ID U2TF85_9ACTN Unreviewed; 839 AA.
AC U2TF85;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=HMPREF1248_0470 {ECO:0000313|EMBL:ERL11709.1};
OS Coriobacteriaceae bacterium BV3Ac1.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL11709.1, ECO:0000313|Proteomes:UP000016652};
RN [1] {ECO:0000313|EMBL:ERL11709.1, ECO:0000313|Proteomes:UP000016652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-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:ERL11709.1}.
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DR EMBL; AWUP01000018; ERL11709.1; -; Genomic_DNA.
DR AlphaFoldDB; U2TF85; -.
DR PATRIC; fig|1111135.3.peg.1333; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9804622at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016652; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016652}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 839 AA; 95799 MW; 224F312F2DDDA4F4 CRC64;
MQIIKRNGSL EEYDSSKIAR AIEKSFAATS TKPAEDEIAK LVSQIERRMA EEHATSVEHI
QDLVEEVLMR EGHFAQAKSY ILYRSRRTEL RQQRQEIVGL VGDEGIDALI LRIQHDFLDE
QYSSSALLNR FRGFLTEDMA YQQRLEALVR AAVELTSKEA PKWSYIAARL LAYSHHAKIN
KLMAARSIES FYDKLRYLTE LGLYGTYILE SYTREEINQA ASFIDNSRDD LFDYAGLDLM
LHRYVIRSFE GEALETPQEM FLGIALHLAM QEKPAVRLGW IKRFYDMLST LKVTMATPTL
SNARRPQHQL SSCFIDTVPD SLEGIYRSIA NFSQVSKFGG GMGMYLGKVR AAGGSIRGYK
GAAGGVIRWI RVINDTAVAV DQLGVRSGAV AVYLDVWHRD LPEFLQLRTN NGDERMKAHD
VFPAVCYPDL FWKMAKENMS QDWYLMDPHD ILTVKGYAIE DYFGDEWEKR YLDCVADSRI
PKRTLPIREL VRLILRSAVE TGTPFAFMRD TVNRANPNPQ AGVIYCSNLC TEIAQNTSAM
ESVSQEVITK EGDTVVVNTT RPGDFVVCNL ASLTLGRINV EDDEELRQII HSLVRALDNV
IDLNFYALPY AKITNHRYRS IGLGVSGYHH MLAKRHIRWE SEEHLRFVDD VFERINRHAI
EASSALAAEK GSYRYFEGSD WQTGAYFDKR GYTGEVWDSL RRRVAVQGMR NAYLLAVAPT
SSTSILSGTT AGLDPLMKRF FLEEKKGMML PRIAPELSMD TYWYYNAAHN TNQLWSVRAA
GVRQRHIDQA QSMNLYITNE YTMSQVLKLY IEAWEHGVKT LYYVRSKSLE VEECESCSS
//
