ID A0A218KMI6_9RICK Unreviewed; 594 AA.
AC A0A218KMI6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ASM33_00985 {ECO:0000313|EMBL:APR97898.1};
OS Wolbachia endosymbiont of Folsomia candida.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=169402 {ECO:0000313|EMBL:APR97898.1, ECO:0000313|Proteomes:UP000247300};
RN [1] {ECO:0000313|EMBL:APR97898.1, ECO:0000313|Proteomes:UP000247300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berlin {ECO:0000313|EMBL:APR97898.1,
RC ECO:0000313|Proteomes:UP000247300};
RX PubMed=28659179; DOI=10.1186/s12864-017-3852-x;
RA Faddeeva-Vakhrusheva A., Kraaijeveld K., Derks M.F.L., Anvar S.Y.,
RA Agamennone V., Suring W., Kampfraath A.A., Ellers J., Le Ngoc G.,
RA van Gestel C.A.M., Marien J., Smit S., van Straalen N.M., Roelofs D.;
RT "Coping with living in the soil: the genome of the parthenogenetic
RT springtail Folsomia candida.";
RL BMC Genomics 18:493-493(2017).
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; CP015510; APR97898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218KMI6; -.
DR KEGG; weo:ASM33_00985; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000247300; Chromosome.
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}.
FT DOMAIN 13..78
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 82..400
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 411..556
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 594 AA; 67951 MW; CDAB36C21B989283 CRC64;
MNNITINYEK DSKLTDFGKA VLSDRYLIEN ESYQDLFIRI ANYYSDDKEH AQRLYDYMSN
LWFMPSTPIL SNGGTKRGLP ISCFLNETED SLQGIVDLWN ENVWLAARGG GIGSYWGNLR
SIGESVKGSG KTSGIVPFIV VQNALTLAIS QGSLRRGSSA VYLPIWHPEI EEFLDLRKPT
GGDPNRKALN IHHAVMVTDK FMQAVENDQE WDLISPHNNK VISTVKARDM WIKILTARIE
TGEPYIIFLD ATNNNKPESY KKLNLDIKMS NLCSEITLTT GYDHLNNSRT AVCCLSSVNL
EYYEEWKDNK LFIEDIMRFL DNVLEDFINK APDEMKRAKY SAMRERSIGL GVMGFHSFLQ
SKMVPFESVA AQQWNKKIFK YLREQADIVS KKLAEEKGSC LDAQEINLLE RFTHKLAIAP
TASISIIAGN TSPGIEPYAA NVFIQKTLTG SFVVRNKFLQ KLLAEKNQDN DKIWSSISTN
EGSVQHLDFL SEHEKLAFKT AYELDQRWII EHASDRTPYV CQSQSVNLFL AANVHKRYLH
KIHMLAWRKG LKSLYYCRSQ SMQRADKVSH DIFKKSEILQ QKTDINYDEC ISCQ
//
