ID A0A401ZYW4_9CHLR Unreviewed; 1557 AA.
AC A0A401ZYW4;
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|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=KTT_18980 {ECO:0000313|EMBL:GCE12039.1};
OS Tengunoibacter tsumagoiensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Tengunoibacter.
OX NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE12039.1, ECO:0000313|Proteomes:UP000287352};
RN [1] {ECO:0000313|Proteomes:UP000287352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
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|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:GCE12039.1}.
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DR EMBL; BIFR01000001; GCE12039.1; -; Genomic_DNA.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000287352; 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; 2.
DR Gene3D; 3.20.70.20; -; 3.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 3.
DR Gene3D; 3.10.28.10; Homing endonucleases; 2.
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 NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 2.
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; 2.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR SUPFAM; SSF55608; Homing endonucleases; 2.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 2.
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:UP000287352}.
FT DOMAIN 324..461
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 806..949
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1038..1060
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 1557 AA; 171489 MW; 28D5C7D56CF0C61C CRC64;
MLEQIERLSS DDDNDNPQTM TQLEGIRQKV FMDRYSLKDP DGNPLEFYPE QLWKRVARGI
AAVEQTEEKR AEWEKLFYEA LNNFQFVPGG RILAGAGTGH QVTYYNCFVI PSPEDSRQGI
LDNLKVMTEI MARGGGVGIN LSTLRPRGSY IKTVNGTASG PCSWAQLYSV ATGDVIQQGG
CFGPNERIST SKGLIPASEL ADRLDAGESF EALTHKGWRA FNYVFRNGTK DLYEVTTSRG
YRVRVTLDHK MGVLRNGEIT TIALRDLAEG DEILLLLGEY DADAPADSEP VQLSTTPYER
SLLSTTLDEQ VTVPTQLTAE LAYLLGFSYG DGHVMGDRGL SLSVANNQPE VQERLVASIR
SLFGIEPAVS AGDDTNNTNI QLDSRVVVEW LHENGLLTQK AETIRVPEAI FRSPADVVEA
FIAGFFATDG YDRRANSGYG IDSISRELLG DIQLLLLNQG VVSHITVQHR AAQGWQPIYR
LIVTGAHFKK RFSAFVQSFE DQGYSGLRSH QSFFKGTKDR VSPYALTRVR ERVAAAGGVA
MVERLDALLG VLPDPIVSIE PLGPSEVFDF EVDDVHLLAG NGLYTSNSRR GALMLMLDDT
HPDVEEFITV KRTAGKIQHA NLSVCISDAF MQAVKDDADW NLTWQGEVKK TIRARSLWDL
ICTSAWESAE PGMVFMDRYN KESNTWYYEN IRCVNPCVTG DTLVYTDQGM IPASELAEMG
APVTVVSPDS ENVALRQASH VFSTGVKPVF RLQTEEGYTI RLTEDHKVLT TGGWKEAGTL
NTGDKIKLLH AEGYFGTTGN ADLGRVLGWL VGDGSINTRR AGSVMLSFFG KEQAIAPQFA
EAVNRLVAAP EGQRQYVVGA QKVADRDETR VESVRLLRLI DPELLSNKLQ VPPSVFRGSH
EMQKGFLSAL FTADGSVQGN LEKGASIRLT SVNQQLLEGV QQLLLNFGIY SRIYTELREA
GSRELPDGKG GSASYECQSY HDLVITKGSF SAFAHQISFL TQEKQSKLED LVAAYKRGPY
KEDFTATFVS LTAEGEEMVY DLTEPEAHLF VANGLVVHNC GEQGLPPWGV CNLGALNLSA
FVSHGEMDWE KLAQISKIAM RFLDNVVDAN EYFIAENREA QLSTRRTGLG TMGLADALIK
MKVAYGSDAS LPIIERIYAT IRDASYEASA DNAAEKGSFP MFDREKYLQG KFIQRLPQPI
QEKIANQGIR NAVLLTQAPT GTTSLLSGAS SGIEPVYDFA MIRRDRTGEH ILYHHLLQEW
RDEHPNEATP DYFVASKDLT PEEHVRVQSM IQRYTDSSIS KTVNAPNEHT VEDVQNLYRL
AYEMGCKGVT YYRDGSRDAV LTRVEDEKKA AEKAEKAAQA QAPMFEPVTS IHQGIKQRPS
VVQGYTRQVR APEGKINITI NSDDQGPFEV FVNVGKAGSD IAALSEALGR LISLNLQLLS
PLSQTDRAQE ITNQLRGIGG SRSVGFGVQQ VRSLPDAVAR ALEIHMEALN EAPETVAPAP
APVSKVTEEP VAESHVSAPV NLNQLRVTGN LCPQCGCNTM VYEEGCKKCY SCGHSEC
//
