ID A0A7I9Y464_9MYCO Unreviewed; 723 AA.
AC A0A7I9Y464;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=nrdE2 {ECO:0000313|EMBL:GFG76673.1};
GN ORFNames=MBOT_40380 {ECO:0000313|EMBL:GFG76673.1};
OS Mycobacterium botniense.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=84962 {ECO:0000313|EMBL:GFG76673.1, ECO:0000313|Proteomes:UP000465361};
RN [1] {ECO:0000313|EMBL:GFG76673.1, ECO:0000313|Proteomes:UP000465361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17322 {ECO:0000313|EMBL:GFG76673.1,
RC ECO:0000313|Proteomes:UP000465361};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
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=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]-
CC disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]-
CC dithiol; 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:ARBA00047754,
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:GFG76673.1}.
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DR EMBL; BLKW01000004; GFG76673.1; -; Genomic_DNA.
DR RefSeq; WP_163760400.1; NZ_BLKW01000004.1.
DR AlphaFoldDB; A0A7I9Y464; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000465361; Unassembled WGS sequence.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:TreeGrafter.
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 CDD; cd01679; RNR_I; 1.
DR FunFam; 1.10.1650.20:FF:000002; Ribonucleoside-diphosphate reductase; 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000465361}.
FT DOMAIN 575..597
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 723 AA; 82104 MW; 19AF9130BB66E280 CRC64;
MPPTATAAEP VTSTGRASAH EETDYHALNA MLNLYGPDGK IQFDKDIQAA HQFFRQHVNQ
NTVFFHDLDE KLDYLVQQNY YEPEVLEKYS RAFVKSLFDR AYAKKFRFPT FLGAFKYYTS
YTLKTFDGKR YLERFEDRVC MVALTLADGD TELAEKLVDE IIDGRFQPAT PTFLNSGKKQ
RGEPVSCFLL RIEDNMESIG RAINSALQLS KRGGGVALLL SNIREHGAPI KNIENQSSGV
IPIMKLLEDS FSYANQLGAR QGAGAVYLHA HHPDIYRFLD TKRENADEKI RIKTLSLGVV
IPDITFELAK RNDDMYLFSP YDVERVYGVP FADISVTEKY YEMLDNPRIR KSKIKAREFF
QTLAELQFES GYPYIMFEDT VNRANPIAGK ITHSNLCSEI LQVSTPSQFN ADLSYAKVGK
DISCNLGSLN IAKTMDSPDF AQTIEVAVRA LTAVSDQTHI WSVPSIEKGN SEAHAIGLGQ
MNLHGYLARE RIFYGSEEAI DFTNIYFYTV CYYALRASNK IAIERGTHFT GFERSKYATG
EFFDKYTDQV WEPKTPKVRK LFADAGIHVP TQDDWRELKA SVQKHGIYNQ NLQAVPPTGS
ISYINHSTSS IHPIVSKIEI RKEGKIGRVY YPAPYMTNDN LEYFQDAYEI GYEKIIDTYA
AATQHVDQGL SLTLFFKDTA TTRDVNKAQI YAWRKGIKTL YYIRLRQMAL EGTEVEGCVS
CAL
//
