ID A0A124HZS2_9ACTN Unreviewed; 793 AA.
AC A0A124HZS2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AQJ54_03935 {ECO:0000313|EMBL:KUN71910.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN71910.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN71910.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN71910.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-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:KUN71910.1}.
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DR EMBL; LMWV01000002; KUN71910.1; -; Genomic_DNA.
DR RefSeq; WP_062233907.1; NZ_KQ948734.1.
DR AlphaFoldDB; A0A124HZS2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054375; 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; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 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 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:UP000054375}.
FT DOMAIN 595..617
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87277 MW; 6F001D34DE47E6DF CRC64;
MTIAPADPAS AAIERTEQRT EQENDGPGAA LLRTLAELTA DLPDADPGRV AAAALRGRSA
RADESELREL ATEAAAGLIS EDPAYSRLAA RLLTISIAAE AASQGVTSFT GSVAVGHREG
LIADRTAEFV RVHAERLDAL VDTEADDRFG YFGLRTLHSR YLLRHPITRK VIETPQHFML
RVASGLAEDD TVRALDEVAA LYGLMSRLDY LPSSPTLFNS GTRHPQMSSC YLLDSPMDEL
DSIYDRYHQV ARLSKHAGGI GIAYSRVRSR GSLIRGTNGH SNGIVPFLKT LDASVAAVNQ
GGRRKGAAAV YLETWHSDIE EFLELRDNTG EDARRTHNLN LAHWIPDEFM RRVNADAEWS
LFSPADVPEL VDLWGEEFDA AYRAAEQKGL AKRTIPARDL YGRMMRTLAQ TGNGWMTFKD
AANRTANQTA LPGHTVHSSN LCTEILEVTD DGETAVCNLG SVNLGAFVDT RTGDIDWERL
DETVRTAVTF LDRVVDINFY PTEQAGRSNA KWRPVGLGAM GLQDVFFKLR LPFGSPEAQA
LSTRIAERIM LAAYEASTDL AERSGPLPAW EKTRTAQGVL HPDHYATDLA WPERWAALRE
RMATTGLRNS LLLAIAPTAT IASIAGVYEC IEPQVSNLFK RETLSGEFLQ VNSYLVNDLK
ALGVWDARTR EALREANGSV QDFAWVPEDV RALYRTAWEI PQRSLIDMAA ARTPFLDQSQ
SLNLFLETPT IGKLSSMYAY AWKSGLKTTY YLRSRPATRI ARAAQATVPV QQVTSEEAVA
CSLENPESCE ACQ
//
