YEAD_SALTY
ID YEAD_SALTY Reviewed; 294 AA.
AC Q8ZPV9;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000250|UniProtKB:Q03161};
DE EC=5.1.3.15 {ECO:0000250|UniProtKB:Q03161};
DE AltName: Full=Putative D-hexose-6-phosphate mutarotase {ECO:0000250|UniProtKB:Q03161};
GN Name=yeaD {ECO:0000312|EMBL:AAL20214.1};
GN OrderedLocusNames=STM1289 {ECO:0000312|EMBL:AAL20214.1};
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:2HTA, ECO:0007744|PDB:2HTB}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, ACTIVE SITE, AND PROBABLE
RP FUNCTION.
RX PubMed=17242513; DOI=10.1107/s090744490604618x;
RA Chittori S., Simanshu D.K., Savithri H.S., Murthy M.R.;
RT "Structure of the putative mutarotase YeaD from Salmonella typhimurium:
RT structural comparison with galactose mutarotases.";
RL Acta Crystallogr. D 63:197-205(2007).
CC -!- FUNCTION: Probably functions as a hexose-6-phosphate 1-epimerase.
CC {ECO:0000305|PubMed:17242513}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC EC=5.1.3.15; Evidence={ECO:0000250|UniProtKB:Q03161};
CC -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:17242513}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL20214.1; -; Genomic_DNA.
DR RefSeq; NP_460255.1; NC_003197.2.
DR RefSeq; WP_000608662.1; NC_003197.2.
DR PDB; 2HTA; X-ray; 1.90 A; A/B=1-294.
DR PDB; 2HTB; X-ray; 2.50 A; A/B/C/D=1-294.
DR PDBsum; 2HTA; -.
DR PDBsum; 2HTB; -.
DR AlphaFoldDB; Q8ZPV9; -.
DR SMR; Q8ZPV9; -.
DR STRING; 99287.STM1289; -.
DR PaxDb; Q8ZPV9; -.
DR EnsemblBacteria; AAL20214; AAL20214; STM1289.
DR GeneID; 1252807; -.
DR KEGG; stm:STM1289; -.
DR PATRIC; fig|99287.12.peg.1370; -.
DR HOGENOM; CLU_048345_4_1_6; -.
DR OMA; TQALHSY; -.
DR PhylomeDB; Q8ZPV9; -.
DR BioCyc; SENT99287:STM1289-MON; -.
DR EvolutionaryTrace; Q8ZPV9; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09020; D-hex-6-P-epi_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR025532; G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..294
FT /note="Putative glucose-6-phosphate 1-epimerase"
FT /id="PRO_0000436310"
FT ACT_SITE 164
FT /evidence="ECO:0000250|UniProtKB:Q03161,
FT ECO:0000305|PubMed:17242513"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:Q03161,
FT ECO:0000305|PubMed:17242513"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT HELIX 1..7
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2HTA"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:2HTA"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 136..163
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2HTA"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2HTA"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:2HTA"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2HTA"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:2HTA"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 263..278
FT /evidence="ECO:0007829|PDB:2HTA"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:2HTA"
SQ SEQUENCE 294 AA; 32560 MW; 80974EE1F913ECFA CRC64;
MINKIFALPV IEQLTPVLSR RQLDDLDLIV VDHPQVKASF ALQGAHLLSW KPVGEEEVLW
LSNNTPFKTG VALRGGVPIC WPWFGPAAQQ GLPSHGFARN LPWALKAHNE DDNGVMLTFE
LQSSEATRKY WPHDFTLLAR FKVGKTCEIE LEAHGEFATT SALHSYFNVG DIANVKVSGL
GDRFIDKVND AKEGVLTDGI QTFPDRTDRV YLNPEACSVI HDATLNRTID VVHHHHLNVV
GWNPGPALSV SMGDMPDDGY KTFVCVETVY ATAPQQATEE KPSRLAQTIC VAKR
