RIR1_MYCGE
ID RIR1_MYCGE Reviewed; 721 AA.
AC P47473;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdE; OrderedLocusNames=MG231;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
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; L43967; AAC71452.1; -; Genomic_DNA.
DR PIR; E64225; E64225.
DR RefSeq; WP_009885768.1; NZ_AAGX01000005.1.
DR AlphaFoldDB; P47473; -.
DR SMR; P47473; -.
DR STRING; 243273.MG_231; -.
DR EnsemblBacteria; AAC71452; AAC71452; MG_231.
DR KEGG; mge:MG_231; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_14; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 357568at2; -.
DR BioCyc; MGEN243273:G1GJ2-278-MON; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000807; 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; IPR013346; NrdE_NrdA.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR TIGRFAMs; TIGR04170; RNR_1b_NrdE; 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..721
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187217"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 386
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175..176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384..388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 589..593
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 213
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 413
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 694
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 695
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 716
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 719
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 176..413
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 721 AA; 82249 MW; 75E0174979CCAA59 CRC64;
MTSKEKIPTF NTEEDVESYI SFNAQAKIYD DFAIDLQAVE SYIQEHVKPK TKVFHSTKER
LDFLIKNDYY DEKIINMYSF EQFEEITHKA YSYRFRYANF MGAFKFYNAY ALKTFDGKYY
LENYEDRVVM NVLMLANGNF NKALKLLKQI ILNRFQPATP TFLNAGRKKR GEFVSCYLLR
IEDNMESIGR AITTTLQLSK RDGGVALLLS NLREAGAPIK KIENQSSGII PIMKLLEDSF
SYSNQLGQRQ GAGAVYLHCH HPDVMQFLDT KRENADEKIR IKSLSLGLVI PDITFQLAKN
NEMMALFSPY DIYQEYGKAL SDISVTEMYY ELLENQRIKK TFISARKFFQ TIAELHFESG
YPYILFDDTV NRRNAHKNRI VMSNLCSEIV QPSLPSEFYS DLTFKKVGSD ISCNLGSLNI
ARAMESGSEL AELIQLAIES LDLVSRISSL ETAPSIKKGN SENHALGLGA MNLHGFLATN
AIYYDSKEAV DFTNIFFYTV AYHAFSASNK LALELGKFKD FENTKFADGS YFDKYTKVAS
DFWTCKTEKV QALFDKYQVK IPTQENWKQL VASIQKDGLA NSHLMAIAPT GSISYLSSCT
PSLQPVVSPV EVRKEGKLGR IYVPAYKLDN DNYQYFKDGA YELGFEPIIN IVAAAQQHVD
QAISLTLFMT DKATTRDLNK AYIYAFKKGC SSIYYVRVRQ DVLKDSEDHT IKIKDCEVCS
I
