ID A0A135VGA7_9ARCH Unreviewed; 1001 AA.
AC A0A135VGA7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AM325_02495 {ECO:0000313|EMBL:KXH71726.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706444 {ECO:0000313|EMBL:KXH71726.1, ECO:0000313|Proteomes:UP000070149};
RN [1] {ECO:0000313|EMBL:KXH71726.1, ECO:0000313|Proteomes:UP000070149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-45 {ECO:0000313|EMBL:KXH71726.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
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:KXH71726.1}.
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DR EMBL; LRSL01000086; KXH71726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VGA7; -.
DR STRING; 1706444.AM325_02495; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000070149; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR005144; ATP-cone_dom.
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 PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
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; PS51161; ATP_CONE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 458..591
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 681..703
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1001 AA; 111731 MW; A7F3503DFC35D19C CRC64;
MKVEKRDKRI VEFDDSKIEA AITKAFESIN ADTGPVRGLT KEVVQIIHEK ERDVIHIEEI
QDIVEDTLML RGFTEIARRY MKYREKHNEA RKILQMMGVV DDLKFGPNAA TVLSRYLLKD
EEGNPTETPS QLFRRVSGAV ASIEKKYDKN ADVREYDDLF YYMMANLEFL PNSPTLFNAG
TEIGQCSACF VLPIEDNMDS IFTSLKHMAV VQKSGGGTGF SFSRLRPVGS TVGTTGGVAS
GPISFMRVYD TATEIIKQGG RRRGANMAIL RCDHPDIMEF IACKSDKQTF RNFNISVALT
SEFINALQGD KEINLVAPHN GVKIQSIRAR VIFDAIVYNA WSTGDPGIVF IDRINDEHPL
GGELIESTNP CVSGNTIVST DVGLLSIQDV PGVIKTAKKL VYCLKTKEGY QVKVTNDHRI
LTTTGWKQAG DLSKGDFICL QSTEGGFGKT GNLRIGQILG WYVGDGWNTG TDQRATLAFY
GDDKGKLAQY FCDIVNEELE SDLVVIKSKN REEVRSRRIL NLVQEWGMES KEISNPILSS
SADCQRGFLQ GLFTADGSIQ GKPEKGISVR LSQSNLDSLR SVQIMLLNFG IASKIYDNRR
REQMRLLPDS KGEPKHYKTK ANHELVISKE NIVKFRDQIG FLLEYKQSRL VKGLDSLSIR
GPYKENFLAR FESLTPQLEE DVFDIVGTPH CGFVGNGIVV HNCGEQPLMP YESCVLGSIN
LSRMVKDGEI DWSRLEEVVK LAVRFLDNII DLNVYPVLEI EQVTKANRKI GLGIMGFAEL
LIKLRNPYDS EKGLEKAEEV MSFIRQKAER ASSELAKIRG NFENFALLKK RNRWKRNASL
ITVAPTGSIS LIAQTSSGIE PLFAIAHSRM LAEGIHLSEV SPLFERVAVE RGFWNDEIEH
EVARSGSVQQ IDGVPDDIKQ VFKAAHEISP EWHVRMQAAF QKHTDNAVSK TVNLPNSATT
EDVEQIFLLA NQLGLKGTTV FRDGCLGGVQ VLYPGCQNCD S
//
