ID A0A5D0NMT2_9ACTN Unreviewed; 1242 AA.
AC A0A5D0NMT2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=FXF69_18530 {ECO:0000313|EMBL:TYB45434.1};
OS Actinomadura chibensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=392828 {ECO:0000313|EMBL:TYB45434.1, ECO:0000313|Proteomes:UP000323380};
RN [1] {ECO:0000313|EMBL:TYB45434.1, ECO:0000313|Proteomes:UP000323380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14158 {ECO:0000313|EMBL:TYB45434.1,
RC ECO:0000313|Proteomes:UP000323380};
RA Songsumanus A., Kuncharoen N., Kudo T., Yuki M., Igarashi Y.,
RA Tanasupawat S.;
RT "Actinomadura sp. nov. CYP1-5 isolated from mountain soil.";
RL Submitted (AUG-2019) 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}.
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:TYB45434.1}.
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DR EMBL; VSFG01000003; TYB45434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D0NMT2; -.
DR STRING; 1220554.GCA_001552135_05779; -.
DR Proteomes; UP000323380; 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: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:TYB45434.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000323380}.
FT DOMAIN 57..121
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 859..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 136375 MW; 3158E7BB7A06190B CRC64;
MRGKRGRADR AAAEVEARLL EAGRFLRNAP TTSDLRAVYR DDQGVNDAPY RERWAHDRVV
RSTHGVNCTG SCSWKVYVKD GLITWETQQT DYPSVGPDRP EYEPRGCPRG ASFSWYTYSP
TRVRYPHARG VLVEMYREAR ARLGDPVAAW AEITGDPERR VRYQSARGHG GLVRIGWDEA
LEIAAAAHLH TIETYGPDRV AGFSPIPAMS MASHAVGARF MSLIGAPMLS FYDWYADLPV
ASPQVFGDQT DVPESADWWD AGYLLLWGSN VPVTRTPDAH WMTEARYRGQ KVVVVSPDYS
DATKFADEWL HPHPGTDGSL AMAMGHVILR EHFVDRSTPY FEDYVKRFTD LPFLVELRDG
GTGGDGGTGG LVPGKFVTAA DLGLETAAAP DDRRWQPLLI DGRTGEPVAP GGTLADRWAP
EGEGRWNLDL AGVEPALTLL GSGEHAEIAM PRFDLPEGAG AVRRGVPVRR FGDRTVTTVF
DLMLAQYGVA RPGVPGDWPD GYDDPDSPCT PAWQEQITGV PAARAAAIAR EFADNAERTR
GRSMIVMGAG TNHWYHSDTI YRSFLSLLLL TGCQGVNGGG WAHYVGQEKV RPLAGWQQLS
TAADWVRPSR QMAGTPYWYL HTDQWRYESY SADALSAATG PGLFAGRHPA DLVAQSARLG
WMPSYPTFAR NPIDLGRTIR EAGRDPSEWV AEEVEAGRLG FAVEDPDAPE NWPRVLTVWR
ANLIGSSAKG NEYFLRHLLG ADDSATAGEA PSGRRPRDVA WRDEAPRGKL DLLLALDFRM
TSTTLFADLV LPAATWYEKH DLSSTDMHPY VHAFSPAINP PWQARTDFEI FHGLARRLGE
LARGRLEVVH DLVATALQHD SPGETAQPGG TVPDWRDGRP ARPGRNLPQV AVVERDYTAV
ADRLAALGPL TRDKGLTTKG VTVGAGPEDA WLAARAGTVT RGPAEGRPLL DTDVKLCEAI
LALSGTTNGR IAAEGFARLA ERCGPKSGLD ELGASVAERR VVFSDTQDRP VQVGASFEWS
GKEAPDRRYS PFTVNTEHAK PWHTLTGRQH FFLDHDWMIE FGEQLPVYRP PLDLAALGES
GPARHDAGDG REVTVRYVTP HSKWSIHSEY QENLLMQTLA RGGPVIWMSV QDAAAVGVAD
NDWIEAVNAN GVVVARAIVS HRMPPGTVFM YHVQERLVNV PRAQAGGRRG GVHNALTKLL
IKPTHLIGGY AQQSFAPNYH GPTGNQRDAV TVIRRRSQEV TY
//
