ID A0A1V4DAW7_9ACTN Unreviewed; 1386 AA.
AC A0A1V4DAW7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Reductase {ECO:0000313|EMBL:OPF83096.1};
GN ORFNames=VT50_0205080 {ECO:0000313|EMBL:OPF83096.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF83096.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF83096.1, ECO:0000313|Proteomes:UP000033615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OPF83096.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAKD02000006; OPF83096.1; -; Genomic_DNA.
DR RefSeq; WP_046084634.1; NZ_LAKD02000006.1.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000033615; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 CDD; cd06199; SiR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.360; -; 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 Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 11..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 838..976
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1015..1235
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 726..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 149049 MW; 8A8E3EE3E87AFBF1 CRC64;
MAASGSRSED TTKVRTVCSY CGVGCGLVLD VGSGPDGRRT VRKASGDKEH PANFGRLCAK
GATTADMLAA PGRLTTALRR PHRAEEPVPT PRDEAIAETA RRLRAIVEEH GPDAVALYVS
GQLSLEAQYL VNKLAKGFLR TNQIESNSRL CMASAGTGYK LSLGADGPPG SYEDFDRADV
FFVIGSNMAD AHPILFLRMM DRVKSAGAKL IVVDPRRTAT AAKADLFLQI KPGTDLALLN
GLLHLLRANG HTDAAFIAAH TEGWEAIPEF LADYPPATVA EITGIPEDDI REAARLIGEA
GEWMSCWTMG LNQSTHGTWN TNALVNLHLA TGAICRPGSG PFSLTGQPNA MGGREMGYMG
PGLPGQRSVL ADADRAFVEN LWGLPQDTIR ADGVGKGTVE MFQRMADGDI KACWIICTNP
VASVANRKTV IEGLEAAEFV VTQDVFAETE TNAYADVVLP GALWTETEGV LINSERNLTL
ARPVVDPPGE AMADWRVIAA VARAMGFARG FGYDSAEEVF EEIKRAWNPV TGWDLRGVSY
ERLRAAPVQW PAASAEGADR NPIRYLGADG APLFPTATGR AVFYPRPHVP AAELPDDDYP
YQLNTGRLQH QWHTLTKTAR VPRLNRLNPG PFVEVHPRDA AELGVAEGDS VEVASRRGRA
VLPAVVTDRV RPGCCFAPFH WNDLFGEYLS VNAVTSDAVD PLSFQPEFKV CAVSLTKVAT
PVTVRAPASA DAQHRSTGTS ATADMTSTTA PAGPLPTAAA PAPFGLEPTP PPSLTEDERR
YLTGFLAGVP SGAPGVPVLP ADAPFHPSHA LWVNGVLAGM HSRAEPTAPT AEVPRRQVVI
LWASQTGNAE EFAAATVDRL TAHGHAASRV SMDEADPAAL PYDADLLLIT STFGDGDAPD
NGSAFWAALT APDAPRLPDR RYSVLAFGDS SYGDFCGHGR RLDRRMAELG AVRLAPRTDC
EPDYGAEAGA WLDQVLIALK NAEQPSPDPA PAPDPAPAAR TAPAARTAAA AGTAPAPATA
RLTGNRRLSL PGAAKEVRRF TFDTRDGETP LGYEAGDALA VRPLNWPELV TEWLAVTGLD
ANAAVRIGNV GEMPFAEALS RHLDITSVTP DLLRFAADRI HDPRELRKLL RPDNKGELAK
WSWGRQAVDV LAEFGIRAGA QEWTDLLGRL RPRLYSISSS PLTDPHLVSL TVSVVRYENL
GGRPRQGVCS PFLADAEPGT RVPVRVQRTP HFRPPADPDT PMVMVGPGTG IAPFIGFLEE
RRARGHRAPN WLFFGEQHRA TDFYYEEELT AFLADGTLTR LDTAFSRDER AKKYVQDRMR
EHGPLLWSWL QDGAQVYVCG DASRMAKDVD QALRDIATVH GGLGGAGAAA YVKQLATDKR
YLRDVY
//