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Entry: D3QZU3_MAGIU
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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
//
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