UniProt: A0A221MHK9

Database: UniProt
Entry: A0A221MHK9_9BACI

LinkDB:  A0A221MHK9_9BACI 
Original site:  A0A221MHK9_9BACI

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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 (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   A0A221MHK9_9BACI        Unreviewed;       746 AA.
AC   A0A221MHK9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   ORFNames=CFK40_20150 {ECO:0000313|EMBL:ASN07148.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN07148.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN07148.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN07148.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT   Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT   Virgibacillus salexigens comb. nov., and emended description of the genus
RT   Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; CP022437; ASN07148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221MHK9; -.
DR   KEGG; vne:CFK40_20150; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000204391; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 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.
DR   SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204391}.
FT   DOMAIN          604..626
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   746 AA;  85608 MW;  A1AA33F8686EAE20 CRC64;
     MQTAILTKSW KSYLEERVKE AFPTMPIQSF LDKNANTKES ISTEEWVNHL TLEALSNIDE
     EHPDWTYVAA MIYSEWLYNQ AAKNRNYDYE KKYGSLYKLI SEITEIGIYD QGLLHTYDKD
     EVDQLERLIR PERDQLFTFI GLKTLADRYL AKNYTKEIYE LPQERFMIIA MTLMQDEPKD
     RRMDLVGQAY WAMSNLYMTV ATPTLSNAGK SYGQLSSCFI DTLDDSLQSI YDSNTDIANL
     SKNGGGIGVY LGKIRSSGSM IKGFKGASSG VIPWMKQLNN TAVSVDQLGQ RKGAICVYLD
     VWHKDIHSFL DAKLNNGDER MRTHDLFTGV TLPDLFMEKV EARDDWYLFD PHEIRTVMGY
     SLENFYDEEK ENGSFRERYA ECVANPTLSK EAVPAIEIMK SIMKGQLETG GPFLFYRDEV
     NRQNVNKHTG MIYCSNLCTE IMQNQSPTKF IDQQTKDGKI LITKEPGDFV VCNLSSINLG
     RAVVDDVLEK LIPIQVRMLD NVIDLNHIPV PQARYTNVRY RAIGLGTFGW HHLLALKRMK
     WESEESIEFA DSLYEKIAYL TIQASMDLAK EKEPYPLFSG SEWDTGKYFE RKGYLNQAES
     NFDWNKLQED VQENGIRNSY LMAVAPNSST SLIAGSSASI DPIFRKFYSE EKKDFKIPVT
     APDLSAETTW YYKSAYMIDQ KWSVAQNAAR QKHIDQGISF NIYVPNGVQA RELLEIHLLA
     WQSGFKTTYY LRSTSSDIEE CESCSS
//

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