ID A0A1B1BFS6_9MICO Unreviewed; 714 AA.
AC A0A1B1BFS6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=PA27867_0362 {ECO:0000313|EMBL:ANP71336.1};
OS Cryobacterium arcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=670052 {ECO:0000313|EMBL:ANP71336.1, ECO:0000313|Proteomes:UP000092582};
RN [1] {ECO:0000313|EMBL:ANP71336.1, ECO:0000313|Proteomes:UP000092582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27867 {ECO:0000313|EMBL:ANP71336.1,
RC ECO:0000313|Proteomes:UP000092582};
RA Lee J., Kim O.-S.;
RT "Genome sequencing of Cryobacterium arcticum PAMC 27867.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016282; ANP71336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1BFS6; -.
DR STRING; 670052.PA27867_0362; -.
DR KEGG; cart:PA27867_0362; -.
DR PATRIC; fig|670052.7.peg.383; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000092582; Chromosome 1.
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 566..588
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 714 AA; 80540 MW; 00EA894399865337 CRC64;
MKVTPISPPS GLDMDYHSLN AMLNLYGPSG EIQFDKDREA AREFFLQHVN QNTVFFHSLR
ERLDYLVEKE YYEQAVLDMY SFEFITRLND LAYSKKFRFQ TFLGAFKYYT SYTLKTFDGK
RYLERFEDRV VMTALGLAQG DENLAVALVE EIIAGRFQPA TPTFLNSGKA QRGELVSCFL
LRIEDNMESI SRGINSSLQL SKRGGGVALL LSNIRESGAP IKQIENQSSG IIPVMKLLED
SFSYANQLGA RQGAGAVYLQ AHHPDIMRFL DTKRENADEK IRIKTLSLGV VIPDITFELA
KNNEDMYLFS PYDVERVYGV PFADISVTEK YHEMVDDPRI KKSKMKARDF FQTLAEIQFE
SGYPYIMFED TVNEANPIKG RVNMSNLCSE ILQVNTPTTY NEDLSYDTIG KDISCNLGSM
NIALAMDAPD FGRVVDTAIR GLSAVSDQSH IASVRSIESG NDKSHAIGLG QMNLHGYLAR
ERVYYGSEEG IDFTNIYFYT VLFHALRASN KIAIERGITF EGFADSTYAS GTFFDKYTDQ
VWEPATARGA ELFANSNVEI PTQADWAELK ASVMEHGIYN QNLQAVPPTG SISYINNSTA
SIHPIASKIE IRKEGKLGRV YYPAPFMTND NTEFYQDAYE IGYEKVIDTY AAATQHVDQG
LSLTLFFKDT ATTRDINRAQ IYAWKKGIKT IYYIRLRQMA LEGTEVEGCV SCAL
//
