ID A0A0G1YDN5_9BACT Unreviewed; 707 AA.
AC A0A0G1YDN5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=UY48_C0005G0038 {ECO:0000313|EMBL:KKW13082.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWB1_49_7.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618448 {ECO:0000313|EMBL:KKW13082.1, ECO:0000313|Proteomes:UP000034588};
RN [1] {ECO:0000313|EMBL:KKW13082.1, ECO:0000313|Proteomes:UP000034588}
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:KKW13082.1}.
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DR EMBL; LCQD01000005; KKW13082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YDN5; -.
DR PATRIC; fig|1618448.3.peg.318; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034588; 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 2..70
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 75..540
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 707 AA; 78352 MW; 9865C6B0BF5D7AA7 CRC64;
MEFSSHAKLV LNERRYLAPG ETPEGMFARV AKQVALVEAK DRAYWEEQFF NIMNNGLFLP
NTPCLFNAGI SNLMSACFVL VPDDSIPSIF DVLGLSASIF QSGGGLGYSF SRLRENGARV
KSGGISSGPI SFMGAYNEMA ESIKQGGRRR GAMMGVLNCS HPDIVEFIRA KETEGRLRNF
NLSVDISQAF IKALKAGDSY PLYHYNGRGV IQPKGEKSAK EIFDLICQGI HKNGEPGVIF
LDEINDINPL PEHIEACNAC SEAYLLSHEA CILGSINLAR FVGGSAELFY DAVTVAHRFL
DNLIDAQEYI HPTIEEAVKK TRKIGLGIMG LHEALILNHI PYDSEAALKF THETLSTFDA
ALHKASSTVG EEKGFYPAHT KVRQGTQFDR FRYRRNMWAS CIAPTGSLSI LAGTSSGLEP
LFILYGTKRY NDEKVEFTFP PFERWLVGKP VKAAKDIMDW AKLYGHVDDC PHMTPHERAL
WKRGASIPWQ AHLKMLEEAQ GHIDMGISKT INIHHNASIQ DVEQIFRAAM DSNVRSLTIY
RENSREAQVF DAGKSKPKEA EEKNDNAFVI RKGQTGEAES GCGKVYITYN QEPKTETFIR
MGKAGACQSA WAEITGRATS LALQAGVPLR EIIKQYQRVK CPRPIYHGGE QYTSCIDCMA
RILNAMSGEV IECGEDTSQS CPECGQALMR EGQCWRCTSC SYSTCGG
//
