UniProt: A0A089IJB9

Database: UniProt
Entry: A0A089IJB9_9BACL

LinkDB:  A0A089IJB9_9BACL 
Original site:  A0A089IJB9_9BACL

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
All databases (10)   

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ID   A0A089IJB9_9BACL        Unreviewed;       872 AA.
AC   A0A089IJB9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   ORFNames=H70737_10580 {ECO:0000313|EMBL:AIQ23255.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ23255.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ23255.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ23255.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009279; AIQ23255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A089IJB9; -.
DR   KEGG; paej:H70737_10580; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_2_0_9; -.
DR   Proteomes; UP000029519; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02888; RNR_II_dimer; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR000788; RNR_lg_C.
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   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   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:UP000029519}.
FT   DOMAIN          143..627
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   872 AA;  95929 MW;  1549C5E11EFDF935 CRC64;
     MERKQRLEGL SEKIFLDRYA WKDADSNNAK VGDVVLVLTK DDPKFPTKEV GEIVERNGRI
     VTVKTRSGEL VKSDVEKLTL NIEKTPEEMW DRLSTAMASV EKTPELQEEW AGKFRSILDD
     WKLVPGGRIA AGAGASEELT LFNCYVIPSP KDSRGGIMQT LAEMTEIMAR GGGVGINLSS
     LRPRRAIVRG VNGSSSGSVS WGGLFSYTTG LIEQGGSRRG ALMLMINDWH PDVEDFITVK
     QTMGQVTNAN LSVCVSNSFM KAVKENLDWD LVFPDTTDPE YNDVWDGDLD KWKAAGKNVI
     HYRTVKARDV WRTIIESAWK SAEPGVVFME YYNQMSNSWY FNPIICTNPC GEQGLPGWGV
     CNLSAVNLSK FYDEKNHDVD WEDLATTTRY SVRFLDNVID KTPYHFPENE ANQKNERRVG
     LGTMGLAELM IKLNIRYGSP ESLAFLDKLY GFMAREAYLA SAEIAGEKGS FLAFDTEKYL
     MSGFMKNMLE TYPEVGEAIR KHGMRNVTVI TQAPTGSTGT MVGTSTGIEP YFAFKYFRQS
     RLGYDEQFVP IAQEWLEAHP GEELPDYFVT SMDLSAKDHI RAQAAIQRWV DSSISKTANC
     PSDFTVEETA ELYEMAFDLG CKGVTIYRDG SRDVQVLQTS KKEDAAEEVA PAVEVATTPE
     ANVVTASPAP QAPTKELDKQ YKKRPQVLRG ATYKINTPFG MAYITINDLD GTPAEIFLNV
     GKAGSDVFAM AEALGRVCSL FLRYGDHGEK VELLIKHLKG IGGSGAIGFG ANRVESIADA
     VAKALETHVL NNAHDDHLPA PIAATLELED FNEALNAELK ASVAAATSTD DSHGAHNHAT
     ASRDLCPSCG GASLINIEGC KTCGNCGYSR CG
//

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