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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)DescriptionActionsGraphical viewLength
    Binding sitei55SubstrateUniRule annotation1
    Binding sitei111SubstrateUniRule annotation1
    Binding sitei172SubstrateUniRule annotation1
    Binding sitei176SubstrateUniRule annotation1
    Binding sitei238Substrate; via carbonyl oxygenUniRule annotation1
    Active sitei248Proton donor/acceptor1 Publication1
    Binding sitei251SubstrateUniRule annotation1
    Binding sitei316SubstrateUniRule annotation1
    Active sitei383Proton donor/acceptor1 Publication1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi55R → A: Loss of activity. 1 Publication1
    Mutagenesisi176H → A: Loss of activity. 1 Publication1
    Mutagenesisi248H → A: Loss of activity. 1 Publication1
    Mutagenesisi251E → A: Strong decrease in activity. 1 Publication1
    Mutagenesisi320E → A: Loss of activity. 1 Publication1
    Mutagenesisi383H → A: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002089541 – 413Sulfoquinovose isomeraseAdd BLAST413

    Proteomic databases

    PaxDbiP32140.
    PRIDEiP32140.

    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 interactors.
    STRINGi511145.b3880.

    Structurei

    Secondary structure

    1413
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 24Combined sources18
    Helixi25 – 27Combined sources3
    Helixi44 – 46Combined sources3
    Helixi50 – 65Combined sources16
    Helixi71 – 82Combined sources12
    Turni83 – 86Combined sources4
    Turni89 – 91Combined sources3
    Beta strandi96 – 99Combined sources4
    Beta strandi102 – 105Combined sources4
    Helixi110 – 124Combined sources15
    Turni125 – 127Combined sources3
    Helixi131 – 145Combined sources15
    Turni149 – 152Combined sources4
    Helixi171 – 186Combined sources16
    Helixi191 – 204Combined sources14
    Turni205 – 208Combined sources4
    Helixi209 – 212Combined sources4
    Turni228 – 233Combined sources6
    Beta strandi242 – 244Combined sources3
    Helixi246 – 265Combined sources20
    Helixi273 – 289Combined sources17
    Beta strandi293 – 295Combined sources3
    Beta strandi308 – 310Combined sources3
    Helixi315 – 332Combined sources18
    Helixi336 – 351Combined sources16
    Turni355 – 357Combined sources3
    Beta strandi358 – 360Combined sources3
    Beta strandi362 – 364Combined sources3
    Turni382 – 384Combined sources3
    Helixi385 – 388Combined sources4
    Helixi390 – 392Combined sources3
    Beta strandi395 – 397Combined sources3
    Helixi399 – 404Combined sources6
    Turni408 – 411Combined sources4

    3D structure databases

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

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    HAMAPiMF_00998. SQ_isomerase. 1 hit.
    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 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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2RGKX-ray2.50A/B/C/D/E/F1-413[»]
    ProteinModelPortaliP32140.
    SMRiP32140.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262638. 4 interactors.
    STRINGi511145.b3880.

    Proteomic databases

    PaxDbiP32140.
    PRIDEiP32140.

    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.

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

    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: November 2, 2016
    This is version 118 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.