ID A0A1F6EIY7_9BACT Unreviewed; 936 AA.
AC A0A1F6EIY7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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};
GN ORFNames=A3A34_02985 {ECO:0000313|EMBL:OGG73615.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_50_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798507 {ECO:0000313|EMBL:OGG73615.1, ECO:0000313|Proteomes:UP000178587};
RN [1] {ECO:0000313|EMBL:OGG73615.1, ECO:0000313|Proteomes:UP000178587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG73615.1}.
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DR EMBL; MFLU01000016; OGG73615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6EIY7; -.
DR STRING; 1798507.A3A34_02985; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000178587; 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 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 3..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 915..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 104647 MW; 8E41016445502A05 CRC64;
MTTFITKRDG KIEPFNADKI NRSIERACVG LLDPVGMVTQ IATETQLTIY DGISTEEMDE
ATINAAVQNI KEDTEYDIIA VRLFLKTIYR RVVGEYDHDP QILRQKHRSG FSSYIQNGIG
SGLLDPRMGE LFDLEVLAGV LSLMRDELFT YAGLSTLMNR YALKGGDRKP IETPQYFFMR
VAMGLAYNEK EPTLWAKKFY NHMSRHLYIA GGSTNLGAGT TRPSLSNCFL LEVHDDIEHI
AKSVADVMKI SKASGGLGVS MTKLRASGSP LSSSNTVSSG PTPFAKIMDT AIRAIQRGGK
KLGAMCFYME NWHLSFQEFI DWKHNAGDDY LRMRTANTAV FLSDEFMRRV ERGEDWYMFD
PKETPDLNEL YGSAFSKRYE EYVEMAREGK MRMWKRVPAR EQWHQILTSL QSTSHPWLTW
KDPINLRALN NNTGTIHMSN LCTEICLPQD KDNIAVCNLA SLNLSTHVEH KQINWVLLEE
SVRLAVRQLD NLIDINVIPI PEATRSDREN RAVGLGLMGL ADTLEQLGMP YESPHAADFV
DRAFEFVSYI AIDESANLAH ERGSYKNFTG SGWSRGIVPL DTMKTLEEDR GAVIELPNGT
RNRRLNWDAL RAKVKEGIRN ATLLAVAPNA NIGLVAGTTP GIDPRFAQVF SRNKISGKYL
DLNRNLVKDL KNMGLWEDVR ERIIESQGDI TDIPEIPAYL KDIYKTSFAT SPYAFIEIAA
RAQKWVDQAL SRNMYLESRD MDEMKNIYMT AWRKGLKTTY YLHMKPRHSA EQSTIAVNKA
EKLGKRGFAA AKSAHAPTLE APVVSSFSAA SFSRQESVRQ DKKQELGGFS AVSKTVQSKP
TVSDMLNAKA ADRNDGRQAP LPAATVKNPA ISLEDMSSAI GSTKSDLGQT KSVVNETDSA
LETPIARDGF SSARSLTHVH NGPSDPQEKL VCDACQ
//
