ID A0A0G1DMU6_9BACT Unreviewed; 706 AA.
AC A0A0G1DMU6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=UV74_C0001G0007 {ECO:0000313|EMBL:KKS98897.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_43_14.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618578 {ECO:0000313|EMBL:KKS98897.1, ECO:0000313|Proteomes:UP000034090};
RN [1] {ECO:0000313|EMBL:KKS98897.1, ECO:0000313|Proteomes:UP000034090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS98897.1}.
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DR EMBL; LCFQ01000001; KKS98897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DMU6; -.
DR STRING; 1618578.UV74_C0001G0007; -.
DR PATRIC; fig|1618578.3.peg.8; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034090; 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: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: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; IPR005144; ATP-cone_dom.
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; 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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 706 AA; 79355 MW; 3F085EF163BB5A16 CRC64;
MKESGEKEPF DPGKLFVGIW KAALDVGGKD KKLAKKLGLQ VLTLVNKHYP NGEAIPTFEI
GEFAEKVLVE NGHTKTAKAF ILYRENKRHA RQDKSKLGVE DDIGLSYNTL YILKERFLKR
NEKGNIVETP KKLVERVAKF LAQAEKTKKL EQKWQEDFYK IMSSFEFLPG TRTLTNAGKR
TPQLANCFVW PVEDDIDEIF NILHKSTLIK KHGGGCGYNF SRVRPEGDSV GGIPGLAAGP
VKMIEMYDLM TSLFRQEGKY ESGNMAILNA NHPDVFNFIS SKQTDGYLSK TNISIGITDQ
FMKAALRNQD WELINPRTGE IVNTVKAKSI LQLMAQMAWA TGDPGIINLS AMNKGTALAN
PLLKKRGMIE ATNPCGEVPL YPYESCNLGY VNFSKFIVNN RFDFKRLSDV MAIAVRLMDN
VIESSWFPIP QVTESVRAHR RIGIGAVGWA EALAKMGIAY DSTEAFKLAG KVARVMYKSA
FEASCDLSEE KGPFPLVNDS IWAHTKRKPR NVALLTFPPS SSNAVICETS FGIEPYFALA
YEQNVLGGMR LKNIVPFFVE ELKRRKIYSE GLIQKVIENH GSVQGIDEVP PDMQKIFRVA
HDIKWQDHIK MQAAFQKWTD NAITKTINLP SNATPTDIEE AFVMAWKLGC KGLTVYRDQT
KNNQVINFGK DNKKDVLRKC PTCDLKLVRD GKCYKCKKCG FSTCEL
//
