ID A0A087D8P8_9BIFI Unreviewed; 717 AA.
AC A0A087D8P8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BSTEL_2187 {ECO:0000313|EMBL:KFI91898.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI91898.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFI91898.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI91898.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI91898.1}.
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DR EMBL; JGZP01000034; KFI91898.1; -; Genomic_DNA.
DR RefSeq; WP_051923096.1; NZ_JGZP01000034.1.
DR AlphaFoldDB; A0A087D8P8; -.
DR STRING; 762211.BSTEL_2187; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029004; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029004}.
FT DOMAIN 569..591
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 717 AA; 80099 MW; 9D47AA57FDD2D5CE CRC64;
MTTIGTTYDP STDYHALNAM LNLYDEHGLI QFGKDKEAER AYVANEIEPN TKRFATAGER
LRWLIDHDYY DGDVFARYDA DFLESFYAHA AASGFEFETF LGAFKFFRSY ALKSFDGKTY
LEDFPQRCAA VALDLAAGDE SAATAYLDEM LAGRFQPATP TFLNLGKAQR GEPVSCFLVR
IEDNMESISR GINAALQLSK RGGGVALLLS NLRELGAPIK HIENQSSGVV PVMKLLEDSF
SYANQLGARQ GAGAVYLNAH HPDIMRFLDT KRENADEKIR IKSLALGVVV PDITFELAKR
KERMALFSPY DVERVYGKPF ADISVTEKYD EMVADDRIRK TYIDARKFFT TLAELQFESG
YPYLVFEDTV NRANPIDGRV TMSNLCSEIL QVQEASTYRE DLSYEHVGRD VSCNLGSLNI
AKAMDGGLAG TVETAIRALT AVAEHTSIDA VPSIRRANDE GHAIGLGQMN LHGFLAREGF
RYGSDEALDF TDMYFMTVAY HAYRASHDLA VERGKAFVGF ERSDYAKPAG AGNYFDKYTD
GRAPAAPRTE RVRELFARYG VAVPTVADWE ALRDAILRDG LYNQNLQAVP PTGSISYINH
STSSIHPIAS KIEIRKEGKI GRMYYPAPYM TNDNLEYFQD AYEIGWQAIV DTYAAATRHV
DQGLSLTLFF PDTATTRDVN KAQIYAWRKG IKTLYYIRIR QQALEGTEVA GCVSCML
//
