ID A0A3M7KM01_9FLAO Unreviewed; 825 AA.
AC A0A3M7KM01;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=EB822_02490 {ECO:0000313|EMBL:RMZ51571.1};
OS Flavobacteriaceae bacterium PRS1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2483459 {ECO:0000313|EMBL:RMZ51571.1, ECO:0000313|Proteomes:UP000276892};
RN [1] {ECO:0000313|EMBL:RMZ51571.1, ECO:0000313|Proteomes:UP000276892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRS1 {ECO:0000313|EMBL:RMZ51571.1,
RC ECO:0000313|Proteomes:UP000276892};
RA Peoples L., Norenberg M., Mcgoldrick M., Novotny M., Bochdansky A.,
RA Bartlett D.;
RT "A Full-Ocean-Depth Rated Modular Lander and Pressure-Retaining Sampler
RT Capable of Collecting Hadal-Endemic Microbes Under in situ Conditions.";
RL Submitted (OCT-2018) 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|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}.
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:RMZ51571.1}.
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DR EMBL; RDRZ01000004; RMZ51571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7KM01; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000276892; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000276892}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 825 AA; 93556 MW; 1EB2971992D1B918 CRC64;
MYVVKRDGRK EPIMFDKITS RVRKMCYDLN SLVDPVKISM RVIEGLYDGV TTSELDNLAA
EVAATMTTAH PDYAKLAARI SVSNLHKSTK KTFSEVMTDL YTYVNPRTEK KAPLLSEEVY
QVIIDNKEKL DSTIIYNRDF GYDFFGFKTL ERSYLLKLNG KIAERPQHML MRVSVGIHLN
DLDAVIETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL TMKDDSIEGI YDTLKQTAKI
SQSAGGIGLS IHNIRATGSY ISGTNGTSNG IVPMLQVFND TARYVDQGGG KRKGSFAIYL
EPWHADIFDF LELKKNHGKE EMRARDLFYA MWISDLFMKR VQEDASWTLM CPNECPGLCD
VYGEEFETLY TKYEAEDKGR KSIKARELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE IMEYTSPDEI AVCNLASIAL PMFIKNGAFD HKELFRITKR VTKNLNRVID
RNYYPVKEAK TSNFRHRPIG LGVQGLADIF IKLRLPFTSD EAKQLNKDIF ETLYFAAVTA
SMEEAKTDGP YQSYKGSPIS KGEFQYNLWG IKDEELSGLW DWAKLRKQVL KHGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVELG LWNDGLKQDI
MRANGSIQGI DNIPDDIKEL YKTVWELSMK DIIDMSRQRG YFIDQSQSLN LFLEGATMAK
LTSMHFYAWK SGLKTGMYYL RTKSAVDAIK VTLDNKKKSE PAVEAVDVNE TLVSQQKQLA
VKTAEKFAKQ TSTEVEVKPM SADEMKALVA QAKEAEGDDC LMCGS
//
