ID A0A0B2AJJ0_9MICC Unreviewed; 706 AA.
AC A0A0B2AJJ0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LK10_14165 {ECO:0000313|EMBL:KHL01932.1};
OS Sinomonas humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL01932.1, ECO:0000313|Proteomes:UP000030982};
RN [1] {ECO:0000313|EMBL:KHL01932.1, ECO:0000313|Proteomes:UP000030982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL01932.1,
RC ECO:0000313|Proteomes:UP000030982};
RA Lee L.-H.;
RT "Genome sequence of Sinomonas sp. MUSC 117.";
RL Submitted (SEP-2014) 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:KHL01932.1}.
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DR EMBL; JTDL01000136; KHL01932.1; -; Genomic_DNA.
DR RefSeq; WP_043124973.1; NZ_JTDL01000136.1.
DR AlphaFoldDB; A0A0B2AJJ0; -.
DR STRING; 1338436.LK10_14165; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000030982; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030982}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 706 AA; 80436 MW; 9CAEFE238D09C14C CRC64;
MPEKFKGLGY HELNAMLNLY GEDGRIQFEA DRYAARQYFL DHVNTNTVFF HDLDEKLEYL
VKHDYYERET LDQYTMNFIR ELFSRAYKKK FRFETFLGAF KFYTSYTLKT FDGKRYLERY
EDRVCMVALH LARGDEQLAT QLVDEIIAGR FQPATPTFLN AGKKQRGELV SCFLLRIEDN
MESIARGINS ALQLSKRGGG VALSLTNIRE HGAPIKQIEN QSSGVIPVMK LLEDSFSYAN
QLGARQGAGA VYLHAHHPDI YRFLDTKREN ADEKIRIKTL SLGVVIPDIT FELAKRNEDM
YLFSPYDVER VYGVPFSDVS VSEKYYDMVD DSRIKKTKIN AREFFQTLAE IQFESGYPYI
MFEDTVNRAN PVAGKVTMSN LCSEILQVSS PSLYNEDLTY AQVGKDISCN LGSMNIAKTM
DSGDFGLSIE TAIRALSAVS DMSYIQSVPS VAEGNAKSHA IGLGQMNLHG YLARERVHYG
SEEGLDFTNI YFYTVLFHAL RASNLLAQEH GQAFGGFENS KYASGEFFDK YTEREWAPQT
EKVRELFANV HVPTQDDWRA LKASVMEHGI YNQNLQAVPP TGSISYINNS TSSIHPVASK
IEIRKEGKIG RVYYPAPYLT NDNLEYYQDA YEIGYEKIID TYAAATQHVD QGLSLTLFFK
DTATTRDVNK AQIYAWRKGI KTLYYIRIRQ LALEGTEVEG CVSCML
//
