GLRX1_ECOLI
ID GLRX1_ECOLI Reviewed; 85 AA.
AC P68688; P00277;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutaredoxin 1;
DE Short=Grx1;
GN Name=grxA; Synonyms=grx; OrderedLocusNames=b0849, JW0833;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=6352262; DOI=10.1111/j.1432-1033.1983.tb07730.x;
RA Hoeoeg J.-O., Joernvall H., Holmgren A., Carlquist M., Persson M.;
RT "The primary structure of Escherichia coli glutaredoxin. Distant homology
RT with thioredoxins in a superfamily of small proteins with a redox-active
RT cystine disulfide/cysteine dithiol.";
RL Eur. J. Biochem. 136:223-232(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3530878; DOI=10.1016/0378-1119(86)90003-x;
RA Hoeoeg J.-O., von Bahr-Lindstroem H., Joernvall H., Holmgren A.;
RT "Cloning and expression of the glutaredoxin (grx) gene of Escherichia
RT coli.";
RL Gene 43:13-21(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chatterjee P.K., Sternberg N.L.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP AMPYLATION AT TYR-13, AND MUTAGENESIS OF GLY-10; CYS-11; PRO-12; TYR-13;
RP CYS-14; VAL-15 AND ARG-16.
RX PubMed=30270044; DOI=10.1016/j.cell.2018.08.046;
RA Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S.,
RA Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M.,
RA Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R.,
RA Tagliabracci V.S.;
RT "Protein AMPylation by an Evolutionarily Conserved Pseudokinase.";
RL Cell 175:809-821(2018).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1889405; DOI=10.1111/j.1432-1033.1991.tb16194.x;
RA Sodano P., Chary K.V.R., Bjoernberg O., Holmgren A., Kren B., Fuchs J.A.,
RA Wuethrich K.;
RT "Nuclear magnetic resonance studies of recombinant Escherichia coli
RT glutaredoxin. Sequence-specific assignments and secondary structure
RT determination of the oxidized form.";
RL Eur. J. Biochem. 200:369-377(1991).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=1942053; DOI=10.1016/0022-2836(91)90935-y;
RA Sodano P., Xia T.-H., Bushweller J.H., Bjoernberg O., Holmgren A.,
RA Billeter M., Wuethrich K.;
RT "Sequence-specific 1H NMR assignments and determination of the three-
RT dimensional structure of reduced Escherichia coli glutaredoxin.";
RL J. Mol. Biol. 221:1311-1324(1991).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=1304339; DOI=10.1002/pro.5560010302;
RA Xia T.-H., Bushweller J.H., Sodano P., Billeter M., Bjoernberg O.,
RA Holmgren A., Wuethrich K.;
RT "NMR structure of oxidized Escherichia coli glutaredoxin: comparison with
RT reduced E. coli glutaredoxin and functionally related proteins.";
RL Protein Sci. 1:310-321(1992).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=9125525; DOI=10.1021/bi962181g;
RA Kelley J.J. III, Caputo M., Eaton S.F., Laue T.M., Bushweller J.H.;
RT "Comparison of backbone dynamics of reduced and oxidized Escherichia coli
RT glutaredoxin-1 using 15N NMR relaxation measurements.";
RL Biochemistry 36:5029-5044(1997).
CC -!- FUNCTION: The disulfide bond functions as an electron carrier in the
CC glutathione-dependent synthesis of deoxyribonucleotides by the enzyme
CC ribonucleotide reductase. In addition, it is also involved in reducing
CC some disulfide bonds in a coupled system with glutathione reductase.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; M13449; AAA23936.1; -; Genomic_DNA.
DR EMBL; U18655; AAC43449.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73936.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35552.1; -; Genomic_DNA.
DR PIR; A00283; GDEC.
DR RefSeq; NP_415370.1; NC_000913.3.
DR RefSeq; WP_001195240.1; NZ_STEB01000019.1.
DR PDB; 1EGO; NMR; -; A=1-85.
DR PDB; 1EGR; NMR; -; A=1-85.
DR PDB; 1GRX; NMR; -; A=1-85.
DR PDB; 1QFN; NMR; -; A=1-85.
DR PDBsum; 1EGO; -.
DR PDBsum; 1EGR; -.
DR PDBsum; 1GRX; -.
DR PDBsum; 1QFN; -.
DR AlphaFoldDB; P68688; -.
DR BMRB; P68688; -.
DR SMR; P68688; -.
DR BioGRID; 4259990; 8.
DR BioGRID; 849853; 5.
DR IntAct; P68688; 16.
DR STRING; 511145.b0849; -.
DR jPOST; P68688; -.
DR PaxDb; P68688; -.
DR PRIDE; P68688; -.
DR EnsemblBacteria; AAC73936; AAC73936; b0849.
DR EnsemblBacteria; BAA35552; BAA35552; BAA35552.
DR GeneID; 66670877; -.
DR GeneID; 945479; -.
DR KEGG; ecj:JW0833; -.
DR KEGG; eco:b0849; -.
DR PATRIC; fig|1411691.4.peg.1429; -.
DR EchoBASE; EB0412; -.
DR eggNOG; COG0695; Bacteria.
DR InParanoid; P68688; -.
DR OMA; VGGCTEF; -.
DR PhylomeDB; P68688; -.
DR BioCyc; EcoCyc:RED-GLUTAREDOXIN; -.
DR BioCyc; MetaCyc:RED-GLUTAREDOXIN; -.
DR SABIO-RK; P68688; -.
DR EvolutionaryTrace; P68688; -.
DR PRO; PR:P68688; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IDA:EcoCyc.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:EcoCyc.
DR GO; GO:0019345; P:cysteine biosynthetic process via S-sulfo-L-cysteine; IMP:EcoCyc.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IMP:EcoCyc.
DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IDA:EcoCyc.
DR DisProt; DP01740; -.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR011902; GRXA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02183; GRXA; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deoxyribonucleotide synthesis; Direct protein sequencing;
KW Disulfide bond; Electron transport; Nucleotide-binding; Phosphoprotein;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..85
FT /note="Glutaredoxin 1"
FT /id="PRO_0000141581"
FT DOMAIN 1..85
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOD_RES 13
FT /note="O-AMP-tyrosine; by YdiU"
FT /evidence="ECO:0000269|PubMed:30270044"
FT DISULFID 11..14
FT /note="Redox-active"
FT MUTAGEN 10
FT /note="G->A: No defect in AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 11
FT /note="C->A: Abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 12
FT /note="P->A: Abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 13
FT /note="Y->F,S,T: Abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 14
FT /note="C->A: Partially abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 15
FT /note="V->A: Partially abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 16
FT /note="R->A: Partially abolishes AMPylation by YdiU."
FT /evidence="ECO:0000269|PubMed:30270044"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1EGO"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:1EGO"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1EGO"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1EGO"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1EGO"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1EGO"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1EGO"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:1EGO"
SQ SEQUENCE 85 AA; 9685 MW; 33C185A47021EF42 CRC64;
MQTVIFGRSG CPYCVRAKDL AEKLSNERDD FQYQYVDIRA EGITKEDLQQ KAGKPVETVP
QIFVDQQHIG GYTDFAAWVK ENLDA
