ID A0A0K6FQ71_9AGAM Unreviewed; 1447 AA.
AC A0A0K6FQ71;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=RSOLAG22IIIB_07918 {ECO:0000313|EMBL:CUA68400.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA68400.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA68400.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA68400.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|ARBA:ARBA00024942,
CC ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; CYGV01000424; CUA68400.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841}.
FT DOMAIN 533..624
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1375..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 158730 MW; AA43B85116774B4C CRC64;
MDKEADIIFV GGGTSACVAA GRLAASNPNI EILIIEQGPD NFKDPSVTTP ALFPTHLSPE
SKTALCWKGA KSEAINGRET VLMSGGVLGG GSSINFMMYA RPSASDFDDW NTVGWSSQDL
IPLLEKNETY HIAPGLKNHG YDGPVNISYG GHFAQVAQEY LDVCDARGIS TKDDIMDLHT
GHSSGRLAKY IDPVSGHRQD AAHRFIHNRS ENKSLRVMTK TLVARVLFEG TKAIGVEVVA
NKKQDPNADQ TPRKIIAHKL VVVSSGAIST PLILERSGVG DPTLLAKLGV EVVVDLPRVG
TEYQDHGISF VPFFVSDDIE TFNPLLAQEP DVMNAATVQF KEGRGPLASN FCDAGSKIRP
TPEELKEMGP AFNHYWKRYL EPAPDKPVAI QVIVNGFLGP PSIVPAKSCL IMFANFVAYP
VSRGHVHITS TDPYAPPDFH PGAIEEQADV EVHKWIYKKT REIARRMPSY RGELDLLHPK
FSEGSAAACV RLDKPLPKDV NDLVYTPEDD KAVEDFVHQF GDSTPHSLGT VRMGPKEKGG
RKERVAFDKI TARITKLCYG LDRSHVDPIE ITKKVIAGVY AGVTTVELDN LASETAAYLT
TKHPDYAILA ARIAISNLHK ETKKNFSAVI ADLYSYVNPK NGRPAGMISK ETYEIVQENA
AALDSAMIYE RDFHYNFFGF KTLERSYLLR INGRVAERPQ HMLMRVAVGI HGRNIDRAIE
TYNLMSERYF THASPTLFNA GTPHPQLSSC FLVAMKDDSI DGIYDTLKTC AMISKTAGGI
GLHIHNIRAT GSYIAGTNGY SNGIVPMLRA YDATARYVDQ GGNKRPGAFA IYLEPWHSDV
FEFLDLRKNH GKEEVRARDL FYALWIPDLF MQRIEEDGDW SLFCPNEAPG LADVHSAAFV
ELYTKYEKEG RARKTIKAQK LWYAILDAQI ETGGPFMVYK DAANAKSNQQ NLGTIKSSNL
CTEIIEYSAP DEVAVCNLAS IALPTFIVND PDAPHGKRYD FKKLHEVTKV VANNLNTIID
VNYYPVPEAR NSNMRHRPIG IGVQGLADAF MCMKMPFDSP EARELNLLIF ETIYHAAVEA
SAEMAEAEGA YSTFPGSPAS QGKLQFDLWG VTPSGLWEWE DLKAKVMRTG LRNSLLLAPM
PTASTSQILG FNECFEPYTS NIYTRRVLAG EFQVVCPWLL RDLVSLGLWD DDMKNMIIAS
GGSIQNIPGI PDDIKAIYKT VWEISQKTVL NLAADRGAFI CQSQSLNVHL QSPNARQLTS
MHFYGWKKGL KTGMYYLRTR PAAQAIQFTV DQSVIKQANA AKKAAVTPTP ITREIKQEAV
TPSLANASNV SLAPTSTDPT VTPTIAALRN LTLADSGAPS PAISTAAVNG SSLSLPVTSS
AGTPSVAETA PTTLPTSEGA NTPSTETPAQ IDPEYAAALE RQRQRELEQA KLYCSLENKE
ACEMCSG
//
