ID A0A285MFE8_9FLAO Unreviewed; 825 AA.
AC A0A285MFE8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN06265377_0863 {ECO:0000313|EMBL:SNY95197.1};
OS Allomuricauda parva.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1247520 {ECO:0000313|EMBL:SNY95197.1, ECO:0000313|Proteomes:UP000219048};
RN [1] {ECO:0000313|Proteomes:UP000219048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25885 {ECO:0000313|Proteomes:UP000219048};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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; OBEH01000001; SNY95197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285MFE8; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000219048; 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}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 825 AA; 93633 MW; AE36D024FC9A434D CRC64;
MYVLKRDGRK EPMMFDKITA RVRKLCYGLN SLVDPVKVAM RVIEGLYDGV TTSELDNLAA
EIAATMTTTH PDYAKLAARI SVSNLHKNTK KSFSETMKDL YEYVNPRTGK KAPLLSDEVF
KVVEENAEKL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG KIAERPQHML MRVAVGIHLN
DLDAAIETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL AMKDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IAGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYV
EPWHADIFDF LDLKKNHGKE EMRARDLFYA MWIPDLFMKR VEADAEWTLM CPNECPDLFN
THSEEFEALY TKYESEGKGR KTIRARELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE IMEYTSPDEV AVCNLASIAL PMFVKNGAFD HKELFRVTKR VTKNLNRVID
RNYYPVKEAE NSNMRHRPIG LGVQGLADTF IMLRLPFTSD EAKQLNQEIF ETLYFAAVTA
SMEASKEEGV YSTYEGSPIS EGKFQHNLWG IKDEELSGRW DWTKLRKDVK KHGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVKLG LWNENLKQEL
MRANGSVQDI DVVPDDIKEL YKTVWELSMK DVIDMSRHRG YFIDQSQSLN LFMENANYSK
LTSMHFYAWK SGLKTGMYYL RTKAAVDAIK FTLDNTKKKE VPVSVAAEAE VVAATPNTVE
DLKVEATPVT QQEVDIQPMT AEEMKEMIAR AKEGQADDDC LMCGS
//
