ID A0A1S1NHS2_9MYCO Unreviewed; 693 AA.
AC A0A1S1NHS2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BKN37_05880 {ECO:0000313|EMBL:OHV05366.1};
OS Mycobacterium talmoniae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1858794 {ECO:0000313|EMBL:OHV05366.1, ECO:0000313|Proteomes:UP000179734};
RN [1] {ECO:0000313|EMBL:OHV05366.1, ECO:0000313|Proteomes:UP000179734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE-TNMC-100812 {ECO:0000313|Proteomes:UP000179734};
RA Greninger A.L., Elliott B., Vasireddy S., Vasireddy R.;
RT "Genome sequence of Mycobacterium talmonii.";
RL Submitted (OCT-2016) 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:OHV05366.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLQM01000018; OHV05366.1; -; Genomic_DNA.
DR RefSeq; WP_071023143.1; NZ_MLQM01000018.1.
DR AlphaFoldDB; A0A1S1NHS2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000179734; 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:UP000179734}.
FT DOMAIN 545..567
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 693 AA; 79076 MW; 7729BD52FF173998 CRC64;
MLNLYDADGK IQFDKDREAA HQYFREHVNQ NTVFFHDLDE KLDYLIQKNY YEREVLDQYS
RNFVKELLGR AYAKKFRFPT FLGAFKYYTS YTLKTFDGKR YLERFEDRVV MVALTLAAGD
TVLAEKLVEE IIDGRFQPAT PTFLNSGKKQ RGEPVSCFLL RIEDNMESIG RSINSALQLS
KRGGGVALLL SNIREHGAPI KNIENQSSGV IPIMKLLEDS FSYANQLGAR QGAGAVYLHA
HHPDIYRFLD TKRENADEKI RIKTLSLGVV IPDITFELAK KNEDMYLFSP YDVERVYGLP
FADISVTEKY YEMVDDSRIR KSKIKAREFF QTLAELQFES GYPYIMFEDT VNRANPIDGK
ITHSNLCSEI LQVSTPSEFN DDLSYAKVGK DISCNLGSLN IAKAMDSPDF AQTIEVAIRA
LTAVSDQTHI TSVPSIEQGN NDSHAIGLGQ MNLHGYLARE GIFYGSDEGV DFTNIYFYTV
CYHALRASNR LAIERGTRFA GFEKSKYATG EFFDKYTEQV WEPKTDKVRR LFADAGIRIP
NQDDWRRLKA SVAEHGIYNQ NLQAVPPTGS ISYINHSTSS IHPIVSKVEI RKEGKIGRVY
YPAPYMTNDN LEYYQDAYEI GYEKIIDTYA AATQHVDQGL SLTLFFKDTA TTRDVNKAQI
YAWRKGIKTL YYIRLRQMAL EGTEVEGCVS CML
//
