SHB17_YEAST
ID SHB17_YEAST Reviewed; 271 AA.
AC P36136; D6VXA5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sedoheptulose 1,7-bisphosphatase;
DE EC=3.1.3.37;
GN Name=SHB17; OrderedLocusNames=YKR043C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FBP, SUBUNIT,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-12;
RP HIS-13; THR-16; SER-19; TYR-24; SER-65; ARG-69; GLU-99; TYR-102; TRP-131;
RP HIS-176; HIS-178 AND ARG-181, AND ACTIVE SITE.
RX PubMed=20427268; DOI=10.1074/jbc.m110.118315;
RA Kuznetsova E., Xu L., Singer A., Brown G., Dong A., Flick R., Cui H.,
RA Cuff M., Joachimiak A., Savchenko A., Yakunin A.F.;
RT "Structure and activity of the metal-independent fructose-1,6-
RT bisphosphatase YK23 from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:21049-21059(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SBP, SUBUNIT,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=21663798; DOI=10.1016/j.cell.2011.05.022;
RA Clasquin M.F., Melamud E., Singer A., Gooding J.R., Xu X., Dong A., Cui H.,
RA Campagna S.R., Savchenko A., Yakunin A.F., Rabinowitz J.D., Caudy A.A.;
RT "Riboneogenesis in yeast.";
RL Cell 145:969-980(2011).
CC -!- FUNCTION: Sedoheptulose 1,7-bisphosphatase involved in riboneogenesis.
CC Dephosphorylates sedoheptulose 1,7-bisphosphate (SBP), which is
CC converted via the non-oxidative pentose phosphate pathway to ribose-5-
CC phosphate. Has a fructose 1,6-bisphosphatase activity in vitro, but
CC this is probably not biologically relevant, since deletion does not
CC affect fructose 1,6-biphosphate (FBP) levels.
CC {ECO:0000269|PubMed:21663798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-
CC phosphate + phosphate; Xref=Rhea:RHEA:17461, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57483, ChEBI:CHEBI:58335; EC=3.1.3.37;
CC Evidence={ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for sedoheptulose 1,7-bisphosphate (SBP)
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC KM=0.2 mM for fructose 1,6-bisphosphate (FBP)
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC KM=0.7 mM for fructose 1,6-bisphosphate (in the presence of 1 mM
CC fructose 2,6-bisphosphate) {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798};
CC KM=2.3 mM for fructose 1,6-bisphosphate (in the presence of 2 mM
CC fructose 2,6-bisphosphate) {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798};
CC KM=1.4 mM for fructose 1-phosphate {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798};
CC KM=1.6 mM for glyceraldehyde 3-phosphate
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC KM=0.3 mM for erythrose 4-phosphate {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798};
CC Vmax=7.8 umol/min/mg enzyme toward sedoheptulose 1,7-bisphosphate
CC (SBP) {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=8.7 umol/min/mg enzyme toward fructose 1,6-bisphosphate (FBP)
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=7.3 umol/min/mg enzyme toward fructose 1,6-bisphosphate (in the
CC presence of 1 mM fructose 2,6-bisphosphate)
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=8.9 umol/min/mg enzyme toward fructose 1,6-bisphosphate,(in the
CC presence of 1 mM fructose 2,6-bisphosphate)
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=7.3 umol/min/mg enzyme toward fructose 1-phosphate
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=1 umol/min/mg enzyme toward glyceraldehyde 3-phosphate
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC Vmax=0.6 umol/min/mg enzyme toward erythrose 4-phosphate
CC {ECO:0000269|PubMed:20427268, ECO:0000269|PubMed:21663798};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20427268,
CC ECO:0000269|PubMed:21663798}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is correlated with levels of ribosomal proteins,
CC thus periodic SHB17 expression coincides with the peak demand for
CC ribose phosphate that occurs during ribosome synthesis.
CC {ECO:0000269|PubMed:21663798}.
