ID A0A1H0H7K2_9ACTN Unreviewed; 792 AA.
AC A0A1H0H7K2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05192576_3489 {ECO:0000313|EMBL:SDO15118.1};
OS Nocardioides szechwanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005944 {ECO:0000313|EMBL:SDO15118.1, ECO:0000313|Proteomes:UP000199004};
RN [1] {ECO:0000313|EMBL:SDO15118.1, ECO:0000313|Proteomes:UP000199004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11147 {ECO:0000313|EMBL:SDO15118.1,
RC ECO:0000313|Proteomes:UP000199004};
RA de Groot N.N.;
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}.
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DR EMBL; FNIC01000006; SDO15118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0H7K2; -.
DR STRING; 1005944.SAMN05192576_3489; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000199004; 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:UP000199004}.
FT DOMAIN 14..103
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 87744 MW; 4F06BFCDA010666A CRC64;
MTVTDLGTET RTTMSVRKRN GDSEPVDVNK IVKAVDRVAR DLADVDPMRV ATRTISGLYD
GATTAELDRL SIQTAAEMIG EEPQYSRLAG RLLAGYVEKE VRNQGVASFS QSVSLGHAEG
LIGDETASFV KDNARKLDFA VDPAGDQRFE YFGLRTVYDR YLLRHPSTRQ VIETPQYFLL
RVACGLAQSP GEAIRFYRLM SSLAYLPSSP TLFNSGTRHT QMSSCYLVDS PRDDLDSIYG
RYAQVAKLSK FAGGIGIAFS RVRSRGALIR GTNGQSNGIV PFLRTLDSSV AAVNQGGRRK
GAACVYLEPW HPDVEEFLEL RDNTGEDARR THNLNLANWV PDEFMRRVEA DEVWSLVDPD
QAPELPDLWG PAFDEAYRRV EAEGRYVRQV KARDLYARMM RTLAQTGNGW MTFKDAANRT
CNQTRDTPGG PVVHLSNLCT EIIEVSSDGE TAVCNLGSVN LAQHVTREGM DWDKLRETVR
TAVPLLDRVI DINFYPSVES AASNPRWRPV GLGLMGLQDV FFALRLAFDS DEAQELSTRI
SEEIYLTALE VSCELARRHG AHPSYDETRA ATGVLQPDLW DVTGSQTERW AALRADIAEN
GLRNSLLVAI APTATIASIA GCYECIEPQV SNLFKRETLS GEFLQVNAAL TRELKALGLW
TPEVREAIKR AEGSVQGIRE LPDDVRLLFR TAWELPQRAL IDMAAARSPY IDQSQSLNLF
LAGPSIGKLS SMYLHAWKAG LKTTYYLRSR PATRITQTTT SVNAPVAIPL TMSDDEALAC
SLENPENCEA CQ
//
