UniProt: A0A1H5PQ48

Database: UniProt
Entry: A0A1H5PQ48_9ACTN

LinkDB:  A0A1H5PQ48_9ACTN 
Original site:  A0A1H5PQ48_9ACTN

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Ontology (6)   
   GO (6)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (25)   
   InterPro (15)   
   Pfam (6)   
   PROSITE (3)   
   SMART (1)   
All databases (32)   

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ID   A0A1H5PQ48_9ACTN        Unreviewed;      1375 AA.
AC   A0A1H5PQ48;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sulfite reductase [NADPH] flavoprotein, alpha-component {ECO:0000313|EMBL:SEF15865.1};
GN   ORFNames=SAMN05216533_7547 {ECO:0000313|EMBL:SEF15865.1};
OS   Streptomyces sp. Ag109_O5-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF15865.1, ECO:0000313|Proteomes:UP000198812};
RN   [1] {ECO:0000313|EMBL:SEF15865.1, ECO:0000313|Proteomes:UP000198812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF15865.1,
RC   ECO:0000313|Proteomes:UP000198812};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNTQ01000001; SEF15865.1; -; Genomic_DNA.
DR   STRING; 1855349.SAMN05216533_7547; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000198812; 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   Reference proteome {ECO:0000313|Proteomes:UP000198812};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          21..82
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   DOMAIN          841..979
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          1004..1224
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1375 AA;  147210 MW;  358FA4C8C20BBB1E CRC64;
     MADEQEQGAP VAAPDSRSTG TRRVRTVCSY CGVGCGMVLD VGRGPDGRRT VLQASGDKEH
     PANFGRLCTK GATTADMLAA PGRLTTALLR PERGAEAVPS AVDAAVAETA RRLRAIVDEH
     GPDAVALYVS GQMSLEAQYL ANKLTKGWLR TNNIESNSRL CMASAATGYK LSLGADGPPG
     SYQDLDRADV FLVIGANMAD CHPILFLRLM DRVKAGAKLI VVDPRRTATA DKADLFLQVR
     PGTDLALLNG LLHLLHANGH TDPDFVAAHT EGWEAMPEFL AGYPPAAVAD ITGIPEADLR
     AAARLIGEAG EWTSCWTMGL NQSTHGTWNT NALVNLHLAT GKICRPGSGP LSLTGQPNAM
     GGREMGYMGP GLPGQRSVLV DADRAFVEEQ WGLAPGSIRA DGVGKGTVEM FRKMADGEIK
     ACWIICTNPV ASVANRRSVI EGLEAAEFVV TQDVFTDTET NAYADVVLPA ALWTETEGVL
     INSERTLTLA RPAADPPGEA TADWRLIAGV ARAMGYEDGF CYDSAEEIFE EIKRFHNPQT
     GYDLRGVTYD RLRAAPVQWP AATAEGPDRN PVRYLDTDGT LTFATASGRA VFHARPHLDP
     AEMPDDDHPF VLNTGRLQHQ WHTLTKTAKV ARLNRLNPGP FVEVHPEDAA ALGLADGDSV
     EVASRRGRAV LPAVVTDRVL PGTCFAPFHW NDLFGEYLSV NAVTSDAVDP LSFQPELKVS
     AVSLTKVATP VSVQVPGAQE APAALDGPVA AVVAPTAVPV PSAASVFGLD PAPPPVLTAA
     ERQYLVGFLA GIPAGAPGVP VLSPDAPFSP DHALWVNGAL AGMYSRSAAV PAPLPTPGRQ
     VVVLWASQTG NAEDFAATAA ERLTAGGHAV SLVAMDQADP AALPPGADLL LITSTFGDGD
     APDNGAGFWD GLAALDAGPL AGRRYAVLAF GDSSYDDFCG HGRRLDSRMD ELGAVRITPR
     ADCEPDYETR AAAWLDQVLM ALQHEPTSSA AADPAPAPAR SRRPVPLTAR LVGNRLLSLP
     GAGKEVRRFT FDTRDGETPL VYEAGDALGV RPLNSPDLVA EWLDVTGLDA ATAVEVNGVG
     EVPLAEAFSR HLDITRVTPD LLRFAAERTR DPRELRKLLR PDNKDGLAKW SWGRQAVDVV
     AEFGIRAGAQ EWAGVLGRLR PRLYSISSSP LTDPHQVSLT VSVVRYENLR GRRRQGVCSP
     FLAEAEPGTP VPVHVQRSPH FRPPADPATP MVMVGPGTGV APFVGFLEER RARGHRAPNW
     LFFGEQHRAT DFYYERELTA LLADGTLSRL DTAFSRDQRA KVYVQDRMRE HGPLLWSWLQ
     DGARFYVCGD ASRMANDVER ALKDIAGAHG GLTEDEATVY VRQLAAERRY VRDVY
//

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