ID A0A0C2RW38_9BACL Unreviewed; 849 AA.
AC A0A0C2RW38;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-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};
GN ORFNames=KR50_26390 {ECO:0000313|EMBL:KIL45964.1};
OS Jeotgalibacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL45964.1, ECO:0000313|Proteomes:UP000031972};
RN [1] {ECO:0000313|EMBL:KIL45964.1, ECO:0000313|Proteomes:UP000031972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL45964.1,
RC ECO:0000313|Proteomes:UP000031972};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Jeotgalibacillus campisalis genome sequencing.";
RL Submitted (JAN-2015) 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:KIL45964.1}.
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DR EMBL; JXRR01000017; KIL45964.1; -; Genomic_DNA.
DR RefSeq; WP_041059226.1; NZ_JXRR01000017.1.
DR AlphaFoldDB; A0A0C2RW38; -.
DR PATRIC; fig|220754.4.peg.2655; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000031972; 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:UP000031972}.
FT DOMAIN 129..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 849 AA; 94887 MW; 32DC9A7260FA0E01 CRC64;
MTSLSTQHST LNVEQLNQDI AKFDPVHPIT PDMKITHKGV SRLVMLDRYA FKDTEKKSLR
TGDFVVLTIR EDPKFPARGL GYIQSINSEK REAHVLIEEE FRNSLDTPKE METGIVVRSL
DVIEKPLEIY YEQIALRNAT GLASVEKTEE QRSKWTEEFY KELSSLHFVP AGRVLYGAGA
KTDVTFFNCY VMPFVKDSRE GISDHRKQVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LSDWHPDIIE FIISKMQNPR ILRFLLETTE
DEFIKKIAQE KLKFTPLTEQ EVGMYQSIIN YKEIPGFGGF NEQIIEEAEE KLATGGTYSV
HNPEFLTGAN ISICLTDDFM QAVERDGEYK LRFPDVESYT KEQMTVYNDT WHEVGDVRKW
EESGNAVRTY RTIKAKELWN LINICATYSA EPGIFFIDNA NEMTNAQSYG QQVVATNPCG
EQPLAPYSVC NLAAVNLAEF ADKETKQVQF DKLKKTVEIG VRMQDNVIDA TPYFLAENQT
QALGERRVGL GVMGLADLLI YCEKEYGSEE GNKLVDEIFE TIAVTAYRAS IELAKERGAF
PFLEGASVEK TAQLRKNFTE TGFMKKMPDD IKEGIRTHGI RNSHLLTVAP TGSTGTMVGV
STGLEPYFSF TYYRSGRLGK FIEVKADIVR EYLSLNPSAS ESDLPDFFVT AMELAPEAHA
DTQCVIQRWI DSSISKTVNA PKGYAVEQVE SVYERLYKGG AKGGTVYVDG SRDSQVLTLK
AEDNNMNEPG KKTKQNVVLV DTIQDLRSTN VTIGSELGNT CPVCRKGTVK EIGGCNTCTN
CNAQLKCGL
//
