RIR1_SYNY3
ID RIR1_SYNY3 Reviewed; 767 AA.
AC P74240;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=slr1164;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18334.1; -; Genomic_DNA.
DR PIR; S75875; S75875.
DR AlphaFoldDB; P74240; -.
DR SMR; P74240; -.
DR IntAct; P74240; 3.
DR STRING; 1148.1653420; -.
DR PaxDb; P74240; -.
DR EnsemblBacteria; BAA18334; BAA18334; BAA18334.
DR KEGG; syn:slr1164; -.
DR eggNOG; COG0209; Bacteria.
DR InParanoid; P74240; -.
DR OMA; RGSIQNI; -.
DR PhylomeDB; P74240; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 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; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..767
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187222"
FT DOMAIN 31..120
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 462
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 460..464
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 631..635
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 251
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 281
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 478
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 745
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 746
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 762
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 765
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 244..478
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 767 AA; 85637 MW; 147151C406A082C5 CRC64;
MHPTLISAPI SSSANDAHAG TSQGSHQGHR IQVIRRDGSS TPLNIGKIRA VVDWACLGLE
VNSIALEAGL TTRLREGIST REIQDNLISC ALEMCSPNEP DWRYVAGRLH VWSLWKDTLV
RRGYQYGQYL RTVQTKVTNG EYDSRILTYS EGELQEAGCW INSDWDTDYD YAGAVLLTSR
YLLPNELPQE ALLTCALLLA SVEAPDRRLQ WARRFYESIA ARRISLATPI LANLRVPGGS
LTSCFIVAME DNLESIFGEI TNAARISKNG GGVGVNVSRI RATGSWVMGK PNASGGVIPW
TKLLNDTAIA VNQGGRRAGA VTVGLDVWHL DVPEFLEMQA ENGDQRRKAY DIFPQLILPD
EFMRRVINKE DWTLVDPYEV REKMGIELAE LWGEQFEGAY REIESNLDTT ITLYKRINAR
ELFKQIMRTQ VETGMPYLSF KDTINKANPN KHLGYIPGTN LCCESFSNVT PGQDAHCCNL
VSLNLANLDL QDIAGVSQIA VRMLDNTIEL TAPPFADAKS HNNKYRTIGV GAMGLADWLA
KRRLNYDELA DINRLFEEIG YWCTQSSMEL AKERGAYPAF PGSDWQKGLL IGSKPVSWFQ
ANAAKPERWE KLSNDIQTHG IRNSHITAIA PNTSSSLVQG CTASILPVYS RFFYDKWAKG
TVPIAPPFIG NCFWFYPENK TMDQRKVVKA VAAIQQWTDT GISMELLFNL NAGIYFPEEP
ERSLNAKDIF DTLVMAWEAG CKAIYYIRTV QKDDFKDSSD GCVACAN
