RIR1A_MYCS2
ID RIR1A_MYCS2 Reviewed; 722 AA.
AC P0CG99; A0QR81; I7F7C8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha 1;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase R1 subunit 1;
GN Name=nrdE1; OrderedLocusNames=MSMEG_1019, MSMEI_0990;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PUPYLATION AT LYS-310, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
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 -!- MISCELLANEOUS: Pupylation of this protein has been demonstrated,
CC although it is unknown if the protein concerned is the product of this
CC gene, of the identical gene MSMEG_2299 (AC P0CH00), or of both genes.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK71849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK71849.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP37470.1; -; Genomic_DNA.
DR RefSeq; WP_014876938.1; NZ_SIJM01000057.1.
DR RefSeq; YP_885419.1; NC_008596.1.
DR RefSeq; YP_886648.1; NC_008596.1.
DR AlphaFoldDB; P0CG99; -.
DR SMR; P0CG99; -.
DR STRING; 246196.MSMEI_0990; -.
DR PRIDE; P0CG99; -.
DR EnsemblBacteria; ABK71849; ABK71849; MSMEG_1019.
DR EnsemblBacteria; AFP37470; AFP37470; MSMEI_0990.
DR KEGG; msg:MSMEI_0990; -.
DR KEGG; msm:MSMEG_1019; -.
DR PATRIC; fig|246196.56.peg.1016; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Isopeptide bond; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..722
FT /note="Ribonucleoside-diphosphate reductase subunit alpha
FT 1"
FT /id="PRO_0000396103"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394..398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 596..600
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 423
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 700
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 701
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 717
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 720
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 186..423
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 310
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
SQ SEQUENCE 722 AA; 82106 MW; 9D24EFB724737F9A CRC64;
MPPTVTAAEP VTTTGHVLPG EADYHALNAM LNLYDADGKI QFEKDREAAK QYFLQHVNQN
TVFFHSQDEK LDYLIENEYY EREVLDQYSR DFIKSLLDRA YAKKFRFPTF LGAFKYYTSY
TLKTFDGKRY LERFEDRVVM VALTLAAGDT ELAEKLVDEI IDGRFQPATP TFLNSGKKQR
GEPVSCFLLR IEDNMESIGR SINSALQLSK RGGGVALLLS NIREHGAPIK NIENQSSGVI
PIMKLLEDSF SYANQLGARQ GAGAVYLHAH HPDIYRFLDT KRENADEKIR IKTLSLGVVI
PDITFELAKK NEDMYLFSPY DVERVYGVPF ADVSVTEKYY EMVDDARIRK TKINAREFFQ
TLAELQFESG YPYIMFEDTV NRSNPIAGKI THSNLCSEIL QVSTPSEFND DLSYAKVGKD
ISCNLGSLNI AKAMDSPDFA QTIEVAIRAL TAVSDQTHIT SVPSIEQGNN DSHAIGLGQM
NLHGYLARER IYYGSEEGID FTNIYFYTVL FHALRASNKI AIERGTHFKG FEKSKYASGE
FFDKYTDQVW EPKTDKVRRL FADADIHIPT QDDWKQLKES VQKHGIYNQN LQAVPPTGSI
SYINHSTSSI HPVASKIEIR KEGKIGRVYY PAPYMTNDNL DYYQDAYEIG YEKIIDTYAA
ATQHVDQGLS LTLFFKDTAT TRDVNKAQIY AWRKGIKTLY YIRLRQMALE GTEVEGCVSC
ML
