ID   A0A4P7SNY9_9MICC        Unreviewed;      1236 AA.
AC   A0A4P7SNY9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, 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=E5206_01655 {ECO:0000313|EMBL:QCB95791.1};
OS   Arthrobacter sp. PAMC25564.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=2565366 {ECO:0000313|EMBL:QCB95791.1, ECO:0000313|Proteomes:UP000296209};
RN   [1] {ECO:0000313|EMBL:QCB95791.1, ECO:0000313|Proteomes:UP000296209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC25564 {ECO:0000313|EMBL:QCB95791.1,
RC   ECO:0000313|Proteomes:UP000296209};
RA   Park H.;
RT   "Complete genome of Arthrobacter sp. PAMC25564.";
RL   Submitted (APR-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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP039290; QCB95791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P7SNY9; -.
DR   KEGG; artp:E5206_01655; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000296209; Chromosome.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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.
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:QCB95791.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296209}.
FT   DOMAIN          55..119
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1236 AA;  136489 MW;  EAD2127632D44160 CRC64;
     MTAGGTAGFD GPASDAMLKL GRFFTKWDQT DDGRAVFREG GRKGDIFYRD RWSHDKVVRS
     THGVNCTGSC SWKVYVKDGI ITWESQQTDY PSVGPDSPEY EPRGCPRGAA FSWYTYSPTR
     VRFPYARGVL VEMYREAKAR LGDPVLAFAD VVGDPERRRR YQQARGKGGL VRVSWQEAIE
     IAAAAHVNTI KAYGPDRCAG FSPIPAMSMV SHAVGTRFIQ LIGGVMTSFY DWYADLPVAS
     PQVFGDQTDV PESGDWWDAR YLMMWGSNVP VTRTPDAHWM AEVRYRGTKV VTVSPDYADN
     TKFADEWLPA QAGTDAALAM AMGHVMLKEF FVERDVPFFS DYVRQYTDLP FLVRLDRRDD
     GSLTPSKFLT ARDLPAESGA EDAAFRTVLF DKKTGLPAVP NGSMGFRYSG SGEGKWNLDL
     EGIEPALSLR EVSGESAEIL LPCFEDADGA GSVLRRGVPV LEVEGQLVTT VFDLMLAQYG
     VGREGLPGDW AAGYEDASTP YTPAWQEEIT SVPAQACIRV AREFARNAEQ SKGRSMIIMG
     AGICQWFHGD ATYRAVLALV MLTGCMGRNG GGWAHYVGQE KTRPATGWVS LANALDWSRP
     PRTMIGTGYW YMHTDQWRQD GYSADALKSP LSTGALDGMH TADALAQSAR LGWMPFYPQF
     DRNPLDLADE AEAAVAAGTA KDTPGYIADA LKNRTLNPAI EDVDAPENWP RTLVLWRSNL
     FGSSAKGNEY FLRNLLGTHN NVLGKDHAEG LKPRDVKWHE QAPEGKLDLL VSADFRMTST
     TLLSDVVFPA ATWYEKHDLS STDMHPFVHA FTPAIDPPWE TKTDFDTFHL LAQEFSRQAK
     THLGVRRDLV SVPLLHDTPG QLAQPGGIVR DWRDTSIPAV PGQNMPIFSV VDRDYTAIAD
     KLAAVGPLAD KLGFTVKNVT YKLAGPLERL SRSNGVMLGG AADGRPAIDT DAKMAEAILA
     FSGTTNGALS VQGFKDLEIR TGRKLADLSE GSEEKFITFA QTQAGPVPVI TSPEWSGSET
     GGRRYAPFTI NVERLKPWHT LTGRMHFFLD HDWMIDIGEA LPIYRPPLDM HRLFGEPKLG
     QDGSMEVVVR YLTPHSKWSI HSEYQDNLLM LSLSRGGPTV WMSPSDAESI QVNDNDWVEC
     VNINGVLVAR AIVSHRMPAG VVYVHHAQER TIDVPKSEAT GRRGGIHNSV TRLLVKPSHL
     IGGYAQLAYA FNYLGPTGNQ RDMVATVRRR SQEVQY
//