ID SQASE_ECOLI Reviewed; 678 AA. AC P32138; P76775; Q2M8H5; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 13-APR-2016, entry version 120. DE RecName: Full=Sulfoquinovosidase {ECO:0000303|PubMed:26878550}; DE Short=SQase {ECO:0000303|PubMed:26878550}; DE EC=3.2.1.- {ECO:0000269|PubMed:26878550}; GN Name=yihQ {ECO:0000303|PubMed:26878550, ECO:0000312|EMBL:AAC76875.1}; GN Synonyms=squQ {ECO:0000312|EcoGene:EG11843}; GN OrderedLocusNames=b3878, JW3849; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 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 RT region from 87.2 to 89.2 minutes."; RL Nucleic Acids Res. 21:3391-3398(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION RP TO 358 AND 517. 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., RA Mau B., 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION. RX PubMed=15294295; DOI=10.1016/j.pep.2004.05.008; RA Okuyama M., Mori H., Chiba S., Kimura A.; RT "Overexpression and characterization of two unknown proteins, YicI and RT YihQ, originated from Escherichia coli."; RL Protein Expr. Purif. 37:170-179(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PATHWAY. 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 [6] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-472 RP IN COMPLEXES WITH THE SUBSTRATE ANALOG RP 4-NITROPHENYL-ALPHA-D-SULFOQUINOVOSIDE AND THE INHIBITOR 5FIDOF, RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME RP REGULATION, ACTIVE SITE, REACTION MECHANISM, AND MUTAGENESIS OF RP ARG-301; TRP-304; ASP-405 AND ASP-472. RC STRAIN=K12 / DH5-alpha; RX PubMed=26878550; DOI=10.1038/nchembio.2023; RA Speciale G., Jin Y., Davies G.J., Williams S.J., Goddard-Borger E.D.; RT "YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl RT diacylglyceride sulfolipids."; RL Nat. Chem. Biol. 0:0-0(2016). CC -!- FUNCTION: Catalyzes the hydrolysis of sulfoquinovosyl CC diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then CC degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) CC sulfoglycolysis pathway as a source of carbon and sulfur. CC Therefore, is likely involved in the utilization of the CC sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is CC also able to hydrolyze simple sulfoquinovosides such as 1- CC sulfoquinovosylglycerol (SQGro). Is a retaining glycoside CC hydrolase, since it forms the alpha anomer of SQ CC (PubMed:26878550). Also exhibits some alpha-glucosidase activity CC against alpha-glucosyl fluoride in vitro, although natural CC substrates, such as alpha-glucobioses are scarcely hydrolyzed CC (PubMed:15294295). {ECO:0000269|PubMed:15294295, CC ECO:0000269|PubMed:26878550}. CC -!- CATALYTIC ACTIVITY: An alpha-sulfoquinovosyl diacylglycerol + CC H(2)O = sulfoquinovose + a 1,2-diacylglycerol. CC {ECO:0000269|PubMed:26878550}. CC -!- ENZYME REGULATION: Is inactivated in vitro by the mechanism-based CC inactivator 5-fluoro-beta-L-idopyranosyl fluoride (5FIdoF) that CC yields a covalent glycosyl-enzyme complex with the active site CC nucleophile Asp-405. {ECO:0000269|PubMed:26878550}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.22 mM for para-nitrophenyl alpha-sulfoquinovoside CC {ECO:0000269|PubMed:26878550}; CC Note=kcat is 14.3 sec(-1) with para-nitrophenyl alpha- CC sulfoquinovoside as substrate. {ECO:0000269|PubMed:26878550}; CC pH dependence: CC Optimum pH is 6. {ECO:0000269|PubMed:26878550}; CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000305|PubMed:24463506}. CC -!- INDUCTION: Induced during growth with sulfoquinovose. CC {ECO:0000269|PubMed:24463506}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L19201; AAB03011.1; -; Genomic_DNA. DR EMBL; U00096; AAC76875.