ID A0A2T0RRS5_9ACTN Unreviewed; 759 AA.
AC A0A2T0RRS5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CLV70_11436 {ECO:0000313|EMBL:PRY23905.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY23905.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY23905.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY23905.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY23905.1}.
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DR EMBL; PVZG01000014; PRY23905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RRS5; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000239209; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PF03477; ATP-cone; 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; PS51161; ATP_CONE; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000239209}.
FT DOMAIN 1..93
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 759 AA; 84275 MW; 39ACF49210735344 CRC64;
MRVRKRNGDL ETVDVNKIVK AVERWVADLD EVDPLRVATR TISGLYDGAT TAELDKLSIQ
TAAELIGEEP QYSKLAARLL ATFVDKEVRN QGVATFSQSI RHAHQQGLIG DGTAAFVARN
ARKLDDAVDV AGDLRFEYFG LRTVADRYLL RHPLSRDVLE TPQYWLLRVA CGLSQTPAEA
IDFYRLMSSL AYLPSSPTLF NSGTRHTQLS SCFLVDSPRD ELDSIYERYH QVAKLSKFSG
GIGISWSRVR GRGALIRGTN GRSNGIVPFL KTLDAGVAAV HQGGRRKGAA CVYLEPWHPD
IEEFLELRDN TGEESRRTHN LNLANWIPDE FMRRVEADGD WSLVDPSDAP ELPDLVGDEF
DEAYRRAEKN AVRTVKARDL YGRMMRTLAQ TGNGWMTFKD RANALSNQTG APGNTIHLSN
LCTEILEVNS DDETAVCNLG SINLGAHLAG GGVDWEKLRA TVRTAVVFLD RVIDLNFYPS
EQAGRSNPRW RPIGLGLMGL QDAFFALRLP FDSAEAKELS TRVQEEIFLT ALESSVALAE
RFGPHPAYPE TRAAQGDLHH ELWGATPSQT ERWAGLKTRI AEHGLRNSLM IAIAPTATIA
SIAGCYECIE PQVSNLFKRE TMSGEFLQIN TYLVRELKAR GLWTAPIRER IKRAEGSVQG
IADLPADVRE LFRTAWELPQ RALIDLAAAR APYIDQSQSL NLFLSAPTIG KLSSMYLHAW
KAGLKTSYYL RSRPATRIQQ ATTAVACSLE NPESCEACQ
//
