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Protein

Sulfoquinovose isomerase

Gene

yihS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy-6-sulfo-D-fructose (SF). In vitro, can also catalyze the interconversion of mannose, fructose and glucose, or lyxose and xylulose, but has extremely low activity with glucose.UniRule annotation2 Publications

Catalytic activityi

Sulfoquinovose = 6-deoxy-6-sulfo-D-fructose.UniRule annotation1 Publication

Enzyme regulationi

Significantly inhibited by Cu2+, Fe3+ and Co2+. Partially inhibited by Mg2+, Ca2+ and Mn2+. Also inhibited by ATP, ADP, dATP, TTP and GTP.1 Publication

Kineticsi

kcat is 25.3 sec(-1) for D-mannose. kcat is 22.2 sec(-1) for D-fructose. kcat is 13.5 sec(-1) for D-lyxose. kcat is 10.3 sec(-1) for D-xylulose.

  1. KM=108 mM for D-mannose1 Publication
  2. KM=276 mM for D-fructose1 Publication
  3. KM=405 mM for D-lyxose1 Publication
  4. KM=163 mM for D-xylulose1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Optimum temperature is 47 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551SubstrateUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation
    Binding sitei172 – 1721SubstrateUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Binding sitei238 – 2381Substrate; via carbonyl oxygenUniRule annotation
    Active sitei248 – 2481Proton donor/acceptor1 Publication
    Binding sitei251 – 2511SubstrateUniRule annotation
    Binding sitei316 – 3161SubstrateUniRule annotation
    Active sitei383 – 3831Proton donor/acceptor1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc
    • mannose isomerase activity Source: EcoCyc
    • sulfoquinovose isomerase activity Source: EcoCyc

    GO - Biological processi

    • 6-sulfoquinovose(1-) catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11845-MONOMER.
    ECOL316407:JW5569-MONOMER.
    MetaCyc:EG11845-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfoquinovose isomeraseUniRule annotation (EC:5.3.1.31UniRule annotation)
    Short name:
    SQ isomeraseUniRule annotation
    Gene namesi
    Name:yihS
    Ordered Locus Names:b3880, JW5569
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11845. yihS.

    Pathology & Biotechi

    Disruption phenotypei

    Mutant fails to grow on sulfoquinovose as a sole carbon source.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551R → A: Loss of activity. 1 Publication
    Mutagenesisi176 – 1761H → A: Loss of activity. 1 Publication
    Mutagenesisi248 – 2481H → A: Loss of activity. 1 Publication
    Mutagenesisi251 – 2511E → A: Strong decrease in activity. 1 Publication
    Mutagenesisi320 – 3201E → A: Loss of activity. 1 Publication
    Mutagenesisi383 – 3831H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 413413Sulfoquinovose isomerasePRO_0000208954Add
    BLAST

    Proteomic databases

    PaxDbiP32140.

    Expressioni

    Inductioni

    Induced during growth with sulfoquinovose.1 Publication

    Interactioni

    Subunit structurei

    Homohexamer.UniRule annotation1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4262638. 4 interactions.
    STRINGi511145.b3880.

