ID A0A2P8H4M1_9BACL Unreviewed; 852 AA.
AC A0A2P8H4M1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=B0H99_103274 {ECO:0000313|EMBL:PSL41140.1};
OS Planomicrobium soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX NCBI_TaxID=1176648 {ECO:0000313|EMBL:PSL41140.1, ECO:0000313|Proteomes:UP000242682};
RN [1] {ECO:0000313|EMBL:PSL41140.1, ECO:0000313|Proteomes:UP000242682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12259 {ECO:0000313|EMBL:PSL41140.1,
RC ECO:0000313|Proteomes:UP000242682};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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:PSL41140.1}.
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; PYAT01000003; PSL41140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8H4M1; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000242682; 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"
SQ SEQUENCE 852 AA; 95045 MW; 7546F4A2B83E41A7 CRC64;
MVSITQSEYT LDAGSLNEAI KSFPQVHAVT PDMKTTHKGV SRLVMIDRYS FKDTEKKTLK
VGDFVVLTVK EDPKFPARGL GYIVAIDKAA NKAQVWIEED YRSAIDKPEE QETGIVSRSL
DVIEKPLEVF YEQIAKRNAT GLASVEETPE KRQHWFEKFY EQLVGLKFIP AGRVLYGAGA
DTDVTYFNCY VMPFVADSRE GISDHRKQVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LADWHPDIAE FIISKMQNPR ILRYLIENTE
DETIKKLAHD KLKFKPLTQQ EEAMYQGILN YRAIPGMGGF NEKIMQDAET KLRDGGTYSV
HNEEFLTGAN ISVTLTDDFM KAVEEDADFA LRFPAVESYS KEEMAIYNEQ WHEVGDVREW
ERLGHRVRTY RTMKARDLWN LINVCATYSA EPGIFFIDNA NDKTNAKAYG QKVVATNPCG
EQPLAPYSVC NLAAVNLAQF ADAQTKQVDF EALKETVRVG VRMQDNVIDA TPYFLEENRI
QALGERRVGL GVMGLADLLI YCDKEYGSPE GNELVDEIFK TIAVAAYEQS TELAVERESF
PFLVGKTDEE TAALRKAFTE TGFMQGMPEH VREAVIQKGI RNSHLLTVAP TGSTGTMVGV
STGLEPYYSF TYYRSGRLGK FIEVKADIVR EYLKNNPEAN EENLPKAFVT SMDLAPEAHA
DVQCIIQRWI DSSISKTVNA PRGYTVEQVE GVYERLYKGG AKGGTVYVDG SRDSQVLTLK
AEENTFEEEP KEEASAKRPI VLIDTIQDLR STNVTIGSEV GDTCPVCRKG TVEEMGGCNT
CTNCNAQLKC GL
//
