SQUS_SALTY
ID SQUS_SALTY Reviewed; 413 AA.
AC Q8ZKT7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Sulfoquinovose isomerase {ECO:0000255|HAMAP-Rule:MF_00998};
DE Short=SQ isomerase {ECO:0000255|HAMAP-Rule:MF_00998};
DE EC=5.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00998};
GN Name=yihS; OrderedLocusNames=STM4021;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0007744|PDB:2AFA}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-413.
RA Kumaran D., Swaminathan S.;
RT "Crystal Structure of putative NAG isomerase from Salmonella typhimurium.";
RL Submitted (JUL-2005) to the PDB data bank.
RN [3] {ECO:0007744|PDB:2ZBL}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANT ALA-248 IN COMPLEX WITH
RP BETA-D-MANNOSE, FUNCTION AS AN ISOMERASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND ACTIVE SITES.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=18328504; DOI=10.1016/j.jmb.2008.01.090;
RA Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Crystal structure of YihS in complex with D-mannose: structural annotation
RT of Escherichia coli and Salmonella enterica yihS-encoded proteins to an
RT aldose-ketose isomerase.";
RL J. Mol. Biol. 377:1443-1459(2008).
CC -!- FUNCTION: Catalyzes the isomerization of sulfoquinovose (SQ) to 6-
CC deoxy-6-sulfo-D-fructose (SF) (By similarity). In vitro, can also
CC catalyze the interconversion of mannose, fructose and glucose, but has
CC extremely low activity with glucose (PubMed:18328504).
CC {ECO:0000255|HAMAP-Rule:MF_00998, ECO:0000269|PubMed:18328504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-sulfo-beta-D-quinovose = 6-deoxy-6-sulfo-D-fructose;
CC Xref=Rhea:RHEA:40439, ChEBI:CHEBI:77133, ChEBI:CHEBI:142957;
CC EC=5.3.1.31; Evidence={ECO:0000255|HAMAP-Rule:MF_00998};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=134 mM for D-mannose {ECO:0000269|PubMed:18328504};
CC KM=292 mM for D-fructose {ECO:0000269|PubMed:18328504};
CC Note=kcat is 23.3 sec(-1) for D-mannose. kcat is 12.3 sec(-1) for D-
CC fructose. {ECO:0000269|PubMed:18328504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00998,
CC ECO:0000269|PubMed:18328504}.
CC -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00998}.
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DR EMBL; AE006468; AAL22860.1; -; Genomic_DNA.
DR RefSeq; NP_462901.1; NC_003197.2.
DR RefSeq; WP_000870946.1; NC_003197.2.
DR PDB; 2AFA; X-ray; 2.15 A; A/B/C/D/E/F=2-413.
DR PDB; 2ZBL; X-ray; 1.60 A; A/B/C/D/E/F=1-413.
DR PDB; 7AG4; X-ray; 2.13 A; A/B/C/D/E/F=1-413.
DR PDBsum; 2AFA; -.
DR PDBsum; 2ZBL; -.
DR PDBsum; 7AG4; -.
DR AlphaFoldDB; Q8ZKT7; -.
DR SMR; Q8ZKT7; -.
DR STRING; 99287.STM4021; -.
DR PaxDb; Q8ZKT7; -.
DR DNASU; 1255547; -.
DR EnsemblBacteria; AAL22860; AAL22860; STM4021.
DR GeneID; 1255547; -.
DR KEGG; stm:STM4021; -.
DR PATRIC; fig|99287.12.peg.4236; -.
DR HOGENOM; CLU_042253_0_0_6; -.
DR OMA; WVQAETF; -.
DR PhylomeDB; Q8ZKT7; -.
DR BioCyc; SENT99287:STM4021-MON; -.
DR EvolutionaryTrace; Q8ZKT7; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0061593; F:sulfoquinovose isomerase activity; IBA:GO_Central.
DR GO; GO:0061720; P:6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00249; AGE; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR HAMAP; MF_00998; SQ_isomerase; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR034116; AGE_dom.
DR InterPro; IPR030875; SQ_isomerase.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..413
FT /note="Sulfoquinovose isomerase"
FT /id="PRO_0000429134"
FT ACT_SITE 248
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT ACT_SITE 383
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00998,
FT ECO:0000305|PubMed:18328504"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 228..233
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 246..265
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:7AG4"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 335..351
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2ZBL"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2ZBL"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:2ZBL"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:2ZBL"
SQ SEQUENCE 413 AA; 47527 MW; 030CB11DC3A1A2E3 CRC64;
MKWFNTLSHN RWLEQETDRI FNFGKNAVVP TGFGWLGNKG QIKEEMGTHL WITARMLHVY
SVAASMGRPG AYDLVDHGIK AMNGALRDKK YGGWYACVND QGVVDASKQG YQHFFALLGA
ASAVTTGHPE ARKLLDYTIE VIEKYFWSEE EQMCLESWDE AFSQTEDYRG GNANMHAVEA
FLIVYDVTHD KKWLDRALRI ASVIIHDVAR NGDYRVNEHF DSQWNPIRDY NKDNPAHRFR
AYGGTPGHWI EWGRLMLHLH AALEARFETP PAWLLEDAKG LFHATIRDAW APDGADGFVY
SVDWDGKPIV RERVRWPIVE AMGTAYALYT LTDDSQYEEW YQKWWDYCIK YLMDYENGSW
WQELDADNKV TTKVWDGKQD IYHLLHCLVI PRLPLAPGLA PAVAAGLLDI NAK
