ID A0A0Q5P951_9SPHN Unreviewed; 635 AA.
AC A0A0Q5P951;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ASG07_08740 {ECO:0000313|EMBL:KQR83324.1};
OS Sphingomonas sp. Leaf343.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR83324.1, ECO:0000313|Proteomes:UP000051323};
RN [1] {ECO:0000313|EMBL:KQR83324.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83324.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR83324.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83324.1,
RC ECO:0000313|Proteomes:UP000051323};
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:KQR83324.1}.
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DR EMBL; LMPG01000012; KQR83324.1; -; Genomic_DNA.
DR RefSeq; WP_055845162.1; NZ_LMPG01000012.1.
DR AlphaFoldDB; A0A0Q5P951; -.
DR STRING; 1736345.ASG07_08740; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051323; 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; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
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; 2.
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.
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:UP000051323}.
FT DOMAIN 53..118
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 122..440
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 450..596
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 635 AA; 70168 MW; 33B42E90B5B16066 CRC64;
MDFSNDRGAA TDTIEAPAAA GVAAPRPAPV ALDSKSVAPQ PYALEVDHSR DALLTDFGKE
TLNDRYLLPG ESYQDLFVRV ASAYADDVAH AQRIYDYISR LWFMPATPVL SNGGTGRGLP
ISCYLNSVPD SLNGIVDTWN ENVWLASRGG GIGTYWGNVR GIGEPVGLNG KTSGIIPFVR
VMDSLTLAIS QGSLRRGSAA CYLDISHPEI EEFLEIRKPS GDFNRKALNL HHGVLIPDAF
MEAVRDGAEW ILRSPKDQSE RGKVDARALF QKLVETRLAT GEPYIVFADH VNSTMPAHHR
QLGLKVSTSN LCSEITLPTG KDHLGNDRTA VCCLSSLNLE TWDQWKDDKM FVEDVMRFLD
NVLQDYIDRH EPGMERAAYS AGRERSVGLG VMGFHSFLQA RGIAFEGAMA KSWNLRIFKQ
INAQVNEASM QLAVERGPCP DAADVGVMER FSCKMAIAPT ASISIICGGT SACIEPIPAN
IYTHKTLSGS FSVKNPYLEK LLNEKSKNTE AVWNSMLENG GSVQHLDFLS QEEKDCYKTS
FEIDQRWLLE LAGDRTPYID QAQSLNLFIP ADVEKWDLLM LHFRAWELGI KSLYYLRSKS
VQRAGFAGGV EADNTIAKPK FELESTDYDE CLACQ
//