CC -!- MISCELLANEOUS: Present with 11500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. SHB17
CC subfamily. {ECO:0000305}.
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DR EMBL; Z28268; CAA82119.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09195.1; -; Genomic_DNA.
DR PIR; S38115; S38115.
DR RefSeq; NP_012969.1; NM_001179833.1.
DR PDB; 3F3K; X-ray; 1.75 A; A/B=2-263.
DR PDB; 3LG2; X-ray; 2.60 A; A/B/C/D=1-271.
DR PDB; 3LL4; X-ray; 2.49 A; A/B=1-271.
DR PDB; 3OI7; X-ray; 2.40 A; A/B/C/D=1-271.
DR PDBsum; 3F3K; -.
DR PDBsum; 3LG2; -.
DR PDBsum; 3LL4; -.
DR PDBsum; 3OI7; -.
DR AlphaFoldDB; P36136; -.
DR SMR; P36136; -.
DR BioGRID; 34175; 102.
DR DIP; DIP-4847N; -.
DR IntAct; P36136; 1.
DR MINT; P36136; -.
DR STRING; 4932.YKR043C; -.
DR iPTMnet; P36136; -.
DR MaxQB; P36136; -.
DR PaxDb; P36136; -.
DR PRIDE; P36136; -.
DR DNASU; 853917; -.
DR EnsemblFungi; YKR043C_mRNA; YKR043C; YKR043C.
DR GeneID; 853917; -.
DR KEGG; sce:YKR043C; -.
DR SGD; S000001751; SHB17.
DR VEuPathDB; FungiDB:YKR043C; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_13_0_1; -.
DR InParanoid; P36136; -.
DR OMA; WLIWRDG; -.
DR BioCyc; YEAST:G3O-32014-MON; -.
DR BRENDA; 3.1.3.11; 984.
DR EvolutionaryTrace; P36136; -.
DR PRO; PR:P36136; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36136; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IDA:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046390; P:ribose phosphate biosynthetic process; IDA:SGD.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Hydrolase; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..271
FT /note="Sedoheptulose 1,7-bisphosphatase"
FT /id="PRO_0000203211"
FT ACT_SITE 13
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT ACT_SITE 99
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:20427268"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT BINDING 24..25
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20427268"
FT SITE 176
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:20427268"
FT MUTAGEN 12
FT /note="R->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 13
FT /note="H->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 16
FT /note="T->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 19
FT /note="S->A: Leads to reduced substrate affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 24
FT /note="Y->A: Leads to low activity and reduced substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 65
FT /note="S->A: Leads to low activity and reduced substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 69
FT /note="R->A: Leads to reduced substrate affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 99
FT /note="E->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 102
FT /note="Y->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 131
FT /note="W->A: Leads to reduced substrate affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 176
FT /note="H->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 178
FT /note="H->A: Leads to low activity and reduced substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT MUTAGEN 181
FT /note="R->A: Leads to reduced substrate affinity."
FT /evidence="ECO:0000269|PubMed:20427268"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3OI7"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3LG2"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3F3K"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 141..164
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3F3K"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3F3K"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:3F3K"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3LG2"
SQ SEQUENCE 271 AA; 31022 MW; FF934DE2F5145C40 CRC64;
MPSLTPRCII VRHGQTEWSK SGQYTGLTDL PLTPYGEGQM LRTGESVFRN NQFLNPDNIT
YIFTSPRLRA RQTVDLVLKP LSDEQRAKIR VVVDDDLREW EYGDYEGMLT REIIELRKSR
GLDKERPWNI WRDGCENGET TQQIGLRLSR AIARIQNLHR KHQSEGRASD IMVFAHGHAL
RYFAAIWFGL GVQKKCETIE EIQNVKSYDD DTVPYVKLES YRHLVDNPCF LLDAGGIGVL
SYAHHNIDEP ALELAGPFVS PPEEESQHGD V
