ID U7LGU0_9CORY Unreviewed; 720 AA.
AC U7LGU0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HMPREF1281_00030 {ECO:0000313|EMBL:ERS58208.1};
OS Corynebacterium sp. KPL1855.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203562 {ECO:0000313|EMBL:ERS58208.1, ECO:0000313|Proteomes:UP000017096};
RN [1] {ECO:0000313|EMBL:ERS58208.1, ECO:0000313|Proteomes:UP000017096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1855 {ECO:0000313|EMBL:ERS58208.1,
RC ECO:0000313|Proteomes:UP000017096};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1855.";
RL Submitted (OCT-2013) 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:ERS58208.1}.
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DR EMBL; AXLX01000002; ERS58208.1; -; Genomic_DNA.
DR RefSeq; WP_023023724.1; NZ_KI515741.1.
DR AlphaFoldDB; U7LGU0; -.
DR PATRIC; fig|1203562.3.peg.26; -.
DR HOGENOM; CLU_000404_4_1_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000017096; 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 572..594
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 720 AA; 81670 MW; 0F3385952B38756C CRC64;
MSTQLGKTVA EPVSQEEQLD YHALNAMLNL YDGDGKIQFD KDREAANQFF LQHVNQNTVY
FHDLEEKIDY LVRNKYYDPA VIEAYDFEFI KSLFKRAYSY KFRFKSFLGA YKYYTSYTLK
TFDGRRYLER FEDRVSMTAL FLGDGDGELA ERLVDEIMTG RFQPATPTFL NAGKQQRGEL
VSCFLLRIED NMESIGRSIN SALQLSKRGG GVALLLSNIR ESGAPIKHIE NQSSGVIPVM
KMLEDAFSYA NQLGARQGAG AVYLNAHHPD IMNFLDTKRE NADEKIRIKT LSLGVVIPDI
TFELAKNNDD MYLFSPYDVE RVYGKAFGDI SVTEHYEEMV EDPRIRKKKI NARHFFQTVA
ELQFESGYPY IMYEDTVNRA NPVKTSRINM SNLCSEILQV NSASELNADL SYDQVGNDIS
CNLGSLNIAM TMDSPDFSQT VETAIRGLTS VADKTSIDSV PSVRKGNDDS HAIGLGQMNL
HGYLGREHIE YGSEEGLDFT NAYFAAIMYA ALRASNKIAR ERDTTFTEFP ESDYASGEFF
DSYDPAEFQP RTEKVKALFD ASSIYTPTAE DWAELKEDVA KHGLYNRNLQ AVPPTGSISY
INNSTSSIHP IASKIEIRKE GKIGRVYYPA AHMDNDNLEY FKDSYEIGYE KIVDTYAEAT
KYVDQGLSLT LFFKDTATTR DVNKAQIYAW RKGIKTLYYI RVRQMALEGT EIEGCVSCML
//
