Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sulfoquinovosidase

Gene

yihQ

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

Functioni

Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as 1-sulfoquinovosylglycerol (SQGro). Is a retaining glycoside hydrolase, since it forms the alpha anomer of SQ (PubMed:26878550). Also exhibits some alpha-glucosidase activity against alpha-glucosyl fluoride in vitro, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed (PubMed:15294295).2 Publications

Catalytic activityi

An alpha-sulfoquinovosyl diacylglycerol + H2O = sulfoquinovose + a 1,2-diacylglycerol.1 Publication

Enzyme regulationi

Is inactivated in vitro by the mechanism-based inactivator 5-fluoro-beta-L-idopyranosyl fluoride (5FIdoF) that yields a covalent glycosyl-enzyme complex with the active site nucleophile Asp-405.1 Publication

Kineticsi

kcat is 14.3 sec(-1) with para-nitrophenyl alpha-sulfoquinovoside as substrate.1 Publication

  1. KM=0.22 mM for para-nitrophenyl alpha-sulfoquinovoside1 Publication

    pH dependencei

    Optimum pH is 6.1 Publication

    Pathwayi: Glycolipid metabolism

    This protein is involved in Glycolipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in Glycolipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei288 – 2881Substrate1 Publication
    Active sitei405 – 4051Nucleophile1 Publication
    Active sitei408 – 4081By similarity
    Active sitei472 – 4721Proton donor1 Publication
    Binding sitei537 – 5371Substrate1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11843-MONOMER.
    ECOL316407:JW3849-MONOMER.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfoquinovosidase1 Publication (EC:3.2.1.-1 Publication)
    Short name:
    SQase1 Publication
    Gene namesi
    Name:yihQ1 PublicationImported
    Synonyms:squQImported
    Ordered Locus Names:b3878, JW3849
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11843. yihQ.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi288 – 2881Q → E: Loss of catalytic activity against para-nitrophenyl alpha-sulfoquinovoside, but in contrast to wild-type, possesses a very weak alpha-glucosidase activity against para-nitrophenyl alpha-D-glucopyranoside. 1 Publication
    Mutagenesisi301 – 3011R → A or E: Loss of catalytic activity. 1 Publication
    Mutagenesisi301 – 3011R → K: Almost complete loss of catalytic activity. 1 Publication
    Mutagenesisi301 – 3011R → Q: 13-fold decrease in substrate affinity and 4600-fold decrease in catalytic activity. 1 Publication
    Mutagenesisi304 – 3041W → F: Loss of catalytic activity. 1 Publication
    Mutagenesisi405 – 4051D → A or N: Loss of catalytic activity. 1 Publication
    Mutagenesisi472 – 4721D → A or N: Loss of catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 678678SulfoquinovosidasePRO_0000185372Add
    BLAST

    Proteomic databases

    PaxDbiP32138.

    Expressioni

    Inductioni

    Induced during growth with sulfoquinovose.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi4260866. 11 interactions.
    DIPiDIP-12498N.
    IntActiP32138. 1 interaction.
    MINTiMINT-1249337.
    STRINGi511145.b3878.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5AEDX-ray1.91A/B1-678[»]
    5AEEX-ray1.85A/B1-678[»]
    5AEGX-ray1.85A/B1-678[»]
    ProteinModelPortaliP32138.
    SMRiP32138. Positions 309-635.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni301 – 3044Substrate binding1 Publication

