ID A0A1I2BPU4_9FIRM Unreviewed; 842 AA.
AC A0A1I2BPU4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN02910327_01553 {ECO:0000313|EMBL:SFE58156.1};
OS Peptostreptococcaceae bacterium pGA-8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=1520829 {ECO:0000313|EMBL:SFE58156.1, ECO:0000313|Proteomes:UP000242361};
RN [1] {ECO:0000313|Proteomes:UP000242361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=pGA-8 {ECO:0000313|Proteomes:UP000242361};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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|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}.
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DR EMBL; FONK01000015; SFE58156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2BPU4; -.
DR STRING; 1520829.SAMN02910327_01553; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000242361; 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:UP000242361}.
FT DOMAIN 1..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 842 AA; 95664 MW; F68B427958BD742D CRC64;
MKIIKRSGEV TDFQVEKIKV AMEKAFVGVS QPIDDNKLQE MADRVSHKAE TKFPKDHIVT
VEEIQDLVEI ELIENNFYRV VKAYILYRAS HHTMRKTLED FSGYISDKEI IDEMKEIQIA
FPEEVYNLSF LYGKFSSFVK DNMSDDEHLA ILIKASAELT GKEAPKWEYI SARFLNLQVN
REINREMTKA DIFSFREKIH YLTAQGIYGK YMTENYSDDQ IDELEAYMDQ SRNLLFNYSG
LDLVAKRYLI RNFEGHIIES VQEMFMGISM HLAIPEGENR VQWAKKIYDI LSTLKVTMAT
PTMSNARKVY SQLSSCFIDT VPDSLDGIYR SITNFSQVSK HGGGMGLYFG KVRATGSDIR
GIKGVAGGVI RWIKLANDTA VAVDQLGVRQ GACAVYLDIW HKDVPEFLQL KTNNGDDRMK
AHDIFPAVCF PDYFWKLAKE DINANWYMMC PHEIKEVKGY CLEDFIGDEW VKRYLECAED
IRIDKRVMSV KDMVRLIIKS AVETGTPFIF NRDAVNRANP NGHKGMIYAS NLCTEIAQNM
RPIEAVSKEI ISVDGEEIIV EKTKSGDFVV CNLASLVLGN IDVSNKDELK GVISTVVRAL
DNVIDLNYYP LPYAKITNGK YRAIGLGTSG YHHLLAKNGI SFSSEEHLTF ADKVYEDINY
FAIEASKEIA KEKGSYSFFT GSDWQTGEYF AKRGYTDERW KALAGEVAEH GLRNGYLLAV
APTGSTSIIA GTTAAVDPIM NKYFLEEKKG QIVPRVAPDL SSKTYWLYQN AHQIDQSWVI
RASGIRQRHI DQSQSVNIYI TSEMTMSQIL RLYISACEEG VKTLYYVRSK SLEVDECESC
SA
//
