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 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 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};
KW Oxidoreductase {ECO:0000313|EMBL:AHH18798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT DOMAIN 58..122
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1231 AA; 136127 MW; 0E0805D9EF11F6AA CRC64;
MARTARGDNG SLDSELTAAL IRSRRFFTRA TFAADLRTEY VRGGRQADEF YRDRWAHDKV
VRSTHGVNCT GSCSWKVYVK DGIITWETQA TDYPSVGPDR PEYEPRGCPR GAAFSWYTYS
PTRIRYPYIR GVLLEMYREA KARTGDPVTA WESIVSDPEA ARRYKSARGR GGLVRAGWEE
AVELVAAAHV HTIKTYGPDR VAGFSPIPAM SMVSFAAGSR FISLIGGSML SFYDFYADLP
VASPQVFGDQ TDVPESGDWW DAGYLIMWGS NVPVTRTPDA HWMTEARYRG QKVIAVAPDY
ADNVKFADEW LAPRPGTDAA LGMAMGHVIL REFFVDRQVP YFQDYVRRFT DLPFLVRLEE
TGGVYRPGKF LTAADLEQFA DAEHAEFKTV LLGDDGEPVL PNGSLGFRYG DDGAGRWNLE
LDGVRPALSV GGDDAVLVEL PRFDTADGAA TMLRRGVPVR TIGGHRVTTV FDLMLARYGV
RRDGLPGDWP AGYDDATRPG TPGWQETITG VPAAVAARIG REFAANAEET QGRSMIILGA
GTNHWFHSDT MYRTFLALTT LTGCQGRNGG GWAHYVGQEK CRPVTGWATV ANALDWTRPP
RQMNQTVYWY LHTDQFRYDP FSAADLTTTT GAGALSGRST ADLIAQTARM GWTPSYPTFD
RNPLDLADEA EQAGRTPAEH VVTQLQSGEL RFACEDPDDP ANFPRVLSIW RSNLLGSSAK
GNEYFLRHLL GADSSLRAEE APPRSRPREV VWHDQAPTGK LDLLLTLDFR MTSTTMYSDV
VLPAATWYEK YDLSSTDMHP FVHSFSPAIA PPWQTRTDWD AFMGIAAEFS RLARRHLGVR
TDIVATALLH DTPDELANPH GVVKDWKSGD CEPIPGLTMP RLTAVERDYG AVRAKMGALG
PVVDRLGAAT KGVTFDVTAE VADLAARNGI VHGGPAAGRP SLERDIDACE AILALSGTTN
GRLAVQGFRT LEQRTGTRLA DLAAEHEGKR ITFADTQIAP VPVITSPEWS GSESGGRRYS
PFTVNIERAK PWHTLTGRQH FYLDHDWMAE VGEQLPVFRP PLDMSALFAE PRPGQHSGDG
LALRYLTPHS KWSIHSEYQD NLLMLSLSRG GPTLWMSDRD AAKLGVRDNE WIEAVNRNGV
VVARAVVTHR MPEGTVYMNH AQDRLIDVPL AETSGKRGGI HNSLTRLLIK PTHLIGGYAQ
LSFAFNYLGP TGNQRDEVTV IRRRSQEVNY R
//
