ID Q1QZS9_CHRSD Unreviewed; 976 AA.
AC Q1QZS9;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
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 OrderedLocusNames=Csal_0668 {ECO:0000313|EMBL:ABE58029.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58029.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE58029.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(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}.
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DR EMBL; CP000285; ABE58029.1; -; Genomic_DNA.
DR RefSeq; WP_011505975.1; NC_007963.1.
DR AlphaFoldDB; Q1QZS9; -.
DR STRING; 290398.Csal_0668; -.
DR KEGG; csa:Csal_0668; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000239; Chromosome.
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:UP000000239}.
FT DOMAIN 20..120
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 134..223
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 910..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 107949 MW; 6CB77BC2ECEBB14D CRC64;
MDTSISPGKA SVDITAPQRL RVIKRGGEVA AFDGSKISVA ITKAFIATEG DNAAASSRIR
EFVSEATQSI VDTFLRRMPD GGTLHIEDIQ DQVELALMRA GEQKVARAYV LYREEHARAR
QPQGADIAKP HPSLNVTQAD GTVRPLDLGR VETLVADACE GLANVEPQKI VDASLKNLYD
GVPIDGVATA LMMTARTLVE KEPNYTYATA RLLQDNLRRE ALSFLGIADE ATYQEMATLY
APAFKAYIDK GIEFEQLDER LREFDLDRLG AALDHTRDNQ FTYLGLQTLY DRYFLHHDDV
RYELPQVMFM RVAMGLALNE DDPEARAIEF YELLSSFDYM ASTPTLFNAG TQRSQLSSCY
LTTVPDQLDG IYSAIRDNAL LSKWAGGLGN DWTPVRALGS YIKGTNGKSQ GVVPFLKVVN
DTAVAVNQGG KRKGAVCAYL ETWHLDVEEF LELRKNTGDD RRRTHDMNTA NWVPDLFMKR
VFDDEEWTLF SPSTCPDLHD LYGAAFEKRY AEYEEMTRNG QLKLFKRVKA KDLWRKMLSM
LFETGHPWIT FKDPCNLRSP QNHAGVVHSS NLCTEITLNT SADEIAVCNL GSVNLAQHIV
DGQLDGDKLK KTVKTAVRML DNVIDINYYA VPQARNSNFK HRPVGLGLMG FQDALYQLGI
AYASDDAVTF ADTSMELISY HAIEASSDLA TERGRYQSFE GSLWSKGVLP IDSIAKLAEE
RGADYIEVDT STTQDWARLR DKVTRQGMRN SNVMAIAPTA TISNICGVTQ SIEPTYQNLF
VKSNLSGEFT VVNAYMVNDL KARGLWDEVM INDLKYYDGS VQPIDRIPDD LKARYASAFE
VEPKWLVEAA ARRQKWIDQA QSLNLYIAGV SGKKLDVTYR MAWFRGLKTT YYLRALGATS
VEKSTVDRGK LNAVGNTGGS ASPQPAAAPS PSPSPAASDA GGEARGIDDF LTGKSGSGSR
APSAGDIDEL GCEACQ
//
