ID A0A3G2L5X5_9FLAO Unreviewed; 595 AA.
AC A0A3G2L5X5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=D1013_10010 {ECO:0000313|EMBL:AYN67679.1};
OS Euzebyella marina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Euzebyella.
OX NCBI_TaxID=1761453 {ECO:0000313|EMBL:AYN67679.1, ECO:0000313|Proteomes:UP000276309};
RN [1] {ECO:0000313|EMBL:AYN67679.1, ECO:0000313|Proteomes:UP000276309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN62 {ECO:0000313|EMBL:AYN67679.1,
RC ECO:0000313|Proteomes:UP000276309};
RA Xue C.;
RT "The reduced genetic potential of extracellular carbohydrate catabolism in
RT Euzebyella marina RN62, a Flavobacteriia bacterium isolated from the hadal
RT water.";
RL Submitted (AUG-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|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; CP032050; AYN67679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G2L5X5; -.
DR KEGG; emar:D1013_10010; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000276309; Chromosome.
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; IPR013350; RNR_alpha.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02510; NrdE-prime; 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; 3.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003410,
KW ECO:0000313|EMBL:AYN67679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276309}.
FT DOMAIN 43..110
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 114..232
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 237..418
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 423..574
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 595 AA; 67576 MW; FF310A5A2ADD7B50 CRC64;
MDNKTQTLSS TEQENKTIDL VNARKNALAE LKSNSAEGNF AWLNENSRKF LASGYLTDGV
TPEGRIREIA ERAEEILQIP GYADKFYHYM SEGFFSLASP VWSNFGKKRG LPISCFGSHI
DDDMGNILYT QSEVGMMSKL GGGTSGYFGN IRHRGAPVKN NGQASGAVHI MQLFESMVDV
VSQGSVRRGR FSPYLPIEHK DILEFLEIGT EGNPIQQLTH GVTVTNEWMQ EMIDGDVEKR
TVWAKVLQRR GEMGYPYVFF TDNANNGAAE VYQENNYKIH ASNLCTEIML PSNDNWSFVC
VLSSINLLHY DKWKDTDAVE TMVYFLDATI TEFIEKLEAY RDSSNREDRQ TFLFMERAYN
FAKQNRALGL GALGWHSLLQ SKRLAFDSQE AYNLNNEIFR EIKERSYKAS SELAVKFGEP
DVLKGYGRRN ATLNAIAPTT SSAFILGQVS QGIEPIWSNC YVKDIAKIKT TIKNPYLMEL
LEEKGMNVAE VWKDIRDHDG SVQHLEFLTD EEKAVFKTYS ELDQLDIVYQ AAARQHHIDQ
GQSLNIIVHP EMPVKQINKI HVTAWKLGLK SMYYQHSMNA AQKFRQKKEC TSCEA
//
