ID A0A117MKE6_9ACTN Unreviewed; 1238 AA.
AC A0A117MKE6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=ADL12_43060 {ECO:0000313|EMBL:KUL22252.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL22252.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUL22252.1}.
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DR EMBL; LLZG01000399; KUL22252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117MKE6; -.
DR Proteomes; UP000053923; 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 Reference proteome {ECO:0000313|Proteomes:UP000053923}.
FT DOMAIN 65..129
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1238 AA; 137053 MW; 98633381DD5A3421 CRC64;
MVADGSTPGG PVGRDGPAYD GAAADALLRA GRFFTRRDVS ADRRAVFLEG GRQGDVFYRD
RWSHDKVVRS THGVNCTGSC SWKVYVKDGI ITWESQETDY PSVGPDSPEY EPRGCPRGAA
FSWYTYSPTR VRFPYARGVL VEMYREARAR LGDPVLAWAD VVGDPERRRR YQRARGKGGH
VRVTWDEAVE MAAAAHVHTI RRWGPDRIAG FSPIPAMSMV SHAVGSRFIE LIGGCMTSFY
DWYADLPVAS PQVFGDQTDV PESGDWWNAA YLIMWGSNVP VTRTPDAHWM AEARYRGQKV
VVVSPDYADN TKFADQWLHA QPGTDGALAM AMGHVILTEC FVKRRVPMFV DYVRTYTDLP
FLVTLQKHDG AFVPGKFLRA SDLGDTSEGA EWKTVLVDGR TGEPVVPRGT LGERWTESGM
GRWNLDLGDI SPQLTLLGER AEPVEVLLPR FDTTEGSGSV LRRGVPARRI GGRLVTTVFD
LMLAQYGVGR DGLPGNWPTG YDDASQPYTP AWQEEHTSVP AGTVIRVARE MARSSERSGG
RTMIIMGAGI CQWFHGDATY RAILALLMLT GAMGRNGGGW AHYVGQEKCR PFTGWSTLAM
ATDWQRPPRQ MIGTAYWYTH TDQWRYDGYR ADALASPLAR GDLAGLHTAD TIALSARLGW
MPSYPQFDRN PLDLADEAAA AGEAPTEYVA RKLASGELGW ACEDPDAEEN WPRCLTLWRA
NLLGSSGKGN EYFLKHLLGT HSSLRAAQTP PEGRPRDVRW QEEVPEGKLD LLLALDFRMT
SSTLLADIVL PAATWYEKHD LSSTDMHPYV HAFTPAIDPP WETRSDFAAF TVIARRFSEL
AREHLGVRHD VVATALQHDT PGETAQARGT VHDWRGGDVV PVPGRTMPAL TLVTRDYGAV
ADKLTALGPL TEQLGLPVKG LTLHPHEEVE HLARINGVML GGAGDGRPAL DTDAKMAEAV
LALSGTTNGR LAVQGFRTAE RRVGRPLSHL AEGSEERRIT FADTQARPVP VITSPEWSGS
ETGGRRYAAF TTNVEELKPW HTLTGRMHFL LDHDWIHEFG ETLPVYRPPL DMHRLFGEPE
IGPDGEKQVT VRYLTPHSKW SIHSEYQDNL LMLTLSRGGP TVWMSPADAE AIGARDNDWV
EAVNRNGVMV LRAIVSHRMP TGTVYVHHAQ ERVVDVPLTE ASGQRGGIHN SLTRILIKPT
HLIGGYAQLS FAFNYLGPTG NQRDEVTMIR RRSQEVTY
//