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Database: UniProt
Entry: B2HHG0_MYCMM
LinkDB: B2HHG0_MYCMM
Original site: B2HHG0_MYCMM 
ID   B2HHG0_MYCMM            Unreviewed;       721 AA.
AC   B2HHG0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   Name=nrdE {ECO:0000313|EMBL:ACC40092.1};
GN   OrderedLocusNames=MMAR_1642 {ECO:0000313|EMBL:ACC40092.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40092.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40092.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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; CP000854; ACC40092.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HHG0; -.
DR   STRING; 216594.MMAR_1642; -.
DR   KEGG; mmi:MMAR_1642; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_4_1_11; -.
DR   OMA; RGSIQNI; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001190; 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:UniProtKB-UniPathway.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573:SF30; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 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:UP000001190}.
FT   DOMAIN          573..595
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   721 AA;  82061 MW;  CC257496D6DA99DE CRC64;
     MSPTVTAEPV TTSAHALPGE TDYHALNAML NLYDADGKIQ FDRDVLAARQ FFLQHVNQNT
     VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKTLLDRAY AKKFRFPTFL GAFKYYTSYT
     LKTFDGKRYL ERFEDRVVMV ALTLASGDAT LAEKLVDEII DGRFQPATPT FLNSGKKQRG
     EPVSCFLLRI EDNMESIGRS INSALQLSKR GGGVALLLTN IREHGAPIKN IENQSSGVIP
     IMKLLEDSFS YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVVIP
     DITFELAKRN DDMYLFSPYD VERVYGVPFA DISVTEKYYE MVDDSRIRKT KIKAREFFQT
     LAELQFESGY PYIMFEDTVN RANPIEGKIT HSNLCSEILQ VSTPSLFNDD LSYAKVGKDI
     SCNLGSLNIA RTMDSPDFAQ TIEVAIRALT AVSDQTHITS VPSIEQGNND SHAIGLGQMN
     LHGYLAREHI FYGSEEGVDF TNIYFYAVLY HALRASNRIA VERGTRFKGF DQSKYASGEF
     FDKYTERVWE PKTEKVRQLF ADAGIRIPNQ DDWQRLKESV QAHGIYNQNL QAVPPTGSIS
     YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNENLD YYQDAYEIGY EKIIDTYAAA
     TEHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY IRLRQMALEG TEVAGCVSCM
     L
//
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