ID D3QZU3_MAGIU Unreviewed; 844 AA.
AC D3QZU3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 OrderedLocusNames=HMPREF0868_0098 {ECO:0000313|EMBL:ADC91461.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91461.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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 EMBL; CP001850; ADC91461.1; -; Genomic_DNA.
DR RefSeq; WP_012994179.1; NC_013895.2.
DR AlphaFoldDB; D3QZU3; -.
DR STRING; 699246.HMPREF0868_0098; -.
DR KEGG; clo:HMPREF0868_0098; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR OMA; LEIWHID; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008234; Chromosome.
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:UniProtKB-UniPathway.
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:UP000008234}.
FT DOMAIN 1..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 844 AA; 97095 MW; AEFC92C1C408E606 CRC64;
MKIEKRNGQI ETFRSAKITA AMAKAFDGLN VPINDDQLLK LTEKVEKLIN TEVANGYVLK
VERVQDLVEK ILMQEGYYEV AKSYILYRSE RAQKRTMRRQ LTELVKFQGL DETLRSIQKD
YKSDNYSLDL LLAKFNSFYK LDMPFQEAMR MLIKAAVELT TQEAPAWEFI AARLMMLQIN
EQIGEVCKQF KLRNLYDKIS YLENEGLYGR YILQSYSKEE IATAESFIVE ERNKLLNYSG
LDLLCKRYVI HNYRHQIIET PQEMFLGIAL HLAMHEKNGD ERMGWVRKFY DMLSQLQVTM
ATPTLSNARK PYHQLSSCFI DTVPDSLEGI YRSITNFAQV SKFGGGMGLY FGKVRAIGSS
IRGFQGVAGG VIRWVKLAND TAVAVDQLGM RQGSVACYLD IWHKDVPEFL QVRTNNGDDR
MKAHDIFPAI CYPDLFWRQV RDNINSSWYL LCPHEVLTVK GYALEDYYGE EWEKRYLDCV
RDNRISKREI PLKELVRLIL KSCVETGTPF TFNRDIVNRN NPNKHKGIIY CSNLCTEICQ
NMSEIKQVSL ELKDENGDTV VVETTKPGDF VVCNLASLAL GRIDMKRPEE LESIVGTVVR
ALDNVIDLNF YPLPYAKHTN KAYRSLGLGI SGYHHMLAKN GIAWESEEHL QFVDKIFERI
NYAAIKTSME LAKEKGKYKY FEGSDWATGE YFTLRNYTDE KWQSLASAVA KNGLRNAYLI
AIAPTSSTSI IAGTTAGLDP VMKRYFLEEK KGVIMPRVAP ELSLNTYWLY KEAHLIDQEW
TVRAAGVRQR HIDQAQSLNL YVTQNLTFRQ ILGYFIKAWE NGVKTIYYCR SLALEVEDCE
SCSS
//