ID A0A0G0K403_9BACT Unreviewed; 771 AA.
AC A0A0G0K403;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
DE Flags: Fragment;
GN ORFNames=US51_C0007G0001 {ECO:0000313|EMBL:KKQ35366.1};
OS Microgenomates group bacterium GW2011_GWA2_37_6.
OC Bacteria.
OX NCBI_TaxID=1618497 {ECO:0000313|EMBL:KKQ35366.1, ECO:0000313|Proteomes:UP000034211};
RN [1] {ECO:0000313|EMBL:KKQ35366.1, ECO:0000313|Proteomes:UP000034211}
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:KKQ35366.1}.
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DR EMBL; LBTG01000007; KKQ35366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0K403; -.
DR PATRIC; fig|1618497.3.peg.81; -.
DR Proteomes; UP000034211; 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: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; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
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; 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.
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 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,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 3..55
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 62..542
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKQ35366.1"
SQ SEQUENCE 771 AA; 85924 MW; 3ACBBD0C9B163428 CRC64;
PLEQTPDEMW KRVAKGIAGQ EKKTLQKTWE KKFYSAMEGF KFLPGGRILA GAGTGFDVTY
FNCFVIPSPK DSRDGILDNL KIMIEIMARG GGVGINLSSL RPKGSRVKKV NGFSSGPMNW
AELYSLATKD IIQQGGSRRG ALMLMLHDWH PDIEEFITVK EDLRRINGAN LSVCVSDDFM
EAVKANRDWN LEYPDLDDPK YDKKWDGDLK AWKKLGGKAV VKKTVKANYL WDLICTAAWR
SAEPGLHFLD RSNKRSNTAY FETLIATNPC GEQPLGAWAV CNLGAINLSA YVHAGKFDYK
NFGQDVRVAM RFLDNVIDDT YYFYPENEKV AKDIRRTGLG ILGLADALIK MKLKYGAPES
EETLRKIFET LRDNAYDVSS DIAKEKGAFP KFNKEKYLKT WHVEKLPEEI KAKIAKYGIR
NAVLLTIAPT GTTSLISGVS SGVEPVYEFE FIRRDRLGEH KMYHPLYEEW KRAHPGEEKP
DYFVSANDLT PEDHVVVQAI AQEYIDSSIS KTVNAPNAHT VTDVKNLYML AYDHGLKGIT
YMRDGSREGV LSRVSEKKDQ VSTQETPATL PKEYVRAPRP MMVEGVTYKT ETPAGDTYIT
LNHDSNHEPF EVFITIGKTG SDVAAMADAL GRMISLNLRL AGNLPPRERI RRVISQLSGI
GGARSVGFGE NRVRSLPDAV AKVLAKQYAF KVNGAVEDKL APNTSSEGEA PIDIPESKGE
ITVLQQLPLQ EGITVEKAET HLFDICPSCG ATSLAYEEGC RKCYSCGHSE C
//