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CJQ. Bacteria.
    COG1501. LUCA.
    HOGENOMiHOG000064244.
    InParanoidiP32138.
    KOiK15922.
    OMAiHYEDDAR.
    OrthoDBiEOG6Z99WN.
    PhylomeDBiP32138.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32138-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDTPRPQLLD FQFHQNNDSF TLHFQQRLIL THSKDNPCLW IGSGIADIDM
    60 70 80 90 100
    FRGNFSIKDK LQEKIALTDA IVSQSPDGWL IHFSRGSDIS ATLNISADDQ
    110 120 130 140 150
    GRLLLELQND NLNHNRIWLR LAAQPEDHIY GCGEQFSYFD LRGKPFPLWT
    160 170 180 190 200
    SEQGVGRNKQ TYVTWQADCK ENAGGDYYWT FFPQPTFVST QKYYCHVDNS
    210 220 230 240 250
    CYMNFDFSAP EYHELALWED KATLRFECAD TYISLLEKLT ALLGRQPELP
    260 270 280 290 300
    DWIYDGVTLG IQGGTEVCQK KLDTMRNAGV KVNGIWAQDW SGIRMTSFGK
    310 320 330 340 350
    RVMWNWKWNS ENYPQLDSRI KQWNQEGVQF LAYINPYVAS DKDLCEEAAQ
    360 370 380 390 400
    HGYLAKDASG GDYLVEFGEF YGGVVDLTNP EAYAWFKEVI KKNMIELGCG
    410 420 430 440 450
    GWMADFGEYL PTDTYLHNGV SAEIMHNAWP ALWAKCNYEA LEETGKLGEI
    460 470 480 490 500
    LFFMRAGSTG SQKYSTMMWA GDQNVDWSLD DGLASVVPAA LSLAMTGHGL
    510 520 530 540 550
    HHSDIGGYTT LFEMKRSKEL LLRWCDFSAF TPMMRTHEGN RPGDNWQFDG
    560 570 580 590 600
    DAETIAHFAR MTTVFTTLKP YLKEAVALNA KSGLPVMRPL FLHYEDDAHT
    610 620 630 640 650
    YTLKYQYLLG RDILVAPVHE EGRSDWTLYL PEDNWVHAWT GEAFRGGEVT
    660 670
    VNAPIGKPPV FYRADSEWAA LFASLKSI
    Length:678
    Mass (Da):77,275
    Last modified:July 15, 1998 - v3
    Checksum:i85869F52BB72FEE7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti358 – 3581A → R in AAB03011 (PubMed:8346018).Curated
    Sequence conflicti517 – 5171S → T in AAB03011 (PubMed:8346018).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03011.1.
    U00096 Genomic DNA. Translation: AAC76875.1.
    AP009048 Genomic DNA. Translation: BAE77431.1.
    PIRiA65193.
    RefSeqiNP_418314.1. NC_000913.3.
    WP_000380843.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76875; AAC76875; b3878.
    BAE77431; BAE77431; BAE77431.
    GeneIDi948376.
    KEGGiecj:JW3849.
    eco:b3878.
    PATRICi32123259. VBIEscCol129921_3990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03011.1.
    U00096 Genomic DNA. Translation: AAC76875.1.
    AP009048 Genomic DNA. Translation: BAE77431.1.
    PIRiA65193.
    RefSeqiNP_418314.1. NC_000913.3.
    WP_000380843.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5AEDX-ray1.91A/B1-678[»]
    5AEEX-ray1.85A/B1-678[»]
    5AEGX-ray1.85A/B1-678[»]
    ProteinModelPortaliP32138.
    SMRiP32138. Positions 309-635.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260866. 11 interactions.
    DIPiDIP-12498N.
    IntActiP32138. 1 interaction.
    MINTiMINT-1249337.
    STRINGi511145.b3878.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Proteomic databases

    PaxDbiP32138.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76875; AAC76875; b3878.
    BAE77431; BAE77431; BAE77431.
    GeneIDi948376.
    KEGGiecj:JW3849.
    eco:b3878.
    PATRICi32123259. VBIEscCol129921_3990.

    Organism-specific databases

    EchoBASEiEB1789.
    EcoGeneiEG11843. yihQ.

    Phylogenomic databases

    eggNOGiENOG4105CJQ. Bacteria.
    COG1501. LUCA.
    HOGENOMiHOG000064244.
    InParanoidiP32138.
    KOiK15922.
    OMAiHYEDDAR.
    OrthoDBiEOG6Z99WN.
    PhylomeDBiP32138.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11843-MONOMER.
    ECOL316407:JW3849-MONOMER.

    Miscellaneous databases

    PROiP32138.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 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], SEQUENCE REVISION TO 358 AND 517.
      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. "Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli."
      Okuyama M., Mori H., Chiba S., Kimura A.
      Protein Expr. Purif. 37:170-179(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "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: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, PATHWAY.
      Strain: K12.
    6. "YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids."
      Speciale G., Jin Y., Davies G.J., Williams S.J., Goddard-Borger E.D.
      Nat. Chem. Biol. 0:0-0(2016) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-472 IN COMPLEXES WITH THE SUBSTRATE ANALOG 4-NITROPHENYL-ALPHA-D-SULFOQUINOVOSIDE AND THE INHIBITOR 5FIDOF, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, ACTIVE SITE, REACTION MECHANISM, MUTAGENESIS OF ARG-301; TRP-304; ASP-405 AND ASP-472.
      Strain: K12 / DH5-alpha.

    Entry informationi

    Entry nameiSQASE_ECOLI
    AccessioniPrimary (citable) accession number: P32138
    Secondary accession number(s): P76775, Q2M8H5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: July 15, 1998
    Last modified: April 13, 2016
    This is version 120 of the entry and version 3 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. 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.