ID A0A0Q8Y6H5_9MICO Unreviewed; 1258 AA.
AC A0A0Q8Y6H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=ASE25_09585 {ECO:0000313|EMBL:KRC89786.1};
OS Terrabacter sp. Root85.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Terrabacter.
OX NCBI_TaxID=1736603 {ECO:0000313|EMBL:KRC89786.1, ECO:0000313|Proteomes:UP000051752};
RN [1] {ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|Proteomes:UP000051752};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC89786.1, ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|EMBL:KRC89786.1,
RC ECO:0000313|Proteomes:UP000051752};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRC89786.1}.
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DR EMBL; LMIW01000008; KRC89786.1; -; Genomic_DNA.
DR RefSeq; WP_056825092.1; NZ_LMIW01000008.1.
DR AlphaFoldDB; A0A0Q8Y6H5; -.
DR STRING; 1736603.ASE25_09585; -.
DR Proteomes; UP000051752; 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}.
FT DOMAIN 64..128
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 138022 MW; 0D65B82B2D9D0105 CRC64;
MAPVSAAFRS TDTARGGVDG PASAALLRAG RFFTRWEESD DGRAVFREGG RAGDVFYRDR
WSHDKVVRST HGVNCTGSCS WKVYVKDGII TWETQQTDYP SVGPDRPEYE PRGCPRGAAF
SWYTYSPTRV RYPYVRGVLL EMYREAKGRL GDPVAAWHEI TTDPDKRRRY QSARGKGGLV
RASWGEAVEI AAAAHVHTIK EYGPDRVAGF SPIPAMSMVS HCVGTRFIQL IGGVMTSFYD
WYADLPVASP QVFGDQTDVP ESGDWWDATY LMMWGSNVPV TRTPDAHWMA EVRYRGTKIV
TVSPDYADNT KFADEWMPAQ AGTDAALAMA MGHVLLKEFF VDREVPFFTD YVRTYSDLPF
LIRLEAPEEP YAAASGEGAG APFVPGKFLT ASDLSADGAA VPDEDAWKTV LLDEVTGQPV
VPNGSMGFRY ADSGKGRWNL DLDGVAPALT MTGGAAEAVE VLLPAFVEPD GTGSVLRRGV
PARRVGGHLV TTVYDLMLAQ YGVEREGLPG SWPTGYDDVT APYTPAWQAE ITGVPAEQCI
RIAREFATNS EQSQGRSMII MGAGICQWFH GDATYRAILS LLILTGCMGR NGGGWAHYVG
QEKCRPITGW ISLANALDWG RPPRTMTGTS YWYMHTDQWR NDGYSADSLN SPLARGHLAG
KHTADTIAQS ARMGWMPFYP QFGTNPLQVA EDARAAVDAG TAASPAAYVA DALHDGTLTS
AIEDVDAPEN WPRTLVLWRS NLMGSSAKGN EYFLRNLLGT HHNVLGSENP LAPRPSEVKW
HNEAPEGKLD LLLSADFRMT STTLLSDIVL PAATWYEKHD LSSTDMHPFV HAFTPAIDPP
WEAKSDFELF HLLAEKLSDL ARTHLGVRKD LVSVPLMHDT PGETAQPGGR AVDWRATGHP
GVPGRTMPVF QLVERDYTAI SEKLATVGPL ADSLGFTVKN VTYRVEEEVA RLAARNGVML
GGAGDGRPAI DSDAKLAEAI LTFSGTTNGH LAVQGFRTLE ERVGKKLVDL AEGSEEKHVT
FADTQSAPVA VITSPEWSGS ETGGRRYAPF TVNIERLKPF HTLTGRMHFY LDHDWMQDLG
EALPIYRPPL DMHRLFGEPK LGPDGSKQVT VRYLTPHSKW SIHSEYQDNL LMLSLSRGGP
TVWMSPQDAG SIDVADNDWV ECLNTNGVLV GRAIVSPRMP EGVVYVHHAQ ERTIDVPKSE
ATGRRGGIHN SVTRLLVKPT HLIGGYAQLS YTFNYLGPTG NQRDMVSTVR KRSQEVTY
//
