ID A0A3B0CHA4_9FLAO Unreviewed; 829 AA.
AC A0A3B0CHA4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D7Z94_01825 {ECO:0000313|EMBL:RKN82606.1};
OS Ulvibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacterium.
OX NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN82606.1, ECO:0000313|Proteomes:UP000276603};
RN [1] {ECO:0000313|EMBL:RKN82606.1, ECO:0000313|Proteomes:UP000276603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM003 {ECO:0000313|EMBL:RKN82606.1,
RC ECO:0000313|Proteomes:UP000276603};
RA Zhang Z.;
RT "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT prolifera.";
RL Submitted (OCT-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}.
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:RKN82606.1}.
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DR EMBL; RBCJ01000001; RKN82606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0CHA4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000276603; 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:UP000276603}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 829 AA; 94195 MW; 363F35118B06043E CRC64;
MYVVKRDGRK EPMMFDKITA RVRKLCYGLN ELVDPIKVAM RVIEGLYDGV TTSELDNLAA
EQAATMTTTH PDYAKLAARI SVSNLHKNTK KSFSETMKDL YEYINPRTGK KAPLLSDEVY
KVVSENSEKL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG KIAERPQHML MRVAVGIHLN
DLESALETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL AMKDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IAGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYV
EPWHADIFDF LELKKNHGKE EMRARDLFYA MWIPDLFMKR VEANENWTLM CPNECPGLFS
NHSEEFEKLY LKYEAEDKGR KTVKARDLWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE ILEYTSPDEV AVCNLASIAL PMFIKGGKFD HKELFKVTKR VTKNLNRVID
RNYYPVKEAE NSNMRHRPIG LGVQGLADTF ITLRLPFTSD EAKELNHDIF ETLYYAAVTA
SMEEAKEDGA YSSFKGSPIS EGKFQHNLWG IKDEELSGRW DWVKLRKQVM KHGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVKLG IWNENLKQEL
MRANGSIQHI DIIPEEIKEL YKTVWELSMK DIIDMSRQRG YFIDQSQSLN LFMENANYSK
LTSMHFYAWK SGLKTGMYYL RTKAAVDAIK FTLDNTKKKE IPVSVAAEAE VAAAIPPAPE
EAKAIEVKPT PVVQQQESDI RPMTAEEMKE MIARAKEGQA DDDCLMCGS
//
