ID A0A498DDH7_9BACI Unreviewed; 853 AA.
AC A0A498DDH7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=D8M04_02135 {ECO:0000313|EMBL:RLL48096.1};
OS Oceanobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2448030 {ECO:0000313|EMBL:RLL48096.1, ECO:0000313|Proteomes:UP000270219};
RN [1] {ECO:0000313|EMBL:RLL48096.1, ECO:0000313|Proteomes:UP000270219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-02 {ECO:0000313|EMBL:RLL48096.1,
RC ECO:0000313|Proteomes:UP000270219};
RA Yu L.;
RT "Oceanobacillus sp. YLB-02 draft genome.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RLL48096.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCHR01000001; RLL48096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DDH7; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000270219; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000270219}.
FT DOMAIN 127..181
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 188..767
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 853 AA; 95734 MW; DAFD0FF571672DB9 CRC64;
MSIFVNKRDN INIESLNKDI DLFTAVFPIT DDMKLTHKGV SRLVMLDRYS FKDTTKKTLK
IGDFVVLTVK ADPKFPARGL GFIQSIDWDK KEAEVKVEAD YLSVLDDEKE AETGIVKRSL
DTIDKPLEIF YEQIAKRNAK GLSVVEKTEE QQNNWFEAFY SELSQLNFIP AGRVLYGAGS
ETEVTYFNCY VMPYVKDSRE GISDHRKKVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LVDSHPDIIE FIISKMQNPR ILRYLIENTE
DEQIKKLAQE KLKFTPLTPT EEDLYQGILN YRSIPGQGGF TDAVLQEAEL KLNTGGTYSV
QNPDFLTGAN ISVCITKDFM EAVENDDYYE LRFPDVENYT EEEMKAYNEK WHEVGDVRKW
EDMGFGVRVY RRMRAKELWK LINICATYSA EPGIFFIDNA NEMTNAKSYG QQVVATNPCG
EQPLAPYSVC NLAAVNLAEM ADKNTKTVDF EKLKATVEVG VRMQDNVIDA TPYFLPENER
QALGERRIGL GVMGLHDLLI YTESQYGSKE GNELVDKIFE TIATTAYRTS IELAKEKGSF
PFLVGQSDEE TKQLREAFID TGYMRKMPED IRQGVLEYGI RNSHLLTVAP TGSTGTMVGV
STGLEPYYSF SYFRSGRLGK FIEVKADIVQ EYLDNHPESD PENLPNWFVT AMELSPEAHA
DTQCVIQRWV DSSISKTVNA PKGYTVEQVE NVYERLYRGG AKGGTVYVDG SRDSQVLTLK
AEENTFEQTE LFPEKDDKPK VVLMDTVQEL GTTSVTIGSE VGNTCPVCRE GTVEDIGGCN
TCISCGAQLK CGL
//
