ID A0A0Q5UQ28_9FLAO Unreviewed; 797 AA.
AC A0A0Q5UQ28;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ASG38_03780 {ECO:0000313|EMBL:KQS50108.1};
OS Flavobacterium sp. Leaf359.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS50108.1, ECO:0000313|Proteomes:UP000051024};
RN [1] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS50108.1}.
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DR EMBL; LMPW01000010; KQS50108.1; -; Genomic_DNA.
DR RefSeq; WP_056067882.1; NZ_LMPW01000010.1.
DR AlphaFoldDB; A0A0Q5UQ28; -.
DR STRING; 1736351.ASG38_03780; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051024; 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:UP000051024}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 797 AA; 90964 MW; 4BF2B74FE75A9D1C CRC64;
MYVVKRDGHR EPVMFDKITD RIKKLCYGLN DLVDPVKVAM RVIEGLYDGV TTSELDNLAA
ETAAAMTIAH PDYAQLAARI AISNLHKNTK KSFSETMKEM YFYVNPRTNQ ESPLLSEEVY
NVIQENAAFL DSHVIYNRDF NYDYFGFKTL ERSYLLKING KIVERPQHML MRVAVGIHLN
DLDAVLETYD LMSKKFFTHA TPTLFNAGTP KPQMSSCFLL AMQDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IRGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYI
ETWHADIFDF LDLKKNHGKE EMRARDLFFA MWTSDLFMKR VQEDSTWTLM CPNECPGLYD
VYGEEFEALY TSYEEQGRGR KTIKARELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE IMEYTSKDEI AVCNLASISL PMFVENGQFN HELLYNVTKR VTRNLNKVID
RNYYPVPEAE NSNMRHRPVG LGVQGLADAF ILLRMPFTSD EAKKLNQEIF ETLYFAAVTA
SMEMAKEEGP YSTFEGSPIS QGEFQYNLWG LKDEDLSGRW DWASLRKEVM ENGVRNSLLV
APMPTASTSQ ILGNNEAFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVELG LWNEDLKQEI
MRHNGSIQNI DIIPQDLKEL YKTVWEMSMK DIIDMSRQRG YFIDQSQSLN LFMQDANFAK
LTSMHFYAWQ SGLKTGMYYL RTKSAVDAIK FTLNNDKKAE PVAVETVAEP AIAVDEFRAM
LERSKNAEPD DCEMCGS
//
