ID A0A2S5GEL7_9BACL Unreviewed; 847 AA.
AC A0A2S5GEL7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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};
GN ORFNames=C4B60_04810 {ECO:0000313|EMBL:PPA71388.1};
OS Jeotgalibacillus proteolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=2082395 {ECO:0000313|EMBL:PPA71388.1, ECO:0000313|Proteomes:UP000239047};
RN [1] {ECO:0000313|EMBL:PPA71388.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22-7 {ECO:0000313|EMBL:PPA71388.1};
RA Li Y.;
RT "Jeotgalibacillus proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (FEB-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:PPA71388.1}.
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DR EMBL; PREZ01000002; PPA71388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5GEL7; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000239047; 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 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"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 94969 MW; A3927CE5BEEC0DFF CRC64;
MTSLSTQHQT LNISQLNEDI SKFDPVHPIS PDMKLTHKGV SRLVMLDRYA FKDTEKKTLR
TGDFVVLTIR EDPKFPARGL GYIQSINAEK REAHVLIEEE FRNSLDTPKE IETGIVQRSL
DVIEKPLEVF YEQIALRNAT GLASVEKTEE DRKKWTQKFY EELSSLHFVP AGRVLYGAGA
KTDVTFFNCY VMPFVKDSRE GISDHRKQVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LSDWHPDIVE FIISKMQNPR ILRFLLDTTE
DEFIKKIAHE KLKFTPLTEQ EAGMYQSIVN YKEIPGYGGF NEQIIEDAEE KLNTGGTYSV
HNPEFLTGAN ISICLTDDFM KAVEEDGEYK LRFPDVESYS HDQMEAYNNN WHEVGDVREW
EKQGNAVRTY RTIKAKELWN LVNICATYSA EPGIFFIDNA NDMTNAKAYG QQVVATNPCG
EQPLAPYSVC NLAAVNLAEF ADKENKTVQF DKLKKTVEIG VRMQDNVIDA TPYFLEDNQK
QALGERRVGL GVMGLADLLI YCEKEYGSAE GNELVDKIFE TIATTAYRTS IELSKERGSF
PFLEGQTEEE TLRLRKAFTE TGFMKKMPED IKEGILSSGI RNSHLLTVAP TGSTGTMVGV
STGLEPYFSF TYYRSGRLGK FIEVKADIVK EYLDRNHKTD ETDLPEFFVT AMELAPEAHA
DTQCVIQRWI DSSISKTVNA PKGYAVEQVE SVYERLYKGG AKGGTVYVDG SRDSQVLTLK
AEENTMNEKA EKQTVVLVDT IQDLRSTNVT IGSELGNTCP VCRKGTVKEI GGCNTCTNCN
AQLKCGL
//
