ID A0A401Z8V5_9CHLR Unreviewed; 1151 AA.
AC A0A401Z8V5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=KDAU_06290 {ECO:0000313|EMBL:GCE03300.1};
OS Dictyobacter aurantiacus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=1936993 {ECO:0000313|EMBL:GCE03300.1, ECO:0000313|Proteomes:UP000287224};
RN [1] {ECO:0000313|Proteomes:UP000287224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-27 {ECO:0000313|Proteomes:UP000287224};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) 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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {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:GCE03300.1}.
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DR EMBL; BIFQ01000001; GCE03300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Z8V5; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000287224; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000287224}.
FT DOMAIN 399..542
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 631..653
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 126968 MW; 5634CE5F22094E02 CRC64;
MLEQEARSVE NSGDNGKSTM TQLEGIRQKV FMDRYSLKDP DGKALEFYPE QMWQRVARGI
AEVEKTDEKR AEWEKLFNEA LTNFQFVPGG RILAGAGTGH QVTYYNCYVI PSPEDSRQGI
LDNLKVMTEI MARGGGVGIN LSTLRPRGSY IKTVNGTASG PCSWAQLYSV ATGDVIQQGG
SRRGALMLML DDTHPDIEEF ITVKRTAGKI EHANLSVCIS DAFMQAVKDD ADWNLIWQGE
VKKTIRAREL WDLICTSAWE SAEPGLVFMD RYNKESNTWY YENIRCVNPC VTGDTLIYTD
NGLFPASELA EIGTPITVVS SNEDGVALRQ ASHVFPTGVK PVYRLQTSEG YTIRLTKDHK
VLTVNGWKEA GELVAGDKIK LLNGEGHFGT TGNQDLGYVL GWLVGDGYIN TKREGSAVLS
FFGSEQSIAP RFAESVNRLV SSPEGQRQYQ VGTLKVAGRE ETRVESVRLL RLIDPELLVN
KLQVPPSVFR GSHEMQKGFL AALFTADGSV QGSIEKGASI RLTSIDQHLL EGVQQLLLNF
GIYSRIYTER REAGERNLPD GKGGSAPYNC QTYHDLVISK GSFVAFARQI GFLIQEKQTK
LEDLIAAYQR GPYKEEFVAT FESLLADGEE TVYDLTEPQD HRFIANGLVV HNCGEQGLPP
FGVCNLGAIN LSAFVKDGTM DYERLAHISK IAMRFLDNVI DSTEYFIKEN AEAQLGTRRT
GLGTMGLADA LIKMEVAYGS EQSIPIIERI YTTIRNAAYE ASADNAAEKG AFPKFDRDKY
IQGKFIKRLP KNLQEKIRKQ GTRNAVILTQ APTGTTSLLA GVSSGIEPVY DFAMIRRDRT
GEHIMYHPLL QAWRDAHPNE PTPDYFVSSK DLTPEEHVRV QGMIQRYTDS SISKTVNAPN
NHTVEQVQTL YRLAYEMGCK GVTYYRDGSR DAVLTRVEDE QKARQSAATP ETAPAPMFEP
VTSIQQGIKQ RPAVVQGYTR QVVAPEGKIN ITINSDEHGP FEVFVNVGKA GSDIAALSEA
LGRLISINLQ LLSPLSQTDR AQEITNQLRG IGGSRSVGFG AQQVRSLPDA VARALELHLD
TLQEAINTAE SHTEVKASAA VPPLAPANGH SSDVNLSQLK LTGNLCPECG CNTMVYEEGC
RKCYSCGHSE C
//
