ID M1LXG1_9PROT Unreviewed; 940 AA.
AC M1LXG1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=CDEE_0045 {ECO:0000313|EMBL:AGF47894.1};
OS Candidatus Kinetoplastibacterium crithidii TCC036E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208918 {ECO:0000313|EMBL:AGF47894.1, ECO:0000313|Proteomes:UP000011686};
RN [1] {ECO:0000313|EMBL:AGF47894.1, ECO:0000313|Proteomes:UP000011686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC036E {ECO:0000313|EMBL:AGF47894.1,
RC ECO:0000313|Proteomes:UP000011686};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003804; AGF47894.1; -; Genomic_DNA.
DR AlphaFoldDB; M1LXG1; -.
DR STRING; 1208918.CDEE_0045; -.
DR KEGG; kct:CDEE_0045; -.
DR PATRIC; fig|1208918.3.peg.594; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000011686; Chromosome.
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:UP000011686}.
FT DOMAIN 15..115
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 131..222
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 940 AA; 106794 MW; 3B3E4F4FB5367D8D CRC64;
MFSTKDGSEN QWMKYKVIRR DGSVVYFTPH KISTAMAKAF IAVRNEQNTL SISNRELIEK
LTSQVVTALI RNKTDGATFH IEDIQDQVEL SLMRSGLHDV ARSYVLYREK RNQARKTEHN
FSPLQPKNEF QSIIVEDSGI KRQLDIDKLK SIIKSAYTNF ESLLDIEGIL KETIRNLYNG
IKISEVFKSL ILTTRAKIEK EPAYNYITAR LLLHTIRKEV LGKELNHEDM ATEYKEAFES
FIKKGISSGL LSPNMGSYDL KKLGNALDHN RDLKFKYLGL QTLYDRYFLH INNTRIELPQ
IFFMRVAMGI ALKENYKEEK AIEFYEILSS FDFMSSTPTL FNSGTKHSQM SSCYLTTVPD
SLEGIYDAIK ENALLAKYAG GLGNDWTPVR ALRSHINGTN GESLGVVPFL KVVNDTAVAV
NQGGKRKGAV CTYLETWHLD IEEFLELRKN TGDERRRTHD MNTANWIPDL FMKRVHENKE
WTLFSPSDCP DLHDKYGKEF EISYTDYEKK TISGEIKLFK KISAVILWRK MLSMLFETGH
PWIAFKDPCN IRSPQQHVGV IHSSNLCTEI TLNTSDSEIA VCNLGSVNLV NHLKESKNGN
LELDLDKLQK TVNIAMRMLD NIIDINYYAV SKAKTANEKH RPVGLGLMGF QDCLHIMKIP
YSSQEAVSFS DKSTEALCYY AYLASSNLSK ERGRYSSFDG SLWSKGIMPH DSLELLLKER
GDYLDIDNST SLDWNSLRSH ILKHGMRNSN CVAIAPTATI SNIIGVSASI EPTFQNLYVK
SNLSGEFTII NEYLVEDLKK LDLWDQVTIS DLKYFDGSLS KIDRIPNFIK TIYKTAFEIE
PNCLIECAAK RQKWIDQAQS LNIYMNGASG KKIDETYKLA WTKGLKTTYY LRTLGATSVE
KSTGNGGELN SVSIANNSTE DTKPTCSIGN NSYEECEVCQ
//
