ID A0A1J5HN26_9BACT Unreviewed; 860 AA.
AC A0A1J5HN26;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AUK57_01445 {ECO:0000313|EMBL:OIP86116.1};
OS Candidatus Saccharibacteria bacterium CG2_30_41_52.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1805375 {ECO:0000313|EMBL:OIP86116.1, ECO:0000313|Proteomes:UP000183829};
RN [1] {ECO:0000313|EMBL:OIP86116.1, ECO:0000313|Proteomes:UP000183829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_41_52 {ECO:0000313|EMBL:OIP86116.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 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:OIP86116.1}.
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DR EMBL; MNZN01000002; OIP86116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5HN26; -.
DR STRING; 1805375.AUK57_01445; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000183829; 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 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; 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.
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 38..119
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 123..646
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 860 AA; 95333 MW; 38FC064885A64FB8 CRC64;
MKELVQPTLE LNETERLAEI HKIGCDVPKP PDTLPEPKLS ENAWYIGRTR YARRDSKGIP
IETPKELFWR VAYNIATAEL LYGGDKKAHI ATATKFYKLM TSRKFLPNTP TLLNTAKPKQ
QLSACFVLPV PDSLDGILET ASDMAMIHKS GGGTGFAFSR LRPKNDILST SGGSTTGPIS
FMQMYNDITS SIRQGGVRRG ANMGILHYNH PDILLFMIYK LDEFSLTNFN ISVTTSKEFF
NQITIDKQIL DNDYEKEFDF DALVIDAREA LQTRDMDLKN VRLDAVVAKL TEWCKEETPD
YGYALINPRT HQEVGRLNAK KVFDLITRFA WQYGDPGMIF IDRINDSRAN PTPQLGQIEA
TNPCGEQPLL PYDACTLGSI NLALFVKGNS LDWDGLKQTT HQAVHFLDNV LDMNEYPIEK
VRLMVRQIRR IGLGIMGFAD ALIDMDIGYN TDEGVRMAEK IMQFIQAESD AASEELAVKR
GVFPAFEGSI YDKTGEIKPR NGARTTIAPT GTISMLAETS SGCEPLFALT YSKNTIEGKR
IFQSSPYFAS ALKKHGIYSE ELLEQIQANG GSIQNMDSIP ADLKKVFVVA GDISPEWHLK
IQAAFQKYVD NAISKTINFS NTATINDVRN AYLMAHETGC RGITIYRDGS RDKQILEVKK
DSSYFDKLAG NKAEAVAEVE ATPIRIELKP RPSVLNGRTH KVMTPLGKAF VSINEDEDGN
IFEVFINVGR AGSDITADAE AIGRLISLTF RIPTDYSSDQ IAQKVISQLR GIGGSSSTGF
GADRVRSLAD AVAKVIEQHQ ATKKAVIVLE GTEQTETVPL WQAEPSSAHK ITDMCPECGS
ASLRFIEGCQ KCELCGFSKC
//
