ID F3KYF5_9GAMM Unreviewed; 922 AA.
AC F3KYF5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=IMCC3088_1550 {ECO:0000313|EMBL:EGG30890.1};
OS Aequoribacter fuscus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Aequoribacter.
OX NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG30890.1, ECO:0000313|Proteomes:UP000005615};
RN [1] {ECO:0000313|EMBL:EGG30890.1, ECO:0000313|Proteomes:UP000005615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG30890.1,
RC ECO:0000313|Proteomes:UP000005615};
RX PubMed=21551310; DOI=10.1128/JB.05111-11;
RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT bacterium belonging to the OM60/NOR5 clade.";
RL J. Bacteriol. 193:3415-3416(2011).
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:EGG30890.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEIG01000003; EGG30890.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KYF5; -.
DR STRING; 2518989.IMCC3088_1550; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005615; 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; 2.
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; 2.
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:UP000005615}.
FT DOMAIN 1..99
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 116..205
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 922 AA; 102838 MW; 571771A76F0ADA07 CRC64;
MIKRNGQVVP FDNSKISVAI TKAFLAVEGG TAAASSRIHE TVAKLTTQVM GTFERRMPSG
GTIHIEDIQD QVELALMRAG EHKIARDYVI YREEQARKRA QKRALSAEAE RAAGAISVLQ
PDGSRAPLDI ERLQTVVSEA CADLADVSAS KILEEALRNL YDGVTLDEVT TSLVITARTL
IEQEPNYTYA AARLLCDDLR SEALEFLGVT QRATQQEMAL YYPQALQAYI AKGIQLELLS
PELADFDIAR LGAAIQPERD LQFTYLGLQT LYDRYFIHSN ETRFELPQVF FMRIAMGLAV
REDDKNARAI EFYQLLSSFD YMSSTPTLFN AGTLRPQLSS CYLTTVPDDL SGIYGAIRDN
ALLSKWAGGL GNDWTPVRAL GSYIKGTNGK SQGVVPFLKV VNDTAVAVNQ GGKRKGAVCA
YLETWHLDIE EFLELRKNTG DDRRRTHDMN SANWIPDLFM KRVFEGGEWT LFSPNDTPDL
HDSYGADFEA KYEAYEAQTR SGELKLFKRV KAENLWRKML GMLFETGHPW ITFKDPCNLR
SPQSHVGVVH SSNLCTEITL NTSDEEIAVC NLGSVNLPQH IDENGLNLEK LQKTVTTAVR
MLDNVIDINY YSVPQAERSN FRHRPVGLGL MGFQDALYKQ HIAYSSPEAV EFADRSMEAI
SYYAIQASSA LAEERGTYSS FEGSLWSQGI LPIDSLERLA ESRGDQYLQI DRTQTLDWDT
LRERVRAKGM RNSNVMAIAP TATIANITGV SQSIEPTYQN LYVKSNLSGE FTVVNPYLVN
DLKARNLWDK VMVNDLKYYD GSAQAIDRIP ADLKAIYSTA FEVEPRWIVE AASRRQKWID
QAQSLNLYIN NASGKKLDVT YRMAWLSGLK TTYYLRSLAA TGTEKSTVDK GTLNAVAAAA
APQPAPVPKA CSLDDPDCEA CQ
//
