ID G5JRJ9_STRCG Unreviewed; 719 AA.
AC G5JRJ9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=STRCR_2008 {ECO:0000313|EMBL:EHI75079.1};
OS Streptococcus criceti HS-6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI75079.1, ECO:0000313|Proteomes:UP000004322};
RN [1] {ECO:0000313|EMBL:EHI75079.1, ECO:0000313|Proteomes:UP000004322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-6 {ECO:0000313|EMBL:EHI75079.1,
RC ECO:0000313|Proteomes:UP000004322};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (JUL-2011) 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:EHI75079.1}.
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DR EMBL; AEUV02000002; EHI75079.1; -; Genomic_DNA.
DR RefSeq; WP_004229107.1; NZ_AEUV02000002.1.
DR AlphaFoldDB; G5JRJ9; -.
DR STRING; 873449.STRCR_2008; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004322; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 719 AA; 81068 MW; 2F58DA66426F3CF8 CRC64;
MSLKDLGEVS YFRLNNEINR PVNGQIPLNK DKEALQAFFR ENVVPNSMAF DSITDKVRFL
IDNDYIEAEF IGKYSVEFIE ELAQELQAAD FHFQSFMAAY KFYQQYALKT NDGEFYLESI
EDRVLFNALY FADGDEQLAK DLATEMIHQR YQPATPSFLN AGRSRRGELV SCFLIQVTDD
MNAIGRSINS ALQLSRIGGG VGISLSNLRE AGAPIKGYAG AASGVVPVMK LFEDSFSYSN
QLGQRQGAGA VYLDVFHPDI LSFLSTKKEN ADEKVRVKTL SLGITVPDKF YELARKNEDM
YLFSPYSIEK EYGVPFNYIN ITEKYDELVA NPKIVKTKIS ARDLETEISK LQQESGYPYI
INVDAANRSN PIDGRIIMSN LCSEVLQVQK PSLINDAQEF VQMGTDISCN LGSTNVVNMM
ASPDFGRSIK AMTRALTFVT DSSSIEAVPT IKAGNEQAHT FGLGAMGLHS FLARNHIEYG
SPESIEFTDI YFMLMNYWTL VESNNIARER GESFVGFEKS KYADGTYFDK YITGKYVPKS
AKVKELFEDH FIPQAEDWEA LRQAVMKDGL YHQNRLAVAP NGSISYINDV SASIHPITQR
IEERQEKKIG KIYYPASGLS TDTIPYYTSA YDMDMRKVID IYAAATEHVD QGLSLTLFLR
SDIPEGLYEW KKESKQTTRD LSILRNYAFN KGVKSIYYVR TFTDDGDEVG ANQCESCVI
//