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77431.1; -; Genomic_DNA. DR PIR; A65193; A65193. DR RefSeq; NP_418314.1; NC_000913.3. DR RefSeq; WP_000380843.1; NZ_LN832404.1. DR PDB; 5AED; X-ray; 1.91 A; A/B=1-678. DR PDB; 5AEE; X-ray; 1.85 A; A/B=1-678. DR PDB; 5AEG; X-ray; 1.85 A; A/B=1-678. DR PDBsum; 5AED; -. DR PDBsum; 5AEE; -. DR PDBsum; 5AEG; -. DR ProteinModelPortal; P32138; -. DR SMR; P32138; 309-635. DR BioGrid; 4260866; 11. DR DIP; DIP-12498N; -. DR IntAct; P32138; 1. DR MINT; MINT-1249337; -. DR STRING; 511145.b3878; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR PaxDb; P32138; -. DR EnsemblBacteria; AAC76875; AAC76875; b3878. DR EnsemblBacteria; BAE77431; BAE77431; BAE77431. DR GeneID; 948376; -. DR KEGG; ecj:JW3849; -. DR KEGG; eco:b3878; -. DR PATRIC; 32123259; VBIEscCol129921_3990. DR EchoBASE; EB1789; -. DR EcoGene; EG11843; yihQ. DR eggNOG; ENOG4105CJQ; Bacteria. DR eggNOG; COG1501; LUCA. DR HOGENOM; HOG000064244; -. DR InParanoid; P32138; -. DR KO; K15922; -. DR OMA; HYEDDAR; -. DR OrthoDB; EOG6Z99WN; -. DR PhylomeDB; P32138; -. DR BioCyc; EcoCyc:EG11843-MONOMER; -. DR BioCyc; ECOL316407:JW3849-MONOMER; -. DR PRO; PR:P32138; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR000322; Glyco_hydro_31. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF01055; Glyco_hydro_31; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosidase; Hydrolase; KW Reference proteome. FT CHAIN 1 678 Sulfoquinovosidase. FT /FTId=PRO_0000185372. FT REGION 301 304 Substrate binding. FT {ECO:0000305|PubMed:26878550}. FT ACT_SITE 405 405 Nucleophile. FT {ECO:0000269|PubMed:26878550}. FT ACT_SITE 408 408 {ECO:0000250|UniProtKB:P31434}. FT ACT_SITE 472 472 Proton donor. FT {ECO:0000305|PubMed:26878550}. FT BINDING 288 288 Substrate. {ECO:0000305|PubMed:26878550}. FT BINDING 537 537 Substrate. {ECO:0000305|PubMed:26878550}. FT MUTAGEN 288 288 Q->E: Loss of catalytic activity against FT para-nitrophenyl alpha-sulfoquinovoside, FT but in contrast to wild-type, possesses a FT very weak alpha-glucosidase activity FT against para-nitrophenyl alpha-D- FT glucopyranoside. FT {ECO:0000269|PubMed:26878550}. FT MUTAGEN 301 301 R->A,E: Loss of catalytic activity. FT {ECO:0000269|PubMed:26878550}. FT MUTAGEN 301 301 R->K: Almost complete loss of catalytic FT activity. {ECO:0000269|PubMed:26878550}. FT MUTAGEN 301 301 R->Q: 13-fold decrease in substrate FT affinity and 4600-fold decrease in FT catalytic activity. FT {ECO:0000269|PubMed:26878550}. FT MUTAGEN 304 304 W->F: Loss of catalytic activity. FT {ECO:0000269|PubMed:26878550}. FT MUTAGEN 405 405 D->A,N: Loss of catalytic activity. FT {ECO:0000269|PubMed:26878550}. FT MUTAGEN 472 472 D->A,N: Loss of catalytic activity. FT {ECO:0000269|PubMed:26878550}. FT CONFLICT 358 358 A -> R (in Ref. 1; AAB03011). FT {ECO:0000305}. FT CONFLICT 517 517 S -> T (in Ref. 1; AAB03011). FT {ECO:0000305}. SQ SEQUENCE 678 AA; 77275 MW; 85869F52BB72FEE7 CRC64; MDTPRPQLLD FQFHQNNDSF TLHFQQRLIL THSKDNPCLW IGSGIADIDM FRGNFSIKDK LQEKIALTDA IVSQSPDGWL IHFSRGSDIS ATLNISADDQ GRLLLELQND NLNHNRIWLR LAAQPEDHIY GCGEQFSYFD LRGKPFPLWT SEQGVGRNKQ TYVTWQADCK ENAGGDYYWT FFPQPTFVST QKYYCHVDNS CYMNFDFSAP EYHELALWED KATLRFECAD TYISLLEKLT ALLGRQPELP DWIYDGVTLG IQGGTEVCQK KLDTMRNAGV KVNGIWAQDW SGIRMTSFGK RVMWNWKWNS ENYPQLDSRI KQWNQEGVQF LAYINPYVAS DKDLCEEAAQ HGYLAKDASG GDYLVEFGEF YGGVVDLTNP EAYAWFKEVI KKNMIELGCG GWMADFGEYL PTDTYLHNGV SAEIMHNAWP ALWAKCNYEA LEETGKLGEI LFFMRAGSTG SQKYSTMMWA GDQNVDWSLD DGLASVVPAA LSLAMTGHGL HHSDIGGYTT LFEMKRSKEL LLRWCDFSAF TPMMRTHEGN RPGDNWQFDG DAETIAHFAR MTTVFTTLKP YLKEAVALNA KSGLPVMRPL FLHYEDDAHT YTLKYQYLLG RDILVAPVHE EGRSDWTLYL PEDNWVHAWT GEAFRGGEVT VNAPIGKPPV FYRADSEWAA LFASLKSI //