ID V7JQ84_MYCAV Unreviewed; 705 AA.
AC V7JQ84;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=O982_04235 {ECO:0000313|EMBL:ETB00354.1};
OS Mycobacterium avium 10-5581.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETB00354.1, ECO:0000313|Proteomes:UP000018557};
RN [1] {ECO:0000313|EMBL:ETB00354.1, ECO:0000313|Proteomes:UP000018557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-5581 {ECO:0000313|EMBL:ETB00354.1,
RC ECO:0000313|Proteomes:UP000018557};
RA Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT "Genome sequence of MAC strains.";
RL Submitted (OCT-2013) 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:ETB00354.1}.
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DR EMBL; AYNT01000048; ETB00354.1; -; Genomic_DNA.
DR AlphaFoldDB; V7JQ84; -.
DR PATRIC; fig|1392000.4.peg.902; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000018557; 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}.
FT DOMAIN 557..579
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 705 AA; 80399 MW; BCA31E4BE9A62164 CRC64;
MPDETDYHAL NAMLNLYDAD GKIQFDKDVL AARQYFLQHV NQNTVFFHNQ DEKLDYLIRE
NYYEREVLDQ YSRNFVKALL DRAYAKKFRF PTFLGAFKYY TSYTLKTFDG KRYLERFEDR
VVMVALTLAA GDTGLAEKLV DEIIEGRFQP ATPTFLNSGK KQRGEPVSCF LLRIEDNMES
IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS GVIPIMKLLE DSFSYANQLG
ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG VVIPDITFEL AKKNEDMYLF
SPYDVERVYG LPFADISVTE KYYEMVDDAR IRKTKIKARE FFQTLAELQF ESGYPYIMFE
DTVNRANPID GKITHSNLCS EILQVSTPSL FNDDLSYAKV GKDISCNLGS LNIAKTMDSP
DFAQTIEVAI RALTAVSDQT HITSVPSIEQ GNNDSHAIGL GQMNLHGYLA REGIFYGSEE
GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA SGEFFDKYTE QVWEPATEKV
RQLFADAGIR IPTQDDWKRL KESVQAHGIY NQNLQAVPPT GSISYINHST SSIHPIVSKV
EIRKEGKIGR VYYPAPYMTN DNLEYYQDAY EIGYEKIIDT YAAATQHVDQ GLSLTLFFKD
TATTRDVNKA QIYAWRKGIK TLYYIRLRQM ALEGTEVEGC VSCML
//
