ID A0A0Q7L641_9BURK Unreviewed; 970 AA.
AC A0A0Q7L641;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ASD34_03570 {ECO:0000313|EMBL:KQX90353.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX90353.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX90353.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX90353.1,
RC ECO:0000313|Proteomes:UP000051275};
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:KQX90353.1}.
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DR EMBL; LMEV01000014; KQX90353.1; -; Genomic_DNA.
DR RefSeq; WP_056575595.1; NZ_LMEV01000014.1.
DR AlphaFoldDB; A0A0Q7L641; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051275; 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; 2.
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:UP000051275}.
FT DOMAIN 36..136
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 150..239
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 107915 MW; D9A9C9C347CFECDB CRC64;
MQTALNTPST PRAVPATPQQ QQDTAGSPTG QNLAHYQIIR RNGAVVPFEP NKIAIAMMKA
FLAVHGTQGA ASASVRETVD TLTQGVIRAM VRSRPGGGTF HIEDVQDQVE LGLMRGGHHE
IARAYVLYRE RRTQERSKQV EQEAPATPTL HVLDNGERVA LDLNQLKGLI ESACENLGDS
ITAAPIVAET MRNLYDGVPL DEVYKASILA ARTLIEKDPD YTFATARLLL HTIFKEIIGR
EVMPVDRATA YADYFPQFIK KGVENDLLDE KLLQYDLPRL GAALKAERDN QFDYLGLQTL
YDRYFLHVRK TRIELPQAFF MRVAMGLSLG EIDREARAIE FYEVLSSFDF MSSTPTLFNA
GTLRSQLSSC YLTTVPDDLD GIYESIKENA LLSKFAGGLG NDWTRVRALG SHIKGTNGES
QGVVPFLKVV NDTAVAVNQG GKRKGAVCTY LETWHLDIEE FLELRKNTGD DRRRTHDMNT
ANWIPDLFMR RVMEKGTWTL FSPSNVPDLH DLFGADFEKA YVAYEEKAAR GEIKPARTIQ
ASDLWRKMLT MLFETGHPWI TFKDACNVRS PQQHAGVVHS SNLCTEITLN TSDTETAVCN
LGSVNLLQHL KDGKVDQEKL KRTISTAMRM LDNVIDINYY AVKKARDSNL RHRPVGLGLM
GFQDALYELR IPYASQEAVQ FADESMEAIC YHAYWASTEL ARERGKYSSY KGSLWDKGIL
PIDSLDLLEK ARGGYVEVDR SSTLDWDTLR QKIKADGMRN SNCVAIAPTA TISNIIGVDA
SIEPCFGNLS VKSNLSGEFT VINHYLVRDL KRLGLWDDVM VMDLKHFDGS LRPIDRVPQD
VKALYATAFE VETTWLVEAA ARRQKWIDQA QSLNIYMAGA SGKKLDDTYK LAWLRGLKTT
YYLRTQSATH AEKSTVQSGR LNAVSSGNDA PSGMSALEAA AAAAKAQMSA IPATDIAFCG
VDDPTCEACQ
//
