ID A0A1F8RU59_9CHLR Unreviewed; 934 AA.
AC A0A1F8RU59;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A2148_07990 {ECO:0000313|EMBL:OGO50881.1};
OS Chloroflexi bacterium RBG_16_68_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797660 {ECO:0000313|EMBL:OGO50881.1, ECO:0000313|Proteomes:UP000176790};
RN [1] {ECO:0000313|EMBL:OGO50881.1, ECO:0000313|Proteomes:UP000176790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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|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:OGO50881.1}.
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DR EMBL; MGOB01000064; OGO50881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RU59; -.
DR STRING; 1797660.A2148_07990; -.
DR Proteomes; UP000176790; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide 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 CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
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; 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.
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|ARBA:ARBA00022634,
KW 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 60..142
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 163..708
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 101713 MW; 41794F6BB5EADE21 CRC64;
MVTVPAGRTS STSLPPEANP PPAEDGRALR IQRYFTKPGV HPFDEVAWER RNATIADESG
QTVFEQRDVE VPASWSQTAT NVVVSKYFRG PLGTPQRETS VRQLIRRVVG TLTQWGREGG
YFLSEEEAQT FHDELTHLLL HQTACFNSPV WFNVGVEEKP QCSACFILSV GDTMESILEW
CKTEGMIFKG GSGSGINLSS IRSSREQLSS GGQASGPVSF MRGADAIAGS IKSGGKTRRA
AKMVVLNADH PDVLEFIECK AREERKAYDL GSSGWDMSLN GEAWASIQFQ NANNSVRATD
EFMSAASGED RDWELRAITT GEVLEMVKAR EVLRRIAQAT WECGDPGMQF DTTINRWHTC
PASGRINASN PCSEYMHVDD SACNLASLNL MRFLDEEGCF DIEAFRHAAA TVIWAQEIIV
GYSSYPTQKI ERNAREMRQL GLGYANLGAL LMALGVPYDS DVGRAYAAAI TALMTGHAYA
TSAVIAERVG PFAAYEPNRE PMLGVIGQHR DAAYRVPLLG VDPGASNLEE LVGAACEAWD
RALELGRQHG YRNAQATVIA PTGTIAFMMD CDTTGIEPDI ALVKYKKLVG GGLMKMVNQT
VPPALRRLGY DEAEVAQIVR HVDEQGTIEG APGLRQEHLP VFDCAFKAEK GRRCIHPMGH
IKMMGACQPF VSGAISKTVN LPKEATVEEI MDAYIEAWRH GLKAIAIYRD GSKKVQPLST
GTAETNGSAR GGDGQPRRRA LPDTRSSITH KFKIEGHTGY ITVGVYEDGS PAEVFISMAK
QGSTIYGMME SFGRAISYAL QYGVPLRDLV RNFSHMRFEP SGMTSNPEIP FAQSVIDYLF
RWLASQFLSP EEVEELGVLT PEVKQRLTDR LDGVAGGSNG HNGYNGGAGE MVNSGVARLN
GQSDAPACAG CGWIMVRSGT CYRCENCGST SGCS
//
