ID A0A1H3WGF4_9GAMM Unreviewed; 1274 AA.
AC A0A1H3WGF4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05660964_00439 {ECO:0000313|EMBL:SDZ86229.1};
OS Thiothrix caldifontis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=525918 {ECO:0000313|EMBL:SDZ86229.1, ECO:0000313|Proteomes:UP000199397};
RN [1] {ECO:0000313|EMBL:SDZ86229.1, ECO:0000313|Proteomes:UP000199397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21228 {ECO:0000313|EMBL:SDZ86229.1,
RC ECO:0000313|Proteomes:UP000199397};
RA de Groot N.N.;
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; FNQP01000002; SDZ86229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3WGF4; -.
DR STRING; 525918.SAMN05660964_00439; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000199397; 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006141; Intein_N.
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; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
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; PS50817; INTEIN_N_TER; 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}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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 Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000199397}.
FT DOMAIN 29..129
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 146..236
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 1274 AA; 141827 MW; 26C406C0D5AF435A CRC64;
MPAASTQDFQ PVAPSSVTLP VSNANPFACK VIRRNGQVTD FDGSKIQIAM AKAFLDVEGS
QASGSARIHD TVRKLTEQVI EALLRRTPDG GMVHIEDIQD QVELALMRAG EHKVARSYVL
YRAERARLRA EKESKSKKKG KKSENVIHVK SATGDLKPLD EDRLRKIIAE AVDGLEGVSA
EQVMTATMRN LYDGISEKEV ATALIISTRV MIDREPNYSQ AAARMLMDSL RREALSFLEG
QHTEATQHEM VELYAEVLKK TIQIGVKVER LADDLGRYDL AKLGAAIKPE RDLQFTYLGL
QTLYDRYFLH HDGVRFELPQ VFFMRVAMGL AINEVEREDR AIEFYNLLSS FDFMSSTPTL
FNSGTLRPQL SSCYLTTVPD HLEGIYDAIK DNALLSKYAG GLGNDWSRVR GMGAHIKGTN
GKSQGVVPFL KVANDTAVAV NQCFAPDTQL HTADGIKAIR DVKAGDLVLG ISGTYREVKR
AMVYNQHDAM VALDVKHSIE PVKVTAGHPF YALRGVPLEQ ANDRTVNWLA KGKVKPEWVE
AAQLQKGDYV AQVIPTETVM VDGFSVDDAR LYGILLGSQS SDAEIQRLCE RKVVREATTG
CVVNDGAGFT FVYDDFYNAQ GEKRIARRFS HLSQPQTLAL LHGLLENNVV VKQDEDICFS
TVTRALAEGM RYQCLRLGIP TSGQIRDSAF DIRIPAVPEI AALVDCQPID KRNWLTYNGC
VFSRVRGVES IPTLPFVFDL IVEGDESYMT TAALAHNGGK RKGAVCAYLE TWHIDIEDFL
ELRKNTGDER RRTHDMNTAN WIPDLFMKRV AAEAEWTLFS PDDAPDLHDL TGKAFEARYA
EYEAKAARGD MKLFRKVPAV QLWRKMLGMI FETGHPWITF KDPCNVRYTN QHMGVVHSSN
LCTEITLHTN DSEIAVCNLG SVNLTAHVND GKLDVAKLER TVTTAMRMLD NVIDYNYYSV
PQARKSNLRH RPVGMGIMGF QDALYKMNLA YATTEAVEFA DQSMEAVSYF AIRASSNLAA
ERGKYPSYNG SLWSKGILPI DSLELLGEER GEYFIVDHTQ TLDWDALRNQ VKAQGMRNSN
VMAIAPTATI SNICGVSQSI EPTYQNLFVK SNLSGEFTVI NPYLVQDLKA LGMWDEVMIN
DLKYFDGSLQ PLDRVPDALK AKYATAFEID ARWLVEAASR RQKWIDQGQS LNLYMKEPNG
TKLDNLYKLA WVRGLKTTYY LRTLGATGAE KTSSDDSSAA NSVAGIKRAA NLVSVGSEAP
KACSLLDPEC EACQ
//
