ID V9HEC7_9CLOT Unreviewed; 743 AA.
AC V9HEC7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=CSBG_00092 {ECO:0000313|EMBL:EEH96466.1};
OS Clostridium sp. 7_2_43FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH96466.1, ECO:0000313|Proteomes:UP000017809};
RN [1] {ECO:0000313|EMBL:EEH96466.1, ECO:0000313|Proteomes:UP000017809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH96466.1,
RC ECO:0000313|Proteomes:UP000017809};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA Ambrose C., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Clostridium sp. 7_2_43FAA.";
RL Submitted (JAN-2012) 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:EEH96466.1}.
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DR EMBL; ACDK02000041; EEH96466.1; -; Genomic_DNA.
DR RefSeq; WP_008681135.1; NZ_JH815222.1.
DR AlphaFoldDB; V9HEC7; -.
DR STRING; 457396.CSBG_00092; -.
DR GeneID; 65400549; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000017809; 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; 3.20.70.20; -; 1.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017809}.
FT DOMAIN 601..623
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 743 AA; 85528 MW; 7D51928FA63A831B CRC64;
MTHLLNICRL ALDGIDNGQR IYTVERLLEA LNHIVRPNMK DEEIRDSIIQ VALELTSDME
PRWQNAAARL YVFKLYDKIR KNREINNDEN IYGDLYGFIN KLTEKGLYGK YILENYTREE
ILELENEIKP ERDFLFTYSG INLLAKRYLI QDFDRSILEL PQQMFMGIAM HLAIPEKKEV
RVLWAKRFYD VLSSLKATMA TPTMSNARKP FYQLSSCFID TVQDSLKGIY KSLDNFAEVS
KFGGGMGIYI GKVRALESPI RGFKGASGGV IPWVKLFNDT AIAVDQLGVR NGSVAIWLDA
WHKDLPEFLQ LKTNNGDDRK KAHDVFPGLC YPDLFWKLAE TDIDANWYMM CPHEIRLAKG
YSLEDFYGEE WEKKYYECVE DDSISKRVMS VKEIVRLIIK SAAETGTPFA FYRDTVNKMN
PNKHKGMIYS SNLCTEIMQN MSSMDIQQSE VKDENGDTII IEKTKSGDFV VCNLSSVVLG
NIDVKNDEEL GYVVETQIRA MDNVIDLNYY SVPFAEVTNK KYRAIGLGTS GYHHMLANNL
IHWTEDSHKE FADDVYERIN YHAIKASMNI SKEKGRYSCF EGSDWHNGNY FELRGYKSEK
WNQLREEVNT HGMRNGYLMA VAPNGSTATI AGTSEGIDPV MARFWLEEKK GSIIPKTAPN
LSEENYWYYN SAYNIDQKWC VQINGIRQRH IDQGQSFNLY ITTNYTMRQI MNLYIEACKA
GVKSIYYVRS KSLTVSDCES CSA
//
