ID A0A1Q5EAK7_9ACTN Unreviewed; 1327 AA.
AC A0A1Q5EAK7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Reductase {ECO:0000313|EMBL:OKJ05127.1};
GN ORFNames=AMK18_01210 {ECO:0000313|EMBL:OKJ05127.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ05127.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKJ05127.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKJ05127.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 -!- 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:OKJ05127.1}.
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DR EMBL; LISW01000001; OKJ05127.1; -; Genomic_DNA.
DR Proteomes; UP000186839; Unassembled WGS sequence.
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; 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; 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 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; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
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};
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 Reference proteome {ECO:0000313|Proteomes:UP000186839};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 791..929
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 957..1176
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 142823 MW; 68899160B6013DEB CRC64;
MVLDIAAGPD GRRTVRRASG DKAHPANAGR LCTKGATTAD MLAAPGRLTT ALVRPERGAE
PVPVGVDEAV ASTARRLRAV IDTHGPDAVA FYVSGQLSLE AQYLANKLAK GFVRTNRVES
NSRLCMASAG SGYKMSLGAD GPPGSYDDLD RADVFLVIGS NMADCHPILF LRLLDRVKAG
AKLIVVDPRR TATADKADLF LRVRPGTDLA LLNGLLHLLH ANGHTDPAFI AAHTEGWEEM
PEFLADYPPD AVAEITGIPE EDIREAARWI GEAGEWTSCW TMGLNQSTHG TWNTNALINL
HLATGAICRP GSGPLSLTGQ PNAMGGREMG YMGPGLPGQR SLLDDEDRAF TEELWGLAPG
TLRKDECGRG TVEMFERMAA GDIKACWIIC TNPVASVANR RTVIEALEVA ELVITQDVFA
DTETNAYADV VLPGALWSEA EGVLVNSERN LTLARPAVEP PGEALADWRI IARIACALGY
EDAFTYDSAE EVFEEIKRAA NPRTGYDLRG VTYERLRTAP VQWPAPTAEG PDRNPIRYLA
PDGGGPVFPT PTGRARFFGR PHIPAAEMPD DDYPFLLNTG RVQHQWHTLT KTGKVAKLNR
LNPGPFVEVH PEDAARLGLA EGDSVEVESR RGRAVLPAVV TDRVAPGCCF APFHWNDLFG
EYLSVNAVTG DAVDPVSYQP EFKVCAVTLT KVAAAPVPLP VPAVPETAAV FGLETTPPPV
LAEHERQYLV GFLAGLPLGA PGVPVLPAGA PFSAEHARWV NGVLAGMYSR TGPPAEDPEP
VPAAEAPGRE VVVLWASQTG NAEEFAVATA DRLTATGHRA RLLGMDEADP RALPPAADLL
LITSTFGDGD APDNGSGFWE ALTAADLPPL DGRRFAVLAF GDSSYDDFCG HGRRLDSRLD
ELGAVRLAPR TDCEPDYEPS ALSWLDQVLA GLTAPPAEPA PAPPSAPAPA PVRTPKPAPV
TARLAGNRLL GLPGSGKEVR RFTFDTSGTG TALDYAAGDA LGVHAANHPD LVAEWLAVTG
LDADAEIEVS GLGGLRLGDA LLTRLDITRL TPALLGFVTE RTGDRDLKKM LRPDNKGELA
RWSWGRQAVD VLAEYPVKAT PEEWAALLKP LQPRLYSISS SPLTDPDRLS LTVSVVRYEN
TQGRPRSGVC SPFLADAAPD TRVPVFVRRA PHFRPPARPD APMVMVGPGT GVAPFIGFLE
ERRARRDPGP NWLFFGEQHR ATDFFYEEEL TSFLADSTLT RLDTAFSRDQ RAKVYVQDRM
REHGAKLWTW LRDGAHFYVC GDAARMAKDV DRALRDIAVA HGGLDPEAAA LYVKQLAADK
RYVRDVY
//
