ID A0A1G4M7R5_LACFM Unreviewed; 877 AA.
AC A0A1G4M7R5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LAFE_0B04676G {ECO:0000313|EMBL:SCV99886.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCV99886.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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|ARBA:ARBA00024942,
CC 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|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; LT598489; SCV99886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4M7R5; -.
DR STRING; 4955.A0A1G4M7R5; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000190831; Chromosome b.
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:UP000190831}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 877 AA; 99059 MW; 6C358AE2E17D689B CRC64;
MFVYKRDGRQ EPVKFDKITA RISRLCYGLD PKHIDAVKIT QRIISGVYEG VTTVELDNLA
AETCAYMTTI HPDYATLAAR LAISNLHKQT TKQFSQVVSD LYHYVNPKNG IHSPMISKEV
YGIVMEHKDE LNSAIVYDRD FQYNYFGFKT LERSYLLRID GKVAERPQHL IMRVAVGIHG
RDIERVLETY NLMSLRYFTH ASPTLFNAGT PHPQMSSCFL VAMKEDSIEG IYDTLKECAM
ISKTAGGIGL HIHNIRSTGS YIAGTNGTSN GIIPMVRVYN NTARYVDQGG NKRPGAFAIY
LEPWHSDIFD FVDIRKNHGK EEIRARDLFP ALWVPDLFMK RVQENGEWTL FSPSEAPGLA
DVYGDEFEAL YERYVQEGRG RKTIKAQKLW YAILEAQTET GTPFMIYKDS CNRKSNQKNL
GTIKSSNLCC EIVEYSSPEE TAVCNLASVA LPAFIETSED GKTQWYNFEK LHEISKVVTR
NLNRVIDRNY YPVETARRSN MRHRPIALGV QGLADTFMML RIPFDSQEAK ELNIHVFETM
YHAALEASHE LALEEGPYET FKGSPAAEGI LQFDMWGRTP TDLWDWETLR ADIIKDGIRN
SLLLAPMPTA STSQILGYNE CFEPYTSNMY SRRVLSGEFQ IVNPYLLRDL VDLGLWDEAM
KSHIISDNGS IQNLPNIPQE LKDLYKTVWE LSQKTIIDMA ADRSCYIDQS QSLNVHIRAP
TMGKLTSMHF YGWKKGLKTG MYYLRTQAAS AAIQFTIDKS VAEQAGNTVA DLSNLSRPKY
TPRKVNFTEG AAKKLDLTTD IREVSPAPSS AESSMSNSIA SLRIDDSKPV VPATIAPTET
QTEEKPALTD EQEYDIYNSK VVACAINNPE ACEMCSG
//
