SQUS_ECOLI
ID SQUS_ECOLI Reviewed; 413 AA.
AC P32140; Q2M8H7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sulfoquinovose isomerase {ECO:0000255|HAMAP-Rule:MF_00998};
DE Short=SQ isomerase {ECO:0000255|HAMAP-Rule:MF_00998};
DE EC=5.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00998};
GN Name=yihS; OrderedLocusNames=b3880, JW5569;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12;
RX PubMed=24463506; DOI=10.1038/nature12947;
RA Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D.,
RA Huhn T., Cook A.M., Schleheck D.;
RT "Sulphoglycolysis in Escherichia coli K-12 closes a gap in the
RT biogeochemical sulphur cycle.";
RL Nature 507:114-117(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION AS AN ISOMERASE, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES, AND
RP MUTAGENESIS OF ARG-55; HIS-176; HIS-248; GLU-251; GLU-320 AND HIS-383.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18328504; DOI=10.1016/j.jmb.2008.01.090;
RA Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Crystal structure of YihS in complex with D-mannose: structural annotation
RT of Escherichia coli and Salmonella enterica yihS-encoded proteins to an
RT aldose-ketose isomerase.";
RL J. Mol. Biol. 377:1443-1459(2008).
CC -!- FUNCTION: Catalyzes the isomerization of sulfoquinovose (SQ) to 6-
CC deoxy-6-sulfo-D-fructose (SF). In vitro, can also catalyze the
CC interconversion of mannose, fructose and glucose, or lyxose and
CC xylulose, but has extremely low activity with glucose.
CC {ECO:0000255|HAMAP-Rule:MF_00998, ECO:0000269|PubMed:18328504,
CC ECO:0000269|PubMed:24463506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-sulfo-beta-D-quinovose = 6-deoxy-6-sulfo-D-fructose;
CC Xref=Rhea:RHEA:40439, ChEBI:CHEBI:77133, ChEBI:CHEBI:142957;
CC EC=5.3.1.31; Evidence={ECO:0000255|HAMAP-Rule:MF_00998,
CC ECO:0000269|PubMed:24463506};
CC -!- ACTIVITY REGULATION: Significantly inhibited by Cu(2+), Fe(3+) and
CC Co(2+). Partially inhibited by Mg(2+), Ca(2+) and Mn(2+). Also
CC inhibited by ATP, ADP, dATP, TTP and GTP.
CC {ECO:0000269|PubMed:18328504}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=108 mM for D-mannose {ECO:0000269|PubMed:18328504};
CC KM=276 mM for D-fructose {ECO:0000269|PubMed:18328504};
CC KM=405 mM for D-lyxose {ECO:0000269|PubMed:18328504};
CC KM=163 mM for D-xylulose {ECO:0000269|PubMed:18328504};
CC Note=kcat is 25.3 sec(-1) for D-mannose. kcat is 22.2 sec(-1) for D-
CC fructose. kcat is 13.5 sec(-1) for D-lyxose. kcat is 10.3 sec(-1) for
CC D-xylulose.;
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:18328504};
CC Temperature dependence:
CC Optimum temperature is 47 degrees Celsius.
CC {ECO:0000269|PubMed:18328504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00998,
CC ECO:0000269|PubMed:18328504}.
CC -!- INDUCTION: Induced during growth with sulfoquinovose.
CC {ECO:0000269|PubMed:24463506}.
CC -!- DISRUPTION PHENOTYPE: Mutant fails to grow on sulfoquinovose as a sole
CC carbon source. {ECO:0000269|PubMed:24463506}.
CC -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00998}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03013.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L19201; AAB03013.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAD13442.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77429.1; -; Genomic_DNA.
DR PIR; S40824; S40824.
DR RefSeq; NP_418316.4; NC_000913.3.
DR RefSeq; WP_000870916.1; NZ_STEB01000017.1.
DR PDB; 2RGK; X-ray; 2.50 A; A/B/C/D/E/F=1-413.
DR PDBsum; 2RGK; -.
DR AlphaFoldDB; P32140; -.
DR SMR; P32140; -.
DR BioGRID; 4262638; 4.
DR STRING; 511145.b3880; -.
DR PaxDb; P32140; -.
DR PRIDE; P32140; -.
DR EnsemblBacteria; AAD13442; AAD13442; b3880.
DR EnsemblBacteria; BAE77429; BAE77429; BAE77429.
DR GeneID; 66672214; -.
DR GeneID; 948374; -.
DR KEGG; ecj:JW5569; -.
DR KEGG; eco:b3880; -.
DR PATRIC; fig|1411691.4.peg.2831; -.
DR EchoBASE; EB1791; -.
DR eggNOG; COG2942; Bacteria.
DR HOGENOM; CLU_042253_0_0_6; -.
DR InParanoid; P32140; -.
DR OMA; WVQAETF; -.
DR PhylomeDB; P32140; -.
DR BioCyc; EcoCyc:EG11845-MON; -.
DR BioCyc; MetaCyc:EG11845-MON; -.
DR EvolutionaryTrace; P32140; -.
DR PRO; PR:P32140; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0050089; F:mannose isomerase activity; IDA:EcoCyc.
DR GO; GO:0061593; F:sulfoquinovose isomerase activity; IDA:EcoCyc.
DR GO; GO:1902777; P:6-sulfoquinovose(1-) catabolic process; IMP:EcoCyc.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IMP:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR CDD; cd00249; AGE; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR HAMAP; MF_00998; SQ_isomerase; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR034116; AGE_dom.
DR InterPro; IPR030875; SQ_isomerase.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..413
FT /note="Sulfoquinovose isomerase"
FT /id="PRO_0000208954"
FT ACT_SITE 248
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:18328504"
FT ACT_SITE 383
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:18328504"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998"
FT MUTAGEN 55
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT MUTAGEN 176
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT MUTAGEN 248
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT MUTAGEN 251
FT /note="E->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT MUTAGEN 320
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT MUTAGEN 383
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18328504"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 228..233
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 246..265
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 336..351
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2RGK"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2RGK"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:2RGK"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:2RGK"
SQ SEQUENCE 413 AA; 47433 MW; 00BC3BCD31779BE6 CRC64;
MKWFNTLSHN RWLEQETDRI FDFGKNSVVP TGFGWLGNKG QIKEEMGTHL WITARMLHVY
SVAAAMGRPG AYSLVDHGIK AMNGALRDKK YGGWYACVND EGVVDASKQG YQHFFALLGA
ASAVTTGHPE ARKLLDYTIE IIEKYFWSEE EQMCLESWDE AFSKTEEYRG GNANMHAVEA
FLIVYDVTHD KKWLDRAIRV ASVIIHDVAR NNHYRVNEHF DTQWNPLPDY NKDNPAHRFR
AFGGTPGHWI EWGRLMLHIH AALEARCEQP PAWLLEDAKG LFNATVRDAW APDGADGIVY
TVDWEGKPVV RERVRWPIVE AMGTAYALYT VTGDRQYETW YQTWWEYCIK YLMDYENGSW
WQELDADNKV TTKVWDGKQD IYHLLHCLVI PRIPLAPGMA PAVAAGLLDI NAK
