ID A0A0R2SGK2_9FLAO Unreviewed; 802 AA.
AC A0A0R2SGK2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
DE Flags: Fragment;
GN ORFNames=ABR83_03405 {ECO:0000313|EMBL:KRO72443.1};
OS Cryomorphaceae bacterium BACL18 MAG-120924-bin36.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655591 {ECO:0000313|EMBL:KRO72443.1, ECO:0000313|Proteomes:UP000051105};
RN [1] {ECO:0000313|EMBL:KRO72443.1, ECO:0000313|Proteomes:UP000051105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL18 MAG-120924-bin36 {ECO:0000313|EMBL:KRO72443.1};
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:KRO72443.1}.
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DR EMBL; LIBP01000039; KRO72443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2SGK2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051105; 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"
FT NON_TER 802
FT /evidence="ECO:0000313|EMBL:KRO72443.1"
SQ SEQUENCE 802 AA; 90073 MW; 020A3177DBCA3D32 CRC64;
MHVIKRDGRK EAVKFDKITA RIQKLCYGLS PLVDPTAVAL RVIEGLYDGV TTSELDSLAA
EVSASMTVRH PDFAQLAARI AVSNLHKNTN KSFTETMRAM HQYVNPKTNQ AAPLIADDVM
EIVEKNSELL DSTVIYDRDF SYDYFGFKTL ERSYLLRTNG RIAERPQQML LRVSLGIHKE
DIQAAIETYD GMSRGLYTHA TPTLFNAGTP KPQMSSCFLL QMADDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IRGTNGTSNG LIPLLRVFND TARYVDQGGG KRKGSFAVYL
ETWHADIFDF LDLKKNTGKE ELRARDLFYA MWISDLFMER VEADGEWTLM CPNECPGLYD
TYGDAFKVMY EDYERAGKGR RTIKARELWT KILESQIETG TPYMLYKDAA NEKSNQKNLG
TIRSSNLCTE IMEYTAPDEI AVCNLASIAL PKYLDNGAFD HQMLYDITYK VTHNLNDVID
QNYYPVPEAR NSNMRHRPVG LGVQGLADAF IKLRLPFTSP EARQLNKDIF ETIYFAAVTA
SCDLAKRDGA YETFKGSPIS EGKFQFNLWG VTEDELSGRW DWKALRKEVM KHGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNLYTRRV LSGEFIVVNK HLLIDLVKLG LWNDDVKNAI
MANNGSIQAI DGIPDNIKEL YKTVWELSMR DIIDMAADRG LFIDQSQSLN LFVESPNMGK
LTSMHFYAWK KGLKTGMYYL RTKAASAAIK FTVKKKSESA SVTEVFSEVV VKEQQEALAA
MATPDVKLYS SEEAVACSLD NP
//
