ID A0A416G4Q3_9BACE Unreviewed; 839 AA.
AC A0A416G4Q3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
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=DXA74_15690 {ECO:0000313|EMBL:RHP59075.1};
OS Bacteroides sp. OF04-15BH.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292281 {ECO:0000313|EMBL:RHP59075.1, ECO:0000313|Proteomes:UP000284249};
RN [1] {ECO:0000313|EMBL:RHP59075.1, ECO:0000313|Proteomes:UP000284249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OF04-15BH {ECO:0000313|EMBL:RHP59075.1,
RC ECO:0000313|Proteomes:UP000284249};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHP59075.1}.
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DR EMBL; QUEM01000073; RHP59075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416G4Q3; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000284249; 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:UP000284249}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 839 AA; 95805 MW; 4077BA5DDDA16AE4 CRC64;
MQVTKRNGTT EPYNREKIAV AIRKSFASTG REAADDTIQK MVHEVESFVR DDATGRSVER
IQDEVERCLM EHGFYAEAKN YILYRWQRTE CRKTLSYIAA ETARPQIMDV LKGIQADFAS
NEYSLTLLAE RFSGFCKPEM SADERMAALI KTAVELTTQE APDWEFIAAR LLDFVLSEKL
ERQARLAGVH SLYEKLRYLT DEGLYGSYIL DSYSRQEIEE AAAFMRPERD KLLNYSGLDL
LYKRYLIRTH SHEPMESVQE MYLGIALHLA MPEKNGRLQW VRKFYEMLSR LEVTMATPTL
SNARKPYHQL SSCFIDTVPD SLEGIYRSID NFAMVSKFGG GMGMYFGKVR AAGGNIRGFK
GVAGGVIRWM KLVNDTAVAV DQLGMRQGAA AVYLDVWHKD LPEFLQLRTN NGDDRMKAHD
IFPAVCYPDL FWRLAKENLD RQWFLFCPNE IMTVKGYCLE DYYGEEWEKR YWDCVNDARL
SRRTISIKDV VRLVLRSAVE TGTPFTFNRD IVNRANPNSH KGMIYCSNLC TEIAQNMSPI
ESVSSEIRTE GGDTVVVTTV KPGDFVVCNL ASLSLGHLPL EDDALMKEKV ATVVRALDNV
IDLNFYSIPY AKITNRRYRS IGLGVSGYHH ALAIRGIRWE SEEHLSFMDE VFERLNYAAI
EASAKLAKEK GRYECFAGSG WQTGDYFTKR GYTSLKWQTL AEKVAHDGMR NAYLLAIAPT
SSTSIIAGTT AGTDPVMKRF FLEEKKGAML PRVAPALSDR TFWKYKSAYL IDQTWSIRAA
GIRQRHIDQS QSLNIYITND FTMRQLLNLY LMAWECGVKT LYYVRSKSLE VEECENCAS
//
