ID A0A0G0VDZ0_9BACT Unreviewed; 1063 AA.
AC A0A0G0VDZ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=UU48_C0007G0019 {ECO:0000313|EMBL:KKR97886.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWF2_41_16.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618997 {ECO:0000313|EMBL:KKR97886.1, ECO:0000313|Proteomes:UP000034746};
RN [1] {ECO:0000313|EMBL:KKR97886.1, ECO:0000313|Proteomes:UP000034746}
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|ARBA:ARBA00025437, 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:KKR97886.1}.
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DR EMBL; LCAU01000007; KKR97886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VDZ0; -.
DR PATRIC; fig|1618997.3.peg.717; -.
DR Proteomes; UP000034746; 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:0050897; F:cobalt ion binding; IEA:InterPro.
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 CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 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 32..125
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 818..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 117571 MW; 80DB42F0E832F68D CRC64;
MSDSVSRFEE KIRPVSTVGI GDSVWNYMTS VRAVEKRDGI SETFQPEKLR RSLAKIFSAA
GLDNERLLQK VLTQVVSRIQ KSFDGHTVPS TNDIREIVNL TLIDHNLVHV AKKYMAYRTQ
ISTERNSEPQ YGQGITVERF FTKRGVHPYE LMAWERRDAR ITNEKGKVVF EQLGVEVPIS
WSQTATNIVV SKYFRGQIGK PDRENSIKQL IDRVALTMAN WGRLSGYFQT VEDADIFEAE
LTYILVNQMA AFNSPVWFNV GVNLEPQCSA CFINSVQDDM RSILNLAVTE GMLFKGGSGT
GSNLSNLRSS REYLAGSNGR ASGPVSFMKG LDAFAGVIKS GGKTRRAAKM VILNVDHPDI
EDFITCKAEE EKKAWALMDQ GYDGSIDGPA YASIYFQNAN NSVRVTDDFM QAVVDGKEWV
TREVKTGNAS VSYSARDLIN KMAQATWQCG DPGIQYDTTI NRWHTCKNTD RINASNPCSE
YMFLDDSACN LASLNLMKFR KEVNGVMEFD TEAFKKANQI IITAMDIIVG HSSYPTPAIE
QNSLDYRPLG IGYANLGALL MSRGLAYDSD EGRNLAAAMS SLQSGICYEQ SARIAEKMEP
FVGFRQNVEP CTNVMRMHRQ ATFQIPAKGV PTDLLSEART AWNNVVDATM RSGLRNAQIS
VLAPTGTIAF FMDCDTTGIE PDIALVKYKW LVGGGMMKIV NQTIPEALQR LGYSDQEQKD
ILHFIDEKDT IEGAPYIREE HLGIFDCAFK ATNGTRSIHY MGHLRMMAAV QPFISGAISK
TVNMPNEATP ADIANVFMEG WKLGLKAIAV YRDGSKRQQA LTTSREKDQS KKEEGKKEKV
EIVGDGRETT TKPLRRRLAD ERRSITHKFA VGGHEGYLTV GLYDDGTPGE LFVRMAKSGT
VMSGLMDSFS TAVSIGLQYG VPLRVLVNKF VHVRFEPSGY TNNPHIRIAK SIVDYIFRWI
ALKFLTPEEQ RIVGVNGLDE TQEVLIVSTP TVESESAAEA PSTTSVSQTS LFASNQPAPA
AATHTATFDN QADAPACTLC GSIMVRNAAC YKCLNCGSTS GCS
//
