ID A0A0X3UNN8_9ACTN Unreviewed; 822 AA.
AC A0A0X3UNN8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ADL15_17220 {ECO:0000313|EMBL:KUL33737.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL33737.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL33737.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL33737.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
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:KUL33737.1}.
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DR EMBL; LLZH01000134; KUL33737.1; -; Genomic_DNA.
DR RefSeq; WP_067691581.1; NZ_LLZH01000134.1.
DR AlphaFoldDB; A0A0X3UNN8; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000053244; 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:UP000053244}.
FT DOMAIN 18..107
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 822 AA; 90482 MW; 0187BB0D3688D484 CRC64;
MTLTPEKTTV PGQRRHVMQV RKRNGELAPV DVNKIVTAVE RWITGLDEVD PLRVATKTIS
GLYDGATTEE LDKLSIQTAA ELIGEEPQYS RLAARLLIDL VSEEVGEQGV TTFSESIALG
HQQGLISEST LEFVMKFKDK LNNAIDLGND LRFEYFGLRT VADRYLLRHP TKRVPIETPQ
YWLLRVACGL SQTVDEAIGF YRLMSSLAYL PSSPTLFNSG TTHTQMSSCF LVDSPKDELD
SIYERYHQVA KLSKFSGGIG IAWSRVRGRG ALIRGTNGKS NGIVPFLKTL DAGVAAVNQG
GRRKGAACVY LEPWHPDVEE FLELRDNTGE ESRRTHNLNL ANWIPDEFMR RVEADGDWSL
IDPSDAPELP DLFGDEFTEA YRNAEKKAVK TVKARDLYGR MMRTLAQTGN GWMTFKDRSN
ALSNQTGAPG NTIHLSNLCT EILEVNSDAE TAVCNLGSIN LGEHTTADGV DWEKLRATVR
TAVTFLDRVI DINYYPSEQA AASNPRWRPV GLGLMGLQDA FFTLRLPFDS AEAKELSTRV
QEEIFLTALE ASATLAEQFG AHPSYPETRA AKGDLHPELW GATMVQTARW ASVKERIAAH
GLRNSLLIAI APTATIASIA GCYECIEPQV SNLFKRETMS GEFLQVNTYL VRELKARGLW
TAEIRDAIKR AEGSVQEIAE LPADVREIFR TAWELPQKAL IDLAAARAPF IDQSQSLNLF
LSAPTIGKLS SMYLYAWKSG LKTSYYLRSR PATRIQQATT ATAAVTKSPV VSPVVVPAQT
TTLVANPSGA GQVATLSLNL LGDTDGVLAA SLENPDICEA CQ
//
