ID A0A560W7Z3_9MICO Unreviewed; 1250 AA.
AC A0A560W7Z3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=FB557_2386 {ECO:0000313|EMBL:TWD13753.1};
OS Marihabitans asiaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Marihabitans.
OX NCBI_TaxID=415218 {ECO:0000313|EMBL:TWD13753.1, ECO:0000313|Proteomes:UP000315628};
RN [1] {ECO:0000313|EMBL:TWD13753.1, ECO:0000313|Proteomes:UP000315628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18935 {ECO:0000313|EMBL:TWD13753.1,
RC ECO:0000313|Proteomes:UP000315628};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-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:TWD13753.1}.
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DR EMBL; VIUW01000004; TWD13753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A560W7Z3; -.
DR Proteomes; UP000315628; 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:UP000315628}.
FT DOMAIN 63..127
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1250 AA; 138765 MW; BA4A7BA346CE017C CRC64;
MTATSDQTSP LPESAGMDSP LSAALVGTRR FFTKAGISPD QRSMYLEGGR SGDSFYRDRW
SHDKVVRSTH GVNCTGSCSW KVYVKDGIIT WEAQQTDYPS TGADRPEYEP RGCPRGAAFS
WYTYSPTRVR YPYVRGVLLE MFRRAKETHG DPVVAWGSIV QDEEQVRTYK SARGKGGLVR
STWEEVTEMV AAAYVYTVKR WGPDRIAGFS PIPAMSPVSY ASGARFHELI GAPMLSFYDW
YADLPPASPQ MFGDQTDVPE SGDWWDAAYL IMWGSNVPLT RTPDAHWMTE ARYRGQKVIA
VAPDYAENVK FADEWVASAP GTDGALAMGM GHVILREFFA DAQHDFFTRY NQRYTDLPYL
VTLDEVDGEG GDAPAYRPGK FLVAGDIDGH PEATSENAMW KTAVLDSVTG EVVIPNGSIG
HRFGEEGAGR WNLDLGEIEP ALTLYGAHEE SVEVELARFD TPGGAMSTER RGVPVRRVGG
RLVTTVLDLM LAHYGVGRDG LPGRWPQGYE DPSVPATPAW AAEISGVPVE QITRLAREWA
RNALDTGGRG MILMGAGTNH WYHSDQLYRA MLVLTTICGT QGRNGGGWAH YVGQEKIRPI
MGFQHLAFAL DWVRPPRHMN QTAYWYVNTS QYRYDTFTAD EANGSPGAFG QRTTMDLLAQ
SVRLGWTPSY PQFDRSSLAV ADEAVQAGMP AGEYVARSLK EGSLHFAVED PEAPDNHPRV
LALWRSNLFG SSAKGNEYFL KHLLGTDNAV KGTQAPPELR PQSVAWPEEA PEGKLDLLVT
LDFRMTSSTL LSDVVLPAAT WYEKHDLSTT DMHPFVHSFN PAIAPPWQSK SDWETWKVIA
KRFSELAADH LGTRTDVVAK PLWHDTPEAM ATVHGRVLDW AEGEVEPVPG KTLPVLAAVE
RDYPAVYQKM TAIGPLMAKA GMLTKGVKYE VGREVEILGR RNGIVRGGVA DGQPKLETDI
QVADAMLHFS GVSNGHLATQ GFRFLEQRTG TELHDLSAEH EGKQITFADT QAAPVPVITS
PEWSGSESGG RRYSPFTINI ERLKPFHTLT GRQQFYLDHD WMTDMGEGLP TYRPPLDMSR
LSGETPLGEQ TESEGRSVAL SVRYLTPHNK WSIHSEYQDN LFMLSLSRGG QTIWMSDVDA
EKIGVKDNDW VEAVNRNGVV ACRAVVSHRM PEGTVYMHHA QDRLIDTPLT ETDKLRGGIH
NSLTRIMLKP SHIIGGYAQL SYFFNYIGPT GNNRDEVTMI RRRTNQEVTY
//
