ID A9DN45_9FLAO Unreviewed; 812 AA.
AC A9DN45;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=KAOT1_18147 {ECO:0000313|EMBL:EDP97110.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97110.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP97110.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP97110.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
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:EDP97110.1}.
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DR EMBL; ABIB01000002; EDP97110.1; -; Genomic_DNA.
DR RefSeq; WP_007096163.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DN45; -.
DR STRING; 391587.KAOT1_18147; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_1_0_10; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002945; 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:UP000002945}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 812 AA; 91992 MW; 7DD893538208F43A CRC64;
MFVVKRDGRK EPMMFDKITS RVRKLCYGLN NLVDPVKVAM RVIEGLYDGV TTSELDNLAA
EIAATMTTTH PDYARLAARI SVSNLHKNTK KSFSETMVDL YEYVNPRTGK KAPLLSDEVY
NVIMENADRL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG KIAERPQHML MRVSVGIHLN
DLDAAIETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL AMQDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IAGTNGTSNG IVPMLRVYND TARYVDQGGG KRKGSFAIYV
EPWHADIFDF LDLKKNHGKE EMRARDLFYA MWIPDLFMKR VEENGPWTLM CPNECPNLFN
VHSEEFEALY LKYEAEGKGR KTIKARELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE IMEYTSPDEV AVCNLASIAL PMFIKGGEFD HKELFRVTKR VTKNLNKVID
RNYYPVKEAE NSNFRHRPIG LGVQGLADTF IKLRMPFTSD EAKKLNQEIF ETLYFAAVTA
SMEMAKIEGP YQTYEGSPMS KGEFQHNLWG IKDEELSGRW DWGKLRKQVA KNGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVNLG LWTEDLKQEL
MRANGSIQHI DEIPQDIKDL YKTVWELSMK DIIDMSRHRG YFIDQSQSLN LFMEGATMAK
LTSMHFYAWR SGLKTGMYYL RTKSAVDAIK FTVKKAKKSI AVPAEAAAGI SVQTTGSKPA
PVAVEPLTPE EMKEMIARAK DGQDDDCLMC GS
//
