ID A0A3B3C4R3_ORYME Unreviewed; 794 AA.
AC A0A3B3C4R3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000012052.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000012052.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
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 AlphaFoldDB; A0A3B3C4R3; -.
DR STRING; 30732.ENSOMEP00000012052; -.
DR PaxDb; 30732-ENSOMEP00000012052; -.
DR Ensembl; ENSOMET00000019290.1; ENSOMEP00000012052.1; ENSOMEG00000013415.1.
DR GeneTree; ENSGT00910000144246; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 InterPro; IPR005144; ATP-cone_dom.
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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 2..93
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 794 AA; 90298 MW; D823325AFF6DDD9E CRC64;
MMYVIKRDGR QERVMFDKIT SRIQKLCYGL NSEFVDPAQI TMKVIQGLYS GVTTVELDTL
AAEIAATLTT KYPDYAILAA RIAVSNLHKE TKKVFSEVME DLYNYVNPLN KRHSPMISKE
TLDIVLENKD RLNSAIIFDR DFSYNFFGFK TLERSYLLKI NGKVAERPQH MLMRVAVGIH
GRNIDAAIET YNLLSEKWFT HASPTLFNAG TNRPQLSSCF LLAMKDDSIE GIYDTLKQCA
LISKSAGGIG VAVSCIRSTG SYIAGTNGNS NGLVPMLRVY NNTARYVDQG GNKRPGAFAM
YLEPWHYDVF DFLELKKNTG KEEQRARDLF YALWIPDLFM KRVESNQDWS LMCPNECPGL
DECWGEEFEK LYTKYEKEGR VKRVVKAQQL WYAVIESQTE TGTPYMLYKD ACNRKSNQQN
LGTIKCSNLC TEIVEYTSKD EVAVCNLASI ALNMYVTPER TFDFKKLASV TKVIVKNLNK
IIEINYYPII EAERSNKRHR PIGIGVQGLA DAFILMRYPF ESPEAQLLNI QIFETIYYAA
LEASCELAAE LGAYETYEGS PVSKGILQYD MWEKTPTDLW DWKLLKEKIA KHGVRNSLLL
APMPTASTAQ ILGNNESIEA YTSNIYTRRV LSGEFQIVNP HLLKDLTERG LWSEEMKNKL
IANNGSIQDI AEIPNDLKQL YKTVWEISQK TVLKMAADRG AFIDQSQSLN IHIAEPNYGK
LTSMHFFGWK QGLKTGMYYL RTKPAANPIQ FTLNKEKLKE DQPSKTAEQD TKERNAAAMV
CSLENRDECL MCGS
//
