ID A0A3S9Q6I5_9GAMM Unreviewed; 756 AA.
AC A0A3S9Q6I5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=EKO29_10965 {ECO:0000313|EMBL:AZQ84487.1};
OS Colwellia sp. Arc7-635.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2497879 {ECO:0000313|EMBL:AZQ84487.1, ECO:0000313|Proteomes:UP000286937};
RN [1] {ECO:0000313|EMBL:AZQ84487.1, ECO:0000313|Proteomes:UP000286937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arc7-635 {ECO:0000313|EMBL:AZQ84487.1,
RC ECO:0000313|Proteomes:UP000286937};
RA Lin J.;
RT "Complete Genome Sequences of Colwellia sp. Arc7-635, a Denitrifying
RT Bacterium Isolated from Arctic Seawater.";
RL Submitted (DEC-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}.
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DR EMBL; CP034660; AZQ84487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9Q6I5; -.
DR KEGG; cov:EKO29_10965; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000286937; Chromosome.
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 Gene3D; 1.10.1650.20; -; 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}.
FT DOMAIN 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 756 AA; 84572 MW; 912BB06FEDA879BC CRC64;
MNNIIFVTKR NGSKEPIDLE KIHKVIAWAA EGLDNVSVSQ VELKSHIQFY DGIKTADIHE
TIIKSAADLI SEETPDYQYL SARLAIFHLR KKAYGQFEPP KLYPHVVKLV EAGKYDQHLL
EDYSAEEFEL LETFMDHGRD LDFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYILVAACL
FAKYPKETRL DYVKGFYNAI STFKLSLPTP IMAGVRTPTR QFSSCVLIEC GDSLDSINAT
TSSIVKYVSQ RAGIGINAGR IRALGSTIRN GEAFHTGCIP FYKLFQTAVK SCSQGGVRGG
AATLFYPLWH LEVESLLVLK NNRGVEENRV RHLDYGVQFN KLMYQRLIKG QSITLFSPSD
VPGLYDAFFE DQEKFEELYV KYEADDSIRK KCIKAIELFT LFAQERASTG RIYLQNVDHC
NTHSPFDPSV APIRQSNLCL EIALPTKPME DVNDPNGEIA LCTLSAFNLG AISSLDELEG
LADLAIRALD SLLDYQDYPV PAAHTATMGR RTLGIGVINY AYYLAKNGVF YSNGSANNLT
HRTFEAIQYY LLKASNQLAI EQGACPKFNE TRLSQGILPI DTYKKEIDNI TGEPLHLDWE
TLRTSIKKHG VRNSTVSALM PSETSSQISN ATNGIEPPRG LISIKASKDG VLKQVVPEYQ
RLKDNYELLW NIPSNEGYLQ LVGIMQKFVD QTISANTNYD PSRFEGGKVP IKQVLKDILT
AYKLGVKTMY YHNTRDGADD SQIDADDDCA GGACKI
//
