ID U2RD45_LEPWF Unreviewed; 1034 AA.
AC U2RD45;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HMPREF9015_01704 {ECO:0000313|EMBL:ERK48672.1};
OS Leptotrichia wadei (strain F0279).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=888055 {ECO:0000313|EMBL:ERK48672.1, ECO:0000313|Proteomes:UP000016626};
RN [1] {ECO:0000313|EMBL:ERK48672.1, ECO:0000313|Proteomes:UP000016626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0279 {ECO:0000313|EMBL:ERK48672.1,
RC ECO:0000313|Proteomes:UP000016626};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERK48672.1}.
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DR EMBL; AWVM01000090; ERK48672.1; -; Genomic_DNA.
DR AlphaFoldDB; U2RD45; -.
DR PATRIC; fig|888055.3.peg.1633; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR HOGENOM; CLU_000404_4_1_0; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016626; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 569..610
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
SQ SEQUENCE 1034 AA; 119750 MW; 871E7CA6A97CD51B CRC64;
MVDNRAKKWI YLNNEIMVKK GEDFQLEKDK EAVYSYFVDY VNKNTVFFHN LEEKMRYLIK
NDYYIDFYQM YSHDEIKELF KMVYDKKFRF ASFMSASKFY QSYALMDDTG EKFLERYEDR
ISAVSLYLAQ GNFEKAKEYA LMLINQEYQP ATPTFLNSGK KRSGELVSCF LDEMGDNLSG
IGYIFDSSMK LSSIGGGVAI NLSKIRARGE SIKGVEGRAS GVLPIMKILE DIFSYANQLG
QRAGAGAVYL NVFHSDINEF LDSKKINVDE KIRIKSLSIG VIIPDKFMQL AMEDEVCYTF
NPHTVFLEYG QYLDEMDMNE MYEKLVDNPN VKKKKINARE LLVKISQTQK ESGYPYLFFK
DNANREHALK EIGAVKFSNL CVAPYTKILT KEYGYTEIGQ HENEKVHVWN GEEWSKTTVI
KTGTDQKLLK VSTDNFQTVD VTPYHKFYIK DENEKVVEKR AHELKVGDRL IKFDLPKYEN
ENREILENAY ANGFYSGDGC EYDVKDRKNL TNKMIYLYGE KKELLDKFDD LEYSKSENED
RIILNHCKGL KDKFFVPFNY EISSIVKWLS GLADADGTIS KNNGNNSLQI ASTNLEFLSN
IRLLLQEIGI HSKINKMRDT EIRELPLNNG TDECGEFECK ALYRLLITHK NLQKLVELGF
ETFRLKFDLE HTPNRDACAF EKITSVEEID GVYDTYCFTE EKRHMGMFNG MLLGNCTEIM
QLSEVSDINA YYEEDTIRRG ISCNLGSLNI ATVMENKRIK ETTKAAIDSL TMVSDLTNID
VVPTIKKANE ELHSVGLGAM NLHGFLAKNF IMYESKEALD FCNVFFMMVN FYSLERSMEI
AKERGETFKD FEKSEYANGN YFNKYVTKEY MPQTEKVKSL FEGIYIPTKE DWANLKEQVM
KHGVYNAYRM AIAPNQSTSY IMNSTASVMP VVDTIEVREY GDSTTFYPMP YLTNDNFFFY
KSAYDMDQKN ILKLISVIQR HVDQGISTIL YTKSTDSTRD LARLYIYAHR LGLKSLYYTR
TRKAMIEECI SCSV
//
