ID K4IMW2_BIFAP Unreviewed; 731 AA.
AC K4IMW2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 OrderedLocusNames=BAST_1383 {ECO:0000313|EMBL:AFU71952.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71952.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU71952.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71952.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
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; CP003325; AFU71952.1; -; Genomic_DNA.
DR RefSeq; WP_015022388.1; NC_018720.1.
DR AlphaFoldDB; K4IMW2; -.
DR STRING; 1147128.BAST_1383; -.
DR GeneID; 41010602; -.
DR KEGG; bast:BAST_1383; -.
DR PATRIC; fig|1147128.3.peg.1407; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000007006; 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; 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; 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 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}.
FT DOMAIN 583..605
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 82740 MW; 845E869DD139B312 CRC64;
MGANEDTSLA LDRTASEDEE TFDPAHDYHA LNAMLNLYDK DGRIQFDKDR EAERQYMDRH
VGPNTMAFPS TAERITYLLD HEYYDRKVFE RYTPEFLDRI YQHAAESGFE FETFLGAFKF
YTSYALKTFD GKRYLEDFPQ RCVAVALELA DGDEQAAMKY TDEIISGRFQ PATPTFLNLG
KAQRGEPVSC FLVRIEDNME SISRGVNAAL QLSKRGGGVA LLLSNLREMG APIKHIENQS
SGVVPVMKLL EDSFSYANQL GARQGAGAVY LSAHHPDIMR FLDTKRENAD EKIRIKSLAL
GVVIPDITFE LAKRKEPMAL FSPYDVERVY GKPFADISIT EHYEEMVKDK RIHKKYIDAR
DFFMTLAEIQ FESGYPYILF EDTVNKANPI DGRITMSNLC SEILQVQEPS TYSENLNYEH
IGRDISCNLG SLNIAKAMDG GLADTVETSV RALTSVSDHT NIEAVPSIKR GNDEGHAIGL
GQMNLHGFLA REGIHYGSEE GLDFTDMYFM TVAYHAYRAS HALAVERGKA FASFAKSDYA
KPAGQGNYFD KYTEGSRSLE PRTQRIKDLF DQYKVHIPTV EDWKELQAAI LKDGIYNQNL
QAVPPTGSIS YINHSTSSIH PIASKIEIRK EGKIGRVYYP APYMTNENLD YFEDAYEIGW
KKIVDTYAEA TQHVDQGLSL TLFFPDTATT RDLNKAQIYA WRKGIKTLYY IRIRQQALEG
TEVEGCVSCM L
//
