ID E8LYU8_9VIBR Unreviewed; 760 AA.
AC E8LYU8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=VIBR0546_06632 {ECO:0000313|EMBL:EGA64149.1};
OS Vibrio brasiliensis LMG 20546.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA64149.1, ECO:0000313|Proteomes:UP000004371};
RN [1] {ECO:0000313|EMBL:EGA64149.1, ECO:0000313|Proteomes:UP000004371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA64149.1,
RC ECO:0000313|Proteomes:UP000004371};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGA64149.1}.
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DR EMBL; AEVS01000094; EGA64149.1; -; Genomic_DNA.
DR RefSeq; WP_006881020.1; NZ_AEVS01000094.1.
DR AlphaFoldDB; E8LYU8; -.
DR STRING; 945543.VIBR0546_06632; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004371; 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 Gene3D; 1.10.1650.20; -; 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}.
FT DOMAIN 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 737..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 85684 MW; 9358F77029FF90F5 CRC64;
MNQQLTVTKR NGRKESIDLE KIHRVITWAA EGLDNVSVSQ VELRAHIQFY DGITTTDIHE
TIIKSAADLI SEETPDYQYL AARLAVFHLR KKAYGQYEPP ALYDHVARLV DMGKYDQHIL
EDYTKAELDE LDEYLDHKRD LDFSYAAVKQ LEGKYFVQNR VSGEIYESAQ FLYILVAACL
FAKYPKETRL DYIKRFYDAT SKFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT
ASSIVRYVSQ RAGIGINAGR IRALGSEIRG GEAFHTGCIP FYKYFQTAVK CCSQGGVRGG
AATVFYPLWH GESQALMVLK NNRGVEENRV RHMDYGVQLN RLMYQRLVEG GNITLFSPSD
VPGLYDAFFE NQDEFERLYV KYENDPSIKK ETVKAIEMFS ILMQERASTG RIYIQNVDHC
NTHSPFDSEV APVRQSNLCL EIALPTKPLT NVEDDSGEIA LCTLSAFNLG SIKSLDDFEE
LSNLVVRALD ALLDYQDYPL PAAYKSTMNR RTLGVGVINY AYYLAKNGVK YSDGSANGLT
HRTFEAIQYY LLKASVELAK EQGKCPLFDE TNYAKGLMPI DTYKKDVDLI CDEPLHYDWD
GLRQEIMTHG LRNSTLTALM PSETSSQISN ATNGIEPPRG YVSVKASKDG ILKQVVPEFT
EYKDNYELLW NIGSNDGYLH LVGIMQKFVD QAISANTNYD PTRFESGKVP MKKLLQDLLT
AYKFGVKTLY YHNTRDGASD DQKDAVQPQD DDCAGGGCKI
//
