ID A0A0D1J803_9MYCO Unreviewed; 693 AA.
AC A0A0D1J803;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=TL10_07330 {ECO:0000313|EMBL:KIU17708.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU17708.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU17708.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU17708.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-2015) 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:KIU17708.1}.
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DR EMBL; JXST01000007; KIU17708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1J803; -.
DR STRING; 280871.TL10_07330; -.
DR PATRIC; fig|280871.6.peg.1517; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000032221; 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:UP000032221}.
FT DOMAIN 545..567
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 693 AA; 78890 MW; 29A71279733CADFB CRC64;
MLNLYDADGK IQFDKDALAA REYFLQHVNQ NTVFFHSQDE KLDYLIEKEY YEREVLDQYS
RNFVKELLDR AFAKKFRFPT FLGAFKYYTS YTLKTFDGKR YLERFEDRVV MVALTLAAGD
TELAEKLVDE IIDGRFQPAT PTFLNSGKKQ RGEPVSCFLL RIEDNMESIG RSINSALQLS
KRGGGVALLL SNIREHGAPI KNIENQSSGV IPIMKLLEDS FSYANQLGAR QGAGAVYLHA
HHPDIYRFLD TKRENADEKI RIKTLSLGVV IPDITFELAK KNEDMYLFSP YDVEKVYGVP
FADVNVTEKY YEMVDNGAIR KTKIKAREFF QTLAELQFES GYPYIMYEDT VNRANPIAGK
ITHSNLCSEI LQVSTPSEFN EDLSYAKVGK DISCNLGSLN IAKAMDSPDF AQTIEVSIRA
LTAVSDQTHI WSVPSIEQGN NDSHAIGLGQ MNLHGYLARE QIYYGSDEGI DFTNIYFYTV
LFHALRASNR IAIERGSKFG GFEKSKYASG EFFDKYTEQA WEPKTDKVRQ LFADAGIHIP
TQDDWRSLKE SVQAHGIYNQ NLQAVPPTGS ISYINHSTSS IHPVASKIEI RKEGKIGRVY
YPAPYLTNDN LEYYQDAYEI GYEKIIDTYA AATQHVDQGL SLTLFFKDTA STRDVNKAQI
YAWRKGIKTL YYIRLRQMAL EGTEVENCVS CML
//
