ID A0A0N0UY60_9BACT Unreviewed; 790 AA.
AC A0A0N0UY60;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AD998_05290 {ECO:0000313|EMBL:KOY85641.1};
OS bacterium 336/3.
OC Bacteria.
OX NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY85641.1, ECO:0000313|Proteomes:UP000037950};
RN [1] {ECO:0000313|EMBL:KOY85641.1, ECO:0000313|Proteomes:UP000037950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:KOY85641.1,
RC ECO:0000313|Proteomes:UP000037950};
RA Isojarvi J., Battchikova N., Aro E.-M.;
RT "Draft genome sequence of symbiotic bacteroides-like organism.";
RL Submitted (JUL-2015) 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:KOY85641.1}.
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DR EMBL; LJIE01000001; KOY85641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0UY60; -.
DR STRING; 1664068.AD998_05290; -.
DR PATRIC; fig|1664068.3.peg.1072; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000037950; 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:UP000037950}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 790 AA; 89502 MW; 039E190ABF64DBF6 CRC64;
MLVQKRDGRL ESVKFDKITA RIEKLCYGLN MKYVEPVEIA KRVINGIYDK IPTTVLDELA
AQMAASLTTV HPDYAILAAR IAISNLHKET SKSFSNTMKR LYEYIDPKTG ENAGLIAKDV
YEVIRKNAAL LDSSIIYDRD YQYDYFGFKT LERSYLLRTD GKVAERPQHM LMRVAVGIHK
DDIDAAIETY NLLSEKWFTH ATPTLFNAGT PKPQLSSCFL LTMKGDSIDG IYDTLKQCAK
ISQSAGGIGL AIHNIRATGS YIKGTNGYSN GIIPMLKVFN DTARYIDQGG GKRKGAFAIY
IEPWHADVMD FLQLRKNHGA EELRARDLFY ALWISDLFMK RVEANETWSL FCPNEAPGLS
DCYGDEFERL YEKYESEGKA RKVVKAQDLW FEILESQIET GNPYILFKDA ANKKSNQKNL
GTIKSSNLCT EIMEYTAPDE VAVCNLASLA LPKYINNGKF DHQRLYEVTK VITKNLNKII
DINYYPVPEA ERSNKRHRPI GIGVQGLADV FIMLRMPFDS DEARGLNKDI FETIYYASLE
ASMEIAKEKG YYETYPGSPI SQGIFQFDMW GVKPSSGRWD WEALRAKILE NGVRNSLLLA
PMPTASTSQI LGNNECFEPY TSNMYTRRVL SGEFVVVNKH LLNDLIELGL WNENMKNKLQ
AAEGSVQNIK EIPENIKEIY KTAWELKQKS ILEMAADRGA FICQSQSLNV FVTEPNFGKL
TSMHFYAWKL GLKTGMYYLR TQAASSAIKF TVDTNVLQEQ NTQELVSVEQ KQKDMMCSLD
DPDSCEACGS
//
