RIR1_BUCBP
ID RIR1_BUCBP Reviewed; 761 AA.
AC Q89AS4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=bbp_168;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 to separate specificity
CC and activation sites on the alpha subunit. The type of nucleotide bound
CC 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. Stimulated by ATP and
CC inhibited by dATP binding to the activity site (By similarity).
CC {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; AE016826; AAO26901.1; -; Genomic_DNA.
DR RefSeq; WP_011091302.1; NC_004545.1.
DR AlphaFoldDB; Q89AS4; -.
DR SMR; Q89AS4; -.
DR STRING; 224915.bbp_168; -.
DR EnsemblBacteria; AAO26901; AAO26901; bbp_168.
DR GeneID; 56470711; -.
DR KEGG; bab:bbp_168; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 357568at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
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..761
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187208"
FT DOMAIN 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 15..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 209
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 232..234
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 262
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 269
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 437
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 441
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT BINDING 623..625
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P00452"
FT SITE 225
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 462
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 730
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 731
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 754
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 759
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 225..462
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 761 AA; 87124 MW; 7FB14E136283BDCF CRC64;
MNQMLFVTKR NGKIELINLD KIHRVLNWAA KGLENISISQ VALKSRIQFY NNIKTTIIHE
TIIKAAADLI SENSPDYQYM AARLTIFHLR KKAFGQFNPP NLYDHVKNMI KLEKYDQHLL
NDYPKQDFLI MNSFIKHRRD MNFSYAAVKQ LEGKYLIQNR VTKKIYESAQ FLYILISACL
FSKYPNETRM KYIKNFYDAI STFKISLPTP IMAGLRTPTR QFSSCVLIES EDNLNSINAT
TSAIVKYVSQ RAGIGINAGR IRALGSPIRN GDTLHTGCIP FYKHFQSAVK SCSQGGVRGG
AATIFYPIWH FEIESLLVLK NNRGIEENRV RHMDYSVQLN KLMYQRLILG EHITLFSPSD
VPNLYDSFFN NQEKFERLYI KYENDKTIRK KKVKASYLFS LMMQERTSTG RIYIQNVDHC
NSHSAFNPKI APIRQSNLCL EITLPTKALQ DVHDKNGEIS LCTLSAINLG SLNNLNDLSK
LSNLIVRALD SVLDYQEYPI LSAKKSALSR RTLGIGVINF AYYLAKNGVR YSDGSANNLT
HRTFEAIQYH LLNASCVLAQ EKGACHWFSH TNYYKGILPI DTYKKNVDEI CNEPLHLDWE
LLRKKIKKYG LRNSTLSALM PSETSSQISN ATNGIEPPRG LISIKASKDG MLRQVVPEYK
RLKNNYELLW NIPNNTGYLQ LASIMQKFVD QSISANTNYD PKLFPNNKIP MQQLILDLLT
AYKLGLKTLY YQNTRDGASD HQTEDIQFSK NENCNHGACK I
