ID A0A150JKQ0_9EURY Unreviewed; 778 AA.
AC A0A150JKQ0; A0A150JE34; A0A150JMK4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AN188_00165 {ECO:0000313|EMBL:KYC55512.1}, APG08_00128
GN {ECO:0000313|EMBL:KYC57658.1}, APG09_00198
GN {ECO:0000313|EMBL:KYC58452.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC57658.1, ECO:0000313|Proteomes:UP000092421};
RN [1] {ECO:0000313|Proteomes:UP000092420, ECO:0000313|Proteomes:UP000092421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADurb1013_Bin02101 {ECO:0000313|EMBL:KYC55512.1},
RC ADurb1113_Bin01801 {ECO:0000313|EMBL:KYC57658.1}, and
RC ADurb1213_Bin02801 {ECO:0000313|EMBL:KYC58452.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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:KYC57658.1}.
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DR EMBL; LNJB01000001; KYC55512.1; -; Genomic_DNA.
DR EMBL; LNJD01000001; KYC57658.1; -; Genomic_DNA.
DR EMBL; LNJE01000002; KYC58452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150JKQ0; -.
DR PATRIC; fig|1706433.3.peg.165; -.
DR PATRIC; fig|1706434.3.peg.127; -.
DR PATRIC; fig|1706435.3.peg.191; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000092420; Unassembled WGS sequence.
DR Proteomes; UP000092421; Unassembled WGS sequence.
DR Proteomes; UP000092422; 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:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
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.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 38..118
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 121..436
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 443..591
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 778 AA; 86620 MW; 34496A1B09E1B362 CRC64;
MNNSYICFGG IIISLAIPEN YSYDETSNND YAQEPLILSD NVIKVLERRY LKKDREGNVI
ETPNDLFLRV AKSIAIADLI YDDNANVESL TKDFYKMMTN FEFLPNSPTL MNAGRELGQL
SACFVLPVDD SIDSIFDAIK YTALIHKSGG GTGFSFSKLR PKNDVVLTTK GISSGPVSFM
TVFDTATETI KQGGTRRGAN MAILRVDHPD ILEFIRCKEE NTKLNNFNIS VAITDKFIEA
FENNKDYDLF NPRNGKVEGK LNAKEVFNFI VSMAWKNGEP GIVFIDRLNR GNPTPSIGEI
ESTNPCGEQP LLPYESCNLG SINLSKFLMK SSKGYEINFD HLRDIVKKSV HFLDNVIDIN
RYPLAQIEEM TKGNRKIGLG VMGFADMLLL MGIPYNSEDA VAIAKTVMKF IKEEATEASR
DLASKRGAFP NFEKSVFYDR GETPIRNATV TTIAPTGTIS LIANSSSGIE PIFAISYIRN
VMDKDELLET NPVFAEISKK RGIYSQELMK RIAKEGSIKN IAEIPEDIKK IFVTAHDISP
EWHIRIQAAF QEFTDNAVSK TINFPKSANE KEVMQAYLLA YKSGLKGITI YRDGSREEQV
LNIGKVNKKE ITNSSQKAPR PRPKVTKGFT EKIRTGCGNL YVTINEDEYG LCEIFMQMGK
SGGCPASQNE AIARLISLAL RSGIRIETIL EQLKHIRCPM PTWDEGIPVH SCADAIAIVL
DRYIKKELDT KQERLDVVVT SNGGANNNGM PAQCPECGEV LVFSEGCVNC KCCGYTKC
//
