ID A0A239PW26_9PROT Unreviewed; 656 AA.
AC A0A239PW26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN06297382_2219 {ECO:0000313|EMBL:SNT74511.1};
OS Amphiplicatus metriothermophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Amphiplicatus.
OX NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT74511.1, ECO:0000313|Proteomes:UP000198346};
RN [1] {ECO:0000313|EMBL:SNT74511.1, ECO:0000313|Proteomes:UP000198346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT74511.1,
RC ECO:0000313|Proteomes:UP000198346};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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; FZQA01000005; SNT74511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PW26; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198346; 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 Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
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; 2.
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.
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:UP000198346}.
FT DOMAIN 50..115
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 119..438
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 447..592
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71805 MW; 24EDD506A3E6156A CRC64;
MSLSTEAAER VEAASPAGGA ADPAATPAPA RRPALKVVRD IVLDRSRDAL LTDFGKKTLE
DRYLLPGESF QDMFARVART YGDDADHAQR IYDYISKLWF MPATPILSNG GANRGLPISC
FLNAVGDSLE EIVGVWNENV ALASNGGGIG TYWGGVRSIG EKVKGAGQTS GIIPFIRVMD
SLTLAISQGS LRRGSAAVYL DIHHPEIEEF LEIRKPSGDF NRKSLNLHHG VNVTDEFMTA
VLQDAEFALR SPKTGETLRA VSARKLWQKI LETRLATGEP YLVFSDTVNR QMAKHQRDLG
LKVSTSNLCS EIMLHTGPDH LGEDRTAVCC LSSINAEKYF EWKDEPLFVE DVMRFLDNVL
EDFIRRAPAS MAKAVYSARR ERSVGLGLMG FHSFLQQQGV PFESAMAKAW NIRLFKHIRM
GADAASVKLA EERGACPDAA ERGVKQRFSH KLAIAPTASI SIICGGCSPC IEPIPANVYV
HKTLSGSFTV KNAALEKLLA EKGHDTDETW ASIIEHEGSV QHLDCLTDEE KAVFKTAFEI
DQRWVIELAA DRAPLVCQGQ SVNVFLPGDI DKWDLHMLHW TAWEKGVKSL YYCRSKSVQR
ASYAGGRKGE AGAAALDRAE ARAAEAAAAP GDDAPDMQTL MQAAARTDYD ECLACQ
//
