SQASE_ECOLI
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 03-AUG-2022, entry version 154.
DE RecName: Full=Sulfoquinovosidase {ECO:0000303|PubMed:26878550};
DE Short=SQase {ECO:0000303|PubMed:26878550};
DE EC=3.2.1.199 {ECO:0000269|PubMed:26878550};
GN Name=yihQ {ECO:0000303|PubMed:26878550, ECO:0000312|EMBL:AAC76875.1};
GN Synonyms=squQ; OrderedLocusNames=b3878, JW3849;
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], AND SEQUENCE REVISION TO 358
RP 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., 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.
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 IN
RP COMPLEXES WITH THE SUBSTRATE ANALOG 4-NITROPHENYL-ALPHA-D-SULFOQUINOVOSIDE
RP AND THE INHIBITOR 5FIDOF, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, ACTIVE SITE, REACTION MECHANISM, AND
RP MUTAGENESIS OF 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 diacylglyceride
RT sulfolipids.";
RL Nat. Chem. Biol. 12:215-217(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides
CC (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through
CC the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a
CC source of carbon and sulfur. Therefore, is likely involved in the
CC utilization of the sulfoquinovose headgroup found in ubiquitous plant
CC sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as
CC 1-sulfoquinovosylglycerol (SQGro). Is a retaining glycoside hydrolase,
CC since it forms the alpha anomer of SQ (PubMed:26878550). Also exhibits
CC some alpha-glucosidase activity against alpha-glucosyl fluoride in
CC vitro, although natural substrates, such as alpha-glucobioses are
CC scarcely hydrolyzed (PubMed:15294295). {ECO:0000269|PubMed:15294295,
CC ECO:0000269|PubMed:26878550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-sulfo-alpha-D-quinovosyldiacylglycerol + H2O = 6-sulfo-
CC alpha-D-quinovose + a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:49452,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:131487,
CC ChEBI:CHEBI:142956; EC=3.2.1.199;
CC Evidence={ECO:0000269|PubMed:26878550};
CC -!- ACTIVITY REGULATION: Is inactivated in vitro by the mechanism-based
CC inactivator 5-fluoro-beta-L-idopyranosyl fluoride (5FIdoF) that yields
CC a covalent glycosyl-enzyme complex with the active site nucleophile
CC 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. {ECO:0000305}.
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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 PDB; 5OHT; X-ray; 1.87 A; A/B=1-678.
DR PDBsum; 5AED; -.
DR PDBsum; 5AEE; -.
DR PDBsum; 5AEG; -.
DR PDBsum; 5OHT; -.
DR AlphaFoldDB; P32138; -.
DR SMR; P32138; -.
DR BioGRID; 4260866; 11.
DR DIP; DIP-12498N; -.
DR IntAct; P32138; 1.
DR STRING; 511145.b3878; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PaxDb; P32138; -.
DR PRIDE; P32138; -.
DR EnsemblBacteria; AAC76875; AAC76875; b3878.
DR EnsemblBacteria; BAE77431; BAE77431; BAE77431.
DR GeneID; 948376; -.
DR KEGG; ecj:JW3849; -.
DR KEGG; eco:b3878; -.
DR PATRIC; fig|1411691.4.peg.2833; -.
DR EchoBASE; EB1789; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_017110_0_1_6; -.
DR InParanoid; P32138; -.
DR OMA; GWPLLRM; -.
DR PhylomeDB; P32138; -.
DR BioCyc; EcoCyc:EG11843-MON; -.
DR BioCyc; MetaCyc:EG11843-MON; -.
DR BRENDA; 3.2.1.199; 2026.
DR SABIO-RK; P32138; -.
DR PRO; PR:P32138; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:1990929; F:sulfoquinovosidase activity; IDA:EcoCyc.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06594; GH31_glucosidase_YihQ; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR044112; YihQ-like.
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; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..678
FT /note="Sulfoquinovosidase"
FT /id="PRO_0000185372"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:26878550"
FT ACT_SITE 408
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 472
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:26878550"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26878550"
FT BINDING 301..304
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26878550"
FT BINDING 537
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26878550"
FT MUTAGEN 288
FT /note="Q->E: Loss of catalytic activity against para-
FT nitrophenyl alpha-sulfoquinovoside, but in contrast to
FT wild-type, possesses a very weak alpha-glucosidase activity
FT against para-nitrophenyl alpha-D-glucopyranoside."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 301
FT /note="R->A,E: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 301
FT /note="R->K: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 301
FT /note="R->Q: 13-fold decrease in substrate affinity and
FT 4600-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 304
FT /note="W->F: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 405
FT /note="D->A,N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT MUTAGEN 472
FT /note="D->A,N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26878550"
FT CONFLICT 358
FT /note="A -> R (in Ref. 1; AAB03011)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="S -> T (in Ref. 1; AAB03011)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:5AEG"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 38..51
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 54..66
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 212..228
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:5AEG"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 380..393
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 394..398
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 422..443
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 552..567
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 569..582
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 598..602
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 624..630
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:5AEE"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:5AEE"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:5AEE"
FT HELIX 674..677
FT /evidence="ECO:0007829|PDB:5AEE"
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
