ID M1LN71_9PROT Unreviewed; 959 AA.
AC M1LN71;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=CDSE_0041 {ECO:0000313|EMBL:AGF47162.1};
OS Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF47162.1, ECO:0000313|Proteomes:UP000011547};
RN [1] {ECO:0000313|EMBL:AGF47162.1, ECO:0000313|Proteomes:UP000011547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC079E {ECO:0000313|EMBL:AGF47162.1,
RC ECO:0000313|Proteomes:UP000011547};
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; CP003803; AGF47162.1; -; Genomic_DNA.
DR AlphaFoldDB; M1LN71; -.
DR STRING; 1208919.CDSE_0041; -.
DR KEGG; kde:CDSE_0041; -.
DR PATRIC; fig|1208919.3.peg.605; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000011547; 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}.
FT DOMAIN 31..131
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 148..238
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 959 AA; 109731 MW; DAC9308DD9153F28 CRC64;
MHNKTNIIID INHQEDPLPS LNNDNERWLK YKIIRRNGSI VSFAPYKIST AITKAFIAVR
NEQISLSIGD RELIEKLTFQ VINALTRNKS DTAIFHIEDV QDHVELSLMR SGLHDVARAY
VLYREKRNQA RAIELSNIQK EQEFEFPTIN ILENGKKHKL DINRLKSIIQ SAYNGFEHKL
DLKDIIKDTL KNLYDGIHIN EVFKSIIFTT RARIEKDPDY NYITARLLLN TIIKEVIGED
IVSSDLNTQY KKYFPEFIEK GLESGLLAPE MSTYDLNKLG SVLDYKKDLK FKYLGLQTLY
DRYFLHIDGK RIELPQIFFM RVAMGIAINE PQKDDKAIEF YEILSSFDFM SSTPTLFNSG
TKHSQMSSCY LTTVPDNLIG IYDAIKENAL LAKYAGGLGN DWTPVRALRS HIKGTNGESQ
GVVPFLKVVN DTAVAVNQGG KRKGAVCTYL ETWHLDIEEF LELRKNTGDE RRRTHDMNTA
NWIPDLFMKR VHENLDWTLF SPSDCPDLHE KYGKEFEIAY IQYENKTTTG EIKLFKKLPA
VTLWRKMLSM LFETGHPWIT FKDPCNIRSP QQHDGIIHSS NLCTEITLNT NNNEIAVCNL
GSINLVNHLK KSNNGYFYLD VEKIQKTITT AMRMLDNIID INYYAVSKAE ISNRKHRPVG
LGLMGFQDCL HLMRIPYSSQ EAVDFSDKST EILCYYSYLA SSNLSKERGS YNSYNGSLWS
KGIMPHDTLK TLLDEREGYL DVDVSSSLDW DYLRNNIKKY GMRNSNCVAI APTATISNII
GVSASIEPNF QNLYVKSNLS GEFTIINEYL VEDLKKLGLW DQVTIADLKY FDGSLAKIDR
IPASIKELYN TAFEIEPEWL IHCASRRQKW IDQAQSLNIY MSGVSGKKLD EIYKLAWIKG
LKTTYYLRTL AATSAEKSTG KGGELNSVRA DISHITSPNN KNISCPINRS DDSECEVCQ
//
