ID A0A0Q5M1D7_9MICO Unreviewed; 825 AA.
AC A0A0Q5M1D7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASF88_04585 {ECO:0000313|EMBL:KQR54111.1};
OS Leifsonia sp. Leaf336.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR54111.1, ECO:0000313|Proteomes:UP000050966};
RN [1] {ECO:0000313|EMBL:KQR54111.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54111.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR54111.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54111.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR54111.1}.
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DR EMBL; LMOZ01000001; KQR54111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5M1D7; -.
DR STRING; 1736341.ASF88_04585; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000050966; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050966}.
FT DOMAIN 1..89
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 795..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 92279 MW; 6386D8E5B78CDBF9 CRC64;
MKRNGEREPY DANKINLAIE NAAAGLDENI TWVTQIASEL ELTLFDGITT QQLDEAVIQV
ALQNVKDDPA FDTVAARLLL KTIYKRVLGD YEGFEELVEL HSSHFRGYIE RGVSETLLDS
RFTSLFDLDR LAGYLDPSRD ELLKYIGVVT LNNRYGIKAR NGDSLEVPQY FWMRIAMGLS
LNEANPTEHA IAFYDKMSKL EYLAAGSTLV NAGTAYPQLS NCFVMEMQDD IEHIAKSVRD
VMWLTKGTGG IGLSVTKLRA QGSPIRSNNT TSTGPIPFMH TIDSVLRAVS RGGKKFGALC
FYMENWHMDF PEFLDLRQNS GDPYRRTRTA NTAVWISDEF MKRVQNDEDW FLFDPLEVAD
LNELYGKEFS ERYAFYVAEA EAGRIKMFKK ISARSQFKDI LMSLQTTSHP WLTWKDTINN
RALNNNTGTI HLSNLCTEIT LPQDRDNVSV CNLASINLSR HLIDGKMDWE RIEASARQAV
RQLDNLIDIT VSSVDEADYS NQQNRAIGLG VMGFTDIVER LGFSYESEEA YALIDEIMEH
VSYAAIDESA DLAQERGAYP NFEGSRWSKG LVPYDSIALT EADRGIPITV DRTIRLDWDR
LREKVKGGMR NATLMAIAPT ASIGLVAGTT PGFDPQFSQI FSRSTSSGKF LEVNRNLVET
LQERGIWQDV RESILRSQGD IQGIAEIPDE VKATFKTSFQ LSPYAFIEVA ARAQKWIDQA
ISRNMYLETR DLGDMMDIYY AAWEKGVKTT YYLHMKPRHQ AEQSTVKVNK AEEISGGRKG
FATVGAGAPA AAPAVTETAP ATAPARRGFG FGGLTSNTPA GGESK
//
