ID A0A3S1DQB1_9BACT Unreviewed; 791 AA.
AC A0A3S1DQB1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=ECE50_014735 {ECO:0000313|EMBL:NSL88101.1};
OS Chitinophaga solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1233460 {ECO:0000313|EMBL:NSL88101.1, ECO:0000313|Proteomes:UP000281028};
RN [1] {ECO:0000313|EMBL:NSL88101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mgbs1 {ECO:0000313|EMBL:NSL88101.1};
RA Goh C.B.S., Lee M.S., Parimannan S., Pasbakhsh P., Yule C.M., Rajandas H.,
RA Loke S., Croft L., Tan J.B.L.;
RT "Chitinophaga laudate sp. nov., isolated from a tropical peat swamp.";
RL Submitted (MAY-2020) 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:NSL88101.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RIAR02000001; NSL88101.1; -; Genomic_DNA.
DR Proteomes; UP000281028; 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};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000281028}.
SQ SEQUENCE 791 AA; 89258 MW; 92CC204FECFCD92F CRC64;
MYVIKRDGRK EAVKFDKITA RIEKLCYGFN TEYVDAIDVA KKVIQGLYDG VTTSELDNLA
AETAASLTTK HPDYALLASR IAVSNLHKNT EKSFSKTMRK LYNYIDPKTS KNAALLSDEV
WDIIEKNADI LDSNIIYDRD FAFDYFGFKT LERSYLLKTD GRVVERPQHM FMRVSVGIHK
EDIESAIKTY NLMSERWFTH ATPTLFNAGT PKPQMSSCFL LTMQDDSIEG IYDTLKQTAK
ISQSAGGIGL SIHNIRATGS YISGTNGTSN GIIPMLRVFN DTARYVDQGG GKRKGAFAIY
LEPWHADIFE FLDLRKNHGK EEMRARDLFY ALWMPDLFMK RVEANGNWSL FCPHEAPGLH
ECWGEEFEQL FEKYEQEGRA RKTVKAQDLW FAILDAQIET GTPYLLYKDS ANRKSNQQNL
GTIKSSNLCT EIIEYTDANE VAVCNLASLA LPRFVNEGQF DHQKLYEVTY QATLNLNKII
DHNYYPVEEA ERSNLRHRPI GLGVQGLADA FILMRYPFES DEAKKLNSEI FETIYFASLT
ASNDLAKKDG HYETFPGSPA SKGILQFDMW NVTPSSRWNW DALKKAVVKD GIRNSLLLAP
MPTASTSQIL GNNECFEPYT SNIYTRRVLS GEFVVVNKHL LKDLVDLGLW DNEMKTKIIA
SNGSIQHIAE IPANIKELYK TVWEIKQRNL IDMAADRGAF ICQSQSLNLF VDTPTTAKLT
SMHFYAWKKG LKTGMYYLRT QAAAQAVQFT VEKQGGQQIQ PVVAAGGDVS IDDIPVGAVC
TMEEGCVTCS A
//
