ID A0A0R2T8W5_9FLAO Unreviewed; 810 AA.
AC A0A0R2T8W5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=ABR87_03895 {ECO:0000313|EMBL:KRO83644.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO83644.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO83644.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO83644.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO83644.1}.
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DR EMBL; LICF01000006; KRO83644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2T8W5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051535; 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 810 AA; 90453 MW; 8D8882D6C0E299DA CRC64;
MHVLKRDGRK EAIKFDKITA RIQKLCYGLS PLVDSVAVAM RVIEGLYDGV TTSELDSLAA
ETAASMTVRH PDFALLAARI AVSNLHKNTN KSFTETMRDL HTYVSPKTGQ TAPLIADDVM
EIIEANSEML DSTPIYDRDF NYDYFGFKTL ERSYLLRTNG QIAERPQQML LRVAIGIHKE
DIQAAIETYD GMSRGLYTHA TPTLFNAGTP KPQMSSCFLL QMKDDSIDGI YDTLKQCAKI
SQSAGGIGLS IHNIRAMGSY IRGTNGTSNG LIPLLRVFND TARYVDQGGG KRKGSFAMYL
EPWHADVFDF LDLRKNTGKE EQRARDLFYA LWIPDLFMKR VEADAKWTLM CPNECPGLSD
TYGAEFEALY TKYEEGGKGR KTIAARELWT KIMEAQIETG TPYMLYKDAC NAKSNQKNLG
VIRSSNLCTE IIEYTAPDEV AVCNLASIAL PKYVEDGAFD HQLLYDVAYK VTKNLNCVID
VNYYPVPEAR NSNMRHRPIG IGVQGLADTF IKLRLPFTSE EARHLNKDIF ETIYFSAVTA
SCDLAAEHGP YETYEGSPIS QGEFQYNLWG MTEEDLSGRW DWNALRKKVK KHGVRNSLLL
APMPTASTSQ ILGNNECFEP YTSNLYTRRV LSGEFIVVNK HLLVDLVKLG LWNEDVKNAI
MANNGSIQSI EGIPDNLKEL YKTVWEMSMK DIIDMSADRG IFIDQSQSLN LFVESPNMGK
LTSMHFYAWK KGLKTGMYYL RTKAASAAIK FTVKKKAEAA SDATEVFSEI LTASLSAAAT
VSVEPVKVYS AEETLACSID NPDDCEACGS
//
