RIR1_MYCPN
ID RIR1_MYCPN Reviewed; 721 AA.
AC P78027;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdE; OrderedLocusNames=MPN_324; ORFNames=MP512;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00089; AAB96160.1; -; Genomic_DNA.
DR PIR; S73838; S73838.
DR RefSeq; NP_110012.1; NC_000912.1.
DR RefSeq; WP_010874680.1; NC_000912.1.
DR AlphaFoldDB; P78027; -.
DR SMR; P78027; -.
DR IntAct; P78027; 7.
DR STRING; 272634.MPN_324; -.
DR PRIDE; P78027; -.
DR EnsemblBacteria; AAB96160; AAB96160; MPN_324.
DR KEGG; mpn:MPN_324; -.
DR PATRIC; fig|272634.6.peg.348; -.
DR HOGENOM; CLU_000404_4_1_14; -.
DR OMA; RGSIQNI; -.
DR BioCyc; MPNE272634:G1GJ3-515-MON; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000808; 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; 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_0000187218"
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; 82375 MW; 93CAEA95A2A9E647 CRC64;
MSVKEKIPAF NTQEDLESYI SLNAYTKVYG DFKMDLHAVE AYIQEHVKPK TKVFHSTKER
LDFLVKNDYY DENIINMYSF EQFEEITRKA YAYRFRYANF MGAFKFYNAY ALKTFDGKWY
LENYEDRVVM NVLFLANGNY NKALKLLKQI ITNRFQPATP TFLNAGRKKR GEFVSCYLLR
IEDNMESIGR AITTTLQLSK RDGGVALLLT NIRESGAPIK KIENQSSGII PIMKLLEDSF
SYANQLGQRQ GAGAVYLHAH HPDVMQFLDT KRENADEKIR IKSLSLGLVI PDITFTLAKN
NEEMALFSPY DVYEEYGKPL SDISVTEMYY ELLANQRIKK TFINARKFFQ TVAELHFESG
YPYILFDDTV NRRNAHPNRI VMSNLCSEIV QPSTPSEFHH DLAFKKVGND ISCNLGSLNI
AKAMESGPEF SELVKLAIES LDLVSRVSNL ETAPSIQKGN SENHALGLGA MNLHGFLATN
QIYYNSPEAI DFTNIFFYTV AYHAFKASSE LALEKGKFKN FENTKFADGS YFDKYIKVEP
DFWTPKTERV KALFQKYQVE IPTRENWKEL ALNIQKNGLA NSHLLAIAPT GSISYLSSCT
PSLQPVVSPV EVRKEGRLGR IYVPAYQLNK DSYPFYKDGA YELGPEPIIN IAAAAQQHVD
QAISLTLFMT DKATTRDLNK AYIYAFKKGC SSIYYVRVRQ EVLEDSEDHT IQMQQCEACV
I
