ID E4HJM1_9ACTN Unreviewed; 854 AA.
AC E4HJM1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF9607_01105 {ECO:0000313|EMBL:EFS92575.1};
OS Cutibacterium modestum HL044PA1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium; Cutibacterium modestum.
OX NCBI_TaxID=765109 {ECO:0000313|EMBL:EFS92575.1, ECO:0000313|Proteomes:UP000003179};
RN [1] {ECO:0000313|EMBL:EFS92575.1, ECO:0000313|Proteomes:UP000003179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL044PA1 {ECO:0000313|EMBL:EFS92575.1,
RC ECO:0000313|Proteomes:UP000003179};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFS92575.1}.
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DR EMBL; ADZU01000019; EFS92575.1; -; Genomic_DNA.
DR RefSeq; WP_002546615.1; NZ_GL383180.1.
DR AlphaFoldDB; E4HJM1; -.
DR PATRIC; fig|765109.3.peg.1039; -.
DR HOGENOM; CLU_000404_3_0_11; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000003179; 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, 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}.
FT DOMAIN 9..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 854 AA; 94990 MW; 0B222EB1BF4887A7 CRC64;
MSADPISTIR VRKRDGSLAP YDGNEVAASI IDSARGLDDA VARATLLQAE VEITLFDGIT
TDALDEAVIQ VALGNAKDDP AFDTIASRIA VKKLYKEVFG NTHDSLGDVD PEQVHDLHRS
YFPRTIAKLV ADGYLDERLE RIFNLEALAA ALDPTRDDLI GFTGVRTMIN RYLLRTPDKK
ALEVPQYFWM RVAMGLSITE DDPTSSALTL YNSMSNLRHL AAGSTLVNAG TPSAQLSNCF
VMRTEDDLEH IAQTIRDVMW ITKGTGGIGL SMSDLRCEGS PIRSDNTAST GPIPFIHTID
STLRAVSRGG KKLGALCFYL ENWHLDFPQF LDLRQNSGDP YRRTRTADTA VWISDEFMKR
VAKDEDWYLF DPAETPDLTE LTGAAFSKRY AYYVAQAQAG KIKRFRRTTA REQFRTILVS
LQTTSHPWLT WKDSVNTRAL NNNTGTIHSS NLCTEICLPQ DRDHTSVCNL ASVNLAAHLV
GPRGKRRLNW DQLAATTRLA VRHLDNLVDI TASAVPQAQR SNEENRAIGL GVMGLTDMLE
QIRVPYDSPE ACEIVDRVVE FISWHAIDTS SDLATERGSY PMFEGSGWSR GMVPVDTLAV
LERDRGIPVD VDRTTRMDWD ALRAKVRTGI RNATLMAIAP TASIGFIAGT TPGLDPQFSQ
MFSRTTSAGK FLEVNRNLVA DLKDLGLWDS TREELLRRQG DPSEIDAIPA SLRHLYRTSF
TLDPIAYLNV AARAQKWVDQ AISRNIYLAS RSVGDMEDLY TAAWRMGVKT TYYLHMLPRH
TAEQSTVAVN KAAGRRNGPR RGFATTVRRS SRTATIEKPV IEEFDEVKPV SLNLIDGTTC
PVDPQERQQC ESCQ
//
