GLPE_ECOLI
ID GLPE_ECOLI Reviewed; 108 AA.
AC P0A6V5; P09390; Q2M789; Q47235;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Thiosulfate sulfurtransferase GlpE;
DE EC=2.8.1.1 {ECO:0000269|PubMed:10735872};
GN Name=glpE; OrderedLocusNames=b3425, JW3388;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8955387; DOI=10.1128/jb.178.24.7080-7089.1996;
RA Zeng G., Ye S., Larson T.J.;
RT "Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-
RT 12: primary structure and identification of the DNA-binding domain.";
RL J. Bacteriol. 178:7080-7089(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3045764; DOI=10.1093/nar/16.15.7732;
RA Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M.,
RA Utsumi R., Kohara Y., Akiyama K.;
RT "Nucleotide sequence of the glpR gene encoding the repressor for the
RT glycerol-3-phosphate regulon of Escherichia coli K12.";
RL Nucleic Acids Res. 16:7732-7732(1988).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1846566; DOI=10.1016/0167-4781(91)90149-g;
RA Choi Y.-L., Kawase S., Kawamukai M., Sakai H., Komano T.;
RT "Regulation of glpD and glpE gene expression by a cyclic AMP-cAMP receptor
RT protein (cAMP-CRP) complex in Escherichia coli.";
RL Biochim. Biophys. Acta 1088:31-35(1991).
RN [6]
RP CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RC STRAIN=BL21-DE3;
RX PubMed=10735872; DOI=10.1128/jb.182.8.2277-2284.2000;
RA Ray W.K., Zeng G., Potters M.B., Mansuri A.M., Larson T.J.;
RT "Characterization of a 12-kilodalton rhodanese encoded by glpE of
RT Escherichia coli and its interaction with thioredoxin.";
RL J. Bacteriol. 182:2277-2284(2000).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19088907; DOI=10.2174/1874285800802010018;
RA Cheng H., Donahue J.L., Battle S.E., Ray W.K., Larson T.J.;
RT "Biochemical and genetic characterization of pspE and glpE, two single-
RT domain sulfurtransferases of Escherichia coli.";
RL Open Microbiol. J. 2:18-28(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
RC STRAIN=BL21-DE3;
RX PubMed=11092948; DOI=10.1107/s0907444900015304;
RA Bordo D., Larson T.J., Donahue J.L., Spallarossa A., Bolognesi M.;
RT "Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli,
RT display 1.06 A resolution diffraction: a preliminary report.";
RL Acta Crystallogr. D 56:1691-1693(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
RC STRAIN=BL21-DE3;
RX PubMed=11709175; DOI=10.1016/s0969-2126(01)00666-9;
RA Spallarossa A., Donahue J.L., Larson T.J., Bolognesi M., Bordo D.;
RT "Escherichia coli GlpE is a prototype sulfurtransferase for the single-
RT domain rhodanese homology superfamily.";
RL Structure 9:1117-1125(2001).
CC -!- FUNCTION: Catalyzes, although with low efficiency, the sulfur transfer
CC reaction from thiosulfate to cyanide. The relatively low affinity of
CC GlpE for both thiosulfate and cyanide suggests that these compounds are
CC not the physiological substrates. Thioredoxin 1 or related dithiol
CC proteins could instead be the physiological sulfur-acceptor substrate.
CC Possible association with the metabolism of glycerol-phosphate remains
CC to be elucidated.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC Evidence={ECO:0000269|PubMed:10735872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16882;
CC Evidence={ECO:0000305|PubMed:10735872};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By infection by filamentous bacteriophages. Expression is
CC positively regulated by cyclic AMP-cAMP receptor protein (cAMP-CRP).
CC {ECO:0000269|PubMed:1846566, ECO:0000269|PubMed:19088907}.
CC -!- MISCELLANEOUS: Incubation of GlpE with the cysteine-specific modifying
CC reagent DTNB resulted in a greater-than-90% loss of activity.
CC -!- SIMILARITY: Belongs to the GlpE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M96795; AAC28165.1; -; Genomic_DNA.
DR EMBL; X07520; CAA30397.1; -; Genomic_DNA.
DR EMBL; M54940; AAA23889.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA58223.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76450.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77867.1; -; Genomic_DNA.
DR PIR; D65138; BVECGE.
DR RefSeq; NP_417883.1; NC_000913.3.
DR RefSeq; WP_000371928.1; NZ_SSZK01000008.1.
DR PDB; 1GMX; X-ray; 1.10 A; A=1-108.
DR PDB; 1GN0; X-ray; 1.80 A; A=1-108.
DR PDBsum; 1GMX; -.
DR PDBsum; 1GN0; -.
DR AlphaFoldDB; P0A6V5; -.
DR SMR; P0A6V5; -.
DR BioGRID; 4262487; 11.
DR IntAct; P0A6V5; 2.
DR STRING; 511145.b3425; -.
DR jPOST; P0A6V5; -.
DR PaxDb; P0A6V5; -.
DR PRIDE; P0A6V5; -.
DR EnsemblBacteria; AAC76450; AAC76450; b3425.
DR EnsemblBacteria; BAE77867; BAE77867; BAE77867.
DR GeneID; 67417052; -.
DR GeneID; 947935; -.
DR KEGG; ecj:JW3388; -.
DR KEGG; eco:b3425; -.
DR PATRIC; fig|511145.12.peg.3520; -.
DR EchoBASE; EB0390; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_089574_14_0_6; -.
DR InParanoid; P0A6V5; -.
DR OMA; VCYHGIS; -.
DR PhylomeDB; P0A6V5; -.
DR BioCyc; EcoCyc:EG10395-MON; -.
DR BioCyc; MetaCyc:EG10395-MON; -.
DR EvolutionaryTrace; P0A6V5; -.
DR PRO; PR:P0A6V5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:EcoCyc.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006791; P:sulfur utilization; IMP:EcoCyc.
DR CDD; cd01444; GlpE_ST; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR HAMAP; MF_01009; Thiosulf_sulfurtr; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR023695; Thiosulf_sulfurTrfase.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..108
FT /note="Thiosulfate sulfurtransferase GlpE"
FT /id="PRO_0000200549"
FT DOMAIN 17..105
FT /note="Rhodanese"
FT ACT_SITE 65
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="A -> RNALYCPLLCGISDSNDVDDYLFC (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1GMX"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1GMX"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1GMX"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1GMX"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:1GMX"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1GMX"
SQ SEQUENCE 108 AA; 12082 MW; 18D5B461C2A8EF19 CRC64;
MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQA FHLTNDTLGA FMRDNDFDTP
VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF PAEVAYGA
