UniProt: A0A1G8J206

Database: UniProt
Entry: A0A1G8J206_9BACL

LinkDB:  A0A1G8J206_9BACL 
Original site:  A0A1G8J206_9BACL

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (5)   
   InterPro (3)   
   Pfam (2)   
All databases (15)   

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ID   A0A1G8J206_9BACL        Unreviewed;       852 AA.
AC   A0A1G8J206;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   ORFNames=HF394_15445 {ECO:0000313|EMBL:QKX51855.1},
GN   SAMN04487975_113145 {ECO:0000313|EMBL:SDI25093.1};
OS   Planococcus glaciei.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=459472 {ECO:0000313|EMBL:SDI25093.1, ECO:0000313|Proteomes:UP000183022};
RN   [1] {ECO:0000313|Proteomes:UP000183022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6846 {ECO:0000313|Proteomes:UP000183022};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SDI25093.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6846 {ECO:0000313|EMBL:SDI25093.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QKX51855.1, ECO:0000313|Proteomes:UP000509222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCTC7660 {ECO:0000313|EMBL:QKX51855.1}, and NRL-ATB46093
RC   {ECO:0000313|Proteomes:UP000509222};
RA   Pajer P., Broz P.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000509222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRL-ATB46093 {ECO:0000313|Proteomes:UP000509222};
RA   Malisova L., Safrankova R., Jakubu V., Spanelova P.;
RT   "Isolation of Planomicrobium glaciei.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QKX51855.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNCTC7660 {ECO:0000313|EMBL:QKX51855.1};
RA   Malisova L., Safrankova R., Jakubu V., Spanelova P.;
RT   "Isolation of Planomicrobium glaciei.";
RL   Submitted (SEP-2020) 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}.
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DR   EMBL; CP051177; QKX51855.1; -; Genomic_DNA.
DR   EMBL; FNDC01000013; SDI25093.1; -; Genomic_DNA.
DR   RefSeq; WP_036809286.1; NZ_JAHZTB010000003.1.
DR   AlphaFoldDB; A0A1G8J206; -.
DR   STRING; 459472.SAMN04487975_113145; -.
DR   eggNOG; COG0209; Bacteria.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000183022; Unassembled WGS sequence.
DR   Proteomes; UP000509222; Chromosome.
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          128..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;  95072 MW;  753203DE98ED89C8 CRC64;
     MVSVTQTQYT LDPHSLNTDI QAFPQVHAIT PDMKITHKGV SRLVMIDRYS FKDTEKKTLK
     AGDFVVLTVK EDPKFPARGL GYIVSIDKAA NTAKIWIEED YRSAIDKESE QESGIVNRTL
     DVIEKPLEVY YEQIAKRNAT GLASVETTPE KRQEWFEKFY QQLVGLKFIP AGRVLYGAGA
     DTDVTYFNCY VMPFVADSRE GISDHRKQVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
     SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LADWHPDIAE FIISKMQNPR ILRFLIENSE
     DETIKKLAHN KLKFKPLTEQ EEAMYQGILN YRAIPGMGGF NEKIMRDAET KLRDGGTYSV
     HNEEFLTGAN ISVTLTDDFM KAVEEDADFD LRFPAVESYS KEEMAIYNEQ WHEVGDVREW
     ERLGHKVRTY RTMKARELWN LINVCATYSA EPGIFFIDNA NEKTNAKAYG QKVVATNPCG
     EQPLAPYSVC NLAAVNLAQF ADPSTKQVDF EALKETVRVG VRMQDNVIDA TPYFLEENRV
     QALGERRVGL GVMGLADLLI YCDKEYGSPE GNELVDEIFK TIAVAAYEQS TELAVERGSF
     PFLVGNTDEE TAALRKAFTE TGFMQGMPEE VRQGILENGI RNSHLLTVAP TGSTGTMVGV
     STGLEPYYSF TYYRSGRLGK FIEVKADIVR EYLKNNPEAD EENLPKAFVT SMDLAPEAHA
     DVQCIIQRWI DSSISKTVNA PRGYTVEQVQ GVYERLYKGG AKGGTVYVDG SRDSQVLTLK
     AEENTFEESH PEEVKGKRPI VLIDTIQDLR STNVTIGSEV GNTCPVCRKG TVEEMGGCNT
     CTNCNAQLKC GL
//

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