    Structurei

    Secondary structure

    1
    413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2418Combined sources
    Helixi25 – 273Combined sources
    Helixi44 – 463Combined sources
    Helixi50 – 6516Combined sources
    Helixi71 – 8212Combined sources
    Turni83 – 864Combined sources
    Turni89 – 913Combined sources
    Beta strandi96 – 994Combined sources
    Beta strandi102 – 1054Combined sources
    Helixi110 – 12415Combined sources
    Turni125 – 1273Combined sources
    Helixi131 – 14515Combined sources
    Turni149 – 1524Combined sources
    Helixi171 – 18616Combined sources
    Helixi191 – 20414Combined sources
    Turni205 – 2084Combined sources
    Helixi209 – 2124Combined sources
    Turni228 – 2336Combined sources
    Beta strandi242 – 2443Combined sources
    Helixi246 – 26520Combined sources
    Helixi273 – 28917Combined sources
    Beta strandi293 – 2953Combined sources
    Beta strandi308 – 3103Combined sources
    Helixi315 – 33218Combined sources
    Helixi336 – 35116Combined sources
    Turni355 – 3573Combined sources
    Beta strandi358 – 3603Combined sources
    Beta strandi362 – 3643Combined sources
    Turni382 – 3843Combined sources
    Helixi385 – 3884Combined sources
    Helixi390 – 3923Combined sources
    Beta strandi395 – 3973Combined sources
    Helixi399 – 4046Combined sources
    Turni408 – 4114Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RGKX-ray2.50A/B/C/D/E/F1-413[»]
    ProteinModelPortaliP32140.
    SMRiP32140. Positions 1-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32140.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the N-acylglucosamine 2-epimerase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4107QKS. Bacteria.
    COG2942. LUCA.
    HOGENOMiHOG000244284.
    InParanoidiP32140.
    KOiK18479.
    OMAiANMHMTE.
    OrthoDBiEOG6TN45W.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    HAMAPiMF_00998. SQ_isomerase.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR030875. SQ_isomerase.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32140-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKWFNTLSHN RWLEQETDRI FDFGKNSVVP TGFGWLGNKG QIKEEMGTHL
    60 70 80 90 100
    WITARMLHVY SVAAAMGRPG AYSLVDHGIK AMNGALRDKK YGGWYACVND
    110 120 130 140 150
    EGVVDASKQG YQHFFALLGA ASAVTTGHPE ARKLLDYTIE IIEKYFWSEE
    160 170 180 190 200
    EQMCLESWDE AFSKTEEYRG GNANMHAVEA FLIVYDVTHD KKWLDRAIRV
    210 220 230 240 250
    ASVIIHDVAR NNHYRVNEHF DTQWNPLPDY NKDNPAHRFR AFGGTPGHWI
    260 270 280 290 300
    EWGRLMLHIH AALEARCEQP PAWLLEDAKG LFNATVRDAW APDGADGIVY
    310 320 330 340 350
    TVDWEGKPVV RERVRWPIVE AMGTAYALYT VTGDRQYETW YQTWWEYCIK
    360 370 380 390 400
    YLMDYENGSW WQELDADNKV TTKVWDGKQD IYHLLHCLVI PRIPLAPGMA
    410
    PAVAAGLLDI NAK
    Length:413
    Mass (Da):47,433
    Last modified:December 15, 1998 - v2
    Checksum:i00BC3BCD31779BE6
    GO

    Sequence cautioni

    The sequence AAB03013.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03013.1. Different initiation.
    U00096 Genomic DNA. Translation: AAD13442.2.
    AP009048 Genomic DNA. Translation: BAE77429.1.
    PIRiS40824.
    RefSeqiNP_418316.4. NC_000913.3.
    WP_000870916.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAD13442; AAD13442; b3880.
    BAE77429; BAE77429; BAE77429.
    GeneIDi948374.
    KEGGiecj:JW5569.
    eco:b3880.
    PATRICi32123263. VBIEscCol129921_3992.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03013.1. Different initiation.
    U00096 Genomic DNA. Translation: AAD13442.2.
    AP009048 Genomic DNA. Translation: BAE77429.1.
    PIRiS40824.
    RefSeqiNP_418316.4. NC_000913.3.
    WP_000870916.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RGKX-ray2.50A/B/C/D/E/F1-413[»]
    ProteinModelPortaliP32140.
    SMRiP32140. Positions 1-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262638. 4 interactions.
    STRINGi511145.b3880.

    Proteomic databases

    PaxDbiP32140.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD13442; AAD13442; b3880.
    BAE77429; BAE77429; BAE77429.
    GeneIDi948374.
    KEGGiecj:JW5569.
    eco:b3880.
    PATRICi32123263. VBIEscCol129921_3992.

    Organism-specific databases

    EchoBASEiEB1791.
    EcoGeneiEG11845. yihS.

    Phylogenomic databases

    eggNOGiENOG4107QKS. Bacteria.
    COG2942. LUCA.
    HOGENOMiHOG000244284.
    InParanoidiP32140.
    KOiK18479.
    OMAiANMHMTE.
    OrthoDBiEOG6TN45W.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11845-MONOMER.
    ECOL316407:JW5569-MONOMER.
    MetaCyc:EG11845-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP32140.
    PROiP32140.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    HAMAPiMF_00998. SQ_isomerase.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR030875. SQ_isomerase.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle."
      Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D., Huhn T., Cook A.M., Schleheck D.
      Nature 507:114-117(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12.
    5. "Crystal structure of YihS in complex with D-mannose: structural annotation of Escherichia coli and Salmonella enterica yihS-encoded proteins to an aldose-ketose isomerase."
      Itoh T., Mikami B., Hashimoto W., Murata K.
      J. Mol. Biol. 377:1443-1459(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION AS AN ISOMERASE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES, MUTAGENESIS OF ARG-55; HIS-176; HIS-248; GLU-251; GLU-320 AND HIS-383.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiSQUS_ECOLI
    AccessioniPrimary (citable) accession number: P32140
    Secondary accession number(s): Q2M8H7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: December 15, 1998
    Last modified: January 20, 2016
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.