ID A0A0N0N6G9_9ACTN Unreviewed; 819 AA.
AC A0A0N0N6G9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KPI21831.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:KPI21831.1};
GN ORFNames=OK006_9197 {ECO:0000313|EMBL:KPI21831.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI21831.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI21831.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI21831.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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:KPI21831.1}.
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DR EMBL; LJCU01000005; KPI21831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N6G9; -.
DR PATRIC; fig|1592326.3.peg.509; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
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:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPI21831.1}.
FT DOMAIN 42..98
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 778..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 89191 MW; 56029C40CFF7F102 CRC64;
MRPEVDRIAQ PWGDRTPYGR GEAWPVRVDS FLAPGVTADA VERWVPAASL LHSNGDAMDV
AVAHGRIVGV RGRPGDRVNR GRLGPKDLFG WQANHAMDRL TTPLIRKGGR LVPCGWDTAM
DRIVARSGEL LDERGPGSIG FYTTGQLFLE EYYTLAVIAR AGIGTNHLDG NTRLCTATAA
EALKETFGCD GQPASYTDID HADVIALFGH NMAETQPVLW MRVLDRLEGP DPPRLVCVDP
RPTPVARRAT VHLAPRAGTN VALLNALLHE IIRTDRVDHD FVDAHTVGFK ELTERVADCT
PSWAAGICDV PAGKITEAAE NLGGAERLLS TVLQGVYQSH QATAAACQVN NLQLIRGMLG
RPGCGVLQMN GQPSAENTRE CGANGDLPGF RNWENEAHVE DLARIWNVDP TRIPHYAPPT
PAMQIFRYAE QGSIHMLWIT GTNPLVSLPE LHRIRDILGQ ERLFTVVQDL YLTETAQLAD
VVLPAATWAE KTGTLTNADR TVHLCEKAVD PPGAARPDLD ILLDYARRMD FRDQDGRPLV
GWHDAESAFE AWKKCSRSRP CDYTGMTYDR LRDAGGIQWP CTEDTPDGTE RLYTDGISWA
APDDCETYGK DLVTGASVSE TEYRALNPGG KAVLKAAEYV PPHETTDENY PLQLITGRTL
YHFHTRTKTG RTPQLNAAAP EVWVEISADE ALRHDVAEGD LVEVTSPRGS VRGRLRISGI
RDGMVFLPFH YGYWDTPEGH RPGAHGGRAA NETTITDWDP VSKQPLFKTA AARLALVERG
DGTGSPAPTT TASAPVDPRH VPPTAGGSAA MASQSGGEA
//