ID A0A127NVG4_9CORY Unreviewed; 720 AA.
AC A0A127NVG4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=WM42_1904 {ECO:0000313|EMBL:AMO89612.1};
OS Corynebacterium simulans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO89612.1, ECO:0000313|Proteomes:UP000074804};
RN [1] {ECO:0000313|EMBL:AMO89612.1, ECO:0000313|Proteomes:UP000074804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PES1 {ECO:0000313|EMBL:AMO89612.1,
RC ECO:0000313|Proteomes:UP000074804};
RX PubMed=26861018;
RG NISC Comparative Sequencing Program;
RA Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J., Oh J.;
RT "Resolving the Complexity of Human Skin Metagenomes Using Single-Molecule
RT Sequencing.";
RL MBio 7:e01948-15(2016).
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}.
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DR EMBL; CP014634; AMO89612.1; -; Genomic_DNA.
DR RefSeq; WP_062037398.1; NZ_CP014634.1.
DR AlphaFoldDB; A0A127NVG4; -.
DR STRING; 146827.WM42_1904; -.
DR KEGG; csp:WM42_1904; -.
DR PATRIC; fig|146827.5.peg.1870; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000074804; Chromosome.
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; 81556 MW; F5D3344ABAB3D459 CRC64;
MTTQLGKTVA EPVKPEEQLD YHALNALLNL YDEEGKIQFD KDHEAANQFF LQHVNQNTVY
FHDLEEKMRY LVENKYYEPA LLEQYDFDFI KSLFKRAYSY KFRFKSFLGA YKYYTSYTLK
TFDGRRYLER FEDRVSMTAL FLADGDTTIA EHLVDEIMTG RFQPATPTFL NAGKAQRGEL
VSCFLLRIED NMESIGRSIN SALQLSKRGG GVALLLSNIR EAGAPIKHIE NQSSGVIPVM
KLLEDSFSYA NQLGARQGAG AVYLNAHHPD IMNFLDTKRE NADEKIRIKT LSLGVVIPDI
TFELAKNNDD MYLFSPYDVE RVYGKAFGDI SITEHYEEMV EDPRIRKKKV NARHFFQTIA
ELQFESGYPY IMFEDTVNNA NPVKTGRINM SNLCSEILQV NSPSVFADDL SYETMGSDIS
CNLGSLNIAT TMDSPDFALT VETAIRGLTA VADKTAINSV PSVRKGNDDS HAIGLGQMNL
HGFLGREHIE YGSEEALDFT NAYFAAVLYA ALRASNKIAR ERGEYFSEFP QSEYASGEFF
DRYDPAEFAP RTARVQELFD ASSIHTPTAE DWAALKADVA KHGLYNRNLQ AVPPTGSISY
INNSTSSIHP IASKIEIRKE GKIGRVYYPA PHMDNDNLEY FKDSYEIGYE KIIDTYAAAT
KYVDQGLSLT LFFKDTATTR DINRAQIYAW RKGIKTLYYI RLRQMALEGT EVEGCVSCML
//
