ID U2Q892_9FUSO Unreviewed; 699 AA.
AC U2Q892;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=HMPREF1552_00685 {ECO:0000313|EMBL:ERK52596.1};
OS Leptotrichia sp. oral taxon 879 str. F0557.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1227268 {ECO:0000313|EMBL:ERK52596.1, ECO:0000313|Proteomes:UP000016622};
RN [1] {ECO:0000313|EMBL:ERK52596.1, ECO:0000313|Proteomes:UP000016622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0557 {ECO:0000313|EMBL:ERK52596.1,
RC ECO:0000313|Proteomes:UP000016622};
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 (AUG-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:ERK52596.1}.
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DR EMBL; AWVL01000047; ERK52596.1; -; Genomic_DNA.
DR RefSeq; WP_021745374.1; NZ_KI271359.1.
DR AlphaFoldDB; U2Q892; -.
DR STRING; 1227268.HMPREF1552_00685; -.
DR PATRIC; fig|1227268.3.peg.637; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_0; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016622; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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 CDD; cd01679; RNR_I; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
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; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 557..579
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 699 AA; 80615 MW; BE9ECD5DF3EEFA4C CRC64;
MVDKIAKKWI YLNNEIMVKQ GEDFQLEKDK EAVYSYFVDY VNKNTVFFHN LEEKMGYLIK
NDYYIDFYEM YSHDEIKEVF KLVYDKKFRF ASFMSASKFY QSYALMDDTG EKFLERYEDR
IATVSLYLAQ GNVEKAKEYA LMLINQEYQP ATPTFLNSGK KRSGELVSCF LDEMGDNLSG
IGYVFDSSMK LSSIGGGVSI NLSKVRARGE SIKGVEGRAS GVLPIMKILE DIFSYANQLG
QRAGAGAVYL NVFHSDINEF LDSKKINVDE KIRIKSLSIG VIVPDKFMQL AMEDEVCYTF
NPHTVFLEYG QYLDEMDMNK MYEKLVDNPN VKKKKINARE LLVKISQTQK ESGYPYLFFK
DNANKEHALK EIGTVKFSNL CTEIMQLSEV SDINAYYEQD TIRRGISCNL GSLNIATVMK
NKRIKEATKA AIDSLTMVSD LTNIDIVPSI KKANDELHSV GLGAMNLHGY LAKNFIMYES
KEALDFCNVF FMMVNFYSLE RSMEIAKEKG ETFKDFEKSE YANGNYFDKY ITKEYMPQTE
KIKQLFEGIY IPTKEDWANL KEQVMKHGIY NAYRMAIAPN QSTSYIMNST ASVMPVVDTI
EVREYGDSTT FYPMPYLTND NYFFYKSAYD MDQKNILKLI SVIQRHVDQG ISTILYTKST
DSTRDLARLY IYAHRLGLKS LYYTRTRKAT IEECISCSV
//
