SitesBLAST
Comparing WP_011320358.1 NCBI__GCF_000204075.1:WP_011320358.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
34% identity, 46% coverage: 232:438/449 of query aligns to 2:201/207 of 4ij6A
- active site: R8 (= R238), A9 (≠ H239), N15 (= N245), R58 (= R288), E82 (= E313), H150 (= H384)
- binding phosphoserine: R8 (= R238), Q21 (= Q251), R58 (= R288), E82 (= E313), H85 (= H316), H150 (= H384), T151 (≠ D385)
1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
36% identity, 43% coverage: 234:427/449 of query aligns to 4:194/207 of 1h2fA
- active site: R8 (= R238), H9 (= H239), N15 (= N245), R58 (= R288), E82 (= E313), H150 (= H384)
- binding phosphate ion: G142 (≠ R376), E143 (≠ Q377)
- binding trivanadate: R8 (= R238), H9 (= H239), N15 (= N245), Q21 (= Q251), R58 (= R288), E82 (= E313), H150 (= H384), G151 (≠ D385), V152 (≠ A386)
Sites not aligning to the query:
1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
36% identity, 43% coverage: 234:427/449 of query aligns to 4:194/207 of 1h2eA
6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
29% identity, 48% coverage: 1:217/449 of query aligns to 1:195/196 of 6m1xC
5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
29% identity, 48% coverage: 1:217/449 of query aligns to 1:195/198 of 5zr2C
Q9NQ88 Fructose-2,6-bisphosphatase TIGAR; TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; EC 3.1.3.46 from Homo sapiens (Human) (see 4 papers)
34% identity, 32% coverage: 234:377/449 of query aligns to 6:149/270 of Q9NQ88
- H11 (= H239) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.
- E102 (= E326) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.
Sites not aligning to the query:
- 198 H→A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.
- 258:261 mutation Missing: Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.
Q7ZVE3 Fructose-2,6-bisphosphatase TIGAR B; TP53-induced glycolysis and apoptosis regulator B; EC 3.1.3.46 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
36% identity, 31% coverage: 234:373/449 of query aligns to 6:145/257 of Q7ZVE3
- H11 (= H239) active site, Tele-phosphohistidine intermediate
1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
29% identity, 37% coverage: 233:398/449 of query aligns to 2:195/240 of 1qhfA
- active site: H8 (= H239), R59 (= R288), E86 (= E313), H181 (= H384)
- binding 3-phosphoglyceric acid: R7 (= R238), H8 (= H239), G9 (= G240), Q10 (≠ E241), S11 (≠ T242), N14 (= N245), T20 (≠ Q251), R59 (= R288)
Sites not aligning to the query:
P00950 Phosphoglycerate mutase 1; PGAM 1; BPG-dependent PGAM 1; MPGM 1; Phosphoglyceromutase 1; EC 5.4.2.11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 7 papers)
29% identity, 37% coverage: 233:398/449 of query aligns to 3:196/247 of P00950
- 8:15 (vs. 238:245, 75% identical) binding
- H9 (= H239) active site, Tele-phosphohistidine intermediate
- TG 21:22 (≠ QG 251:252) binding
- R60 (= R288) binding
- ERHY 87:90 (≠ EISH 313:316) binding
- K98 (≠ E324) binding
- RR 114:115 (vs. gap) binding
- K169 (≠ T370) mutation to P: Causes dissociation of the homotetramer to dimers at low concentrations.
- H182 (= H384) mutation to A: Reduces kcat of the mutase reaction 10000-fold.
- GN 183:184 (≠ DA 385:386) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
29% identity, 37% coverage: 233:398/449 of query aligns to 2:195/234 of 5pgmE
Sites not aligning to the query:
1bq4A Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate (see paper)
29% identity, 37% coverage: 233:398/449 of query aligns to 2:195/234 of 1bq4A
Sites not aligning to the query:
1bq3A Saccharomyces cerevisiae phosphoglycerate mutase in complex with inositol hexakisphosphate (see paper)
29% identity, 37% coverage: 233:398/449 of query aligns to 2:195/234 of 1bq3A
- active site: H8 (= H239), R59 (= R288), E86 (= E313), H181 (= H384)
- binding inositol hexakisphosphate: R7 (= R238), S11 (≠ T242), N14 (= N245), L18 (≠ R249), F19 (= F250), T20 (≠ Q251), Y89 (≠ H316), K97 (≠ E324), R113 (vs. gap)
P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
36% identity, 24% coverage: 233:339/449 of query aligns to 5:110/223 of P9WIC7
- R10 (= R238) mutation to A: Loss of phosphatase activity.
- H11 (= H239) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
- N17 (= N245) mutation to A: About 5% of wild-type phosphatase activity.
- K47 (≠ N275) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- R60 (= R288) mutation to A: Loss of phosphatase activity.
Sites not aligning to the query:
- 159 H→A: About 5% of wild-type phosphatase activity.
- 209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.
4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
36% identity, 24% coverage: 233:339/449 of query aligns to 4:109/217 of 4pzaB
Sites not aligning to the query:
4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
36% identity, 24% coverage: 233:339/449 of query aligns to 3:108/209 of 4qihA
Sites not aligning to the query:
P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 24% coverage: 222:329/449 of query aligns to 1:115/271 of P36136
- R12 (= R238) binding ; mutation to A: Impairs catalytic activity.
- H13 (= H239) active site, Tele-phosphohistidine intermediate; mutation to A: Impairs catalytic activity.
- T16 (= T242) mutation to A: Impairs catalytic activity.
- S19 (≠ N245) mutation to A: Leads to reduced substrate affinity.
- Y24 (≠ F250) mutation to A: Leads to low activity and reduced substrate affinity.
- YT 24:25 (≠ FQ 250:251) binding
- S65 (= S284) mutation to A: Leads to low activity and reduced substrate affinity.
- R69 (= R288) binding ; mutation to A: Leads to reduced substrate affinity.
- E99 (= E313) mutation to A: Impairs catalytic activity.
- EWEY 99:102 (≠ EISH 313:316) binding
- Y102 (≠ H316) mutation to A: Impairs catalytic activity.
Sites not aligning to the query:
- 131 W→A: Leads to reduced substrate affinity.
- 176 H→A: Impairs catalytic activity.
- 178 H→A: Leads to low activity and reduced substrate affinity.
- 181 binding ; R→A: Leads to reduced substrate affinity.
- 244 binding
P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 37% coverage: 234:401/449 of query aligns to 10:180/211 of P36623
- T37 (≠ N261) modified: Phosphothreonine
- S62 (= S284) modified: Phosphoserine
- Y96 (≠ H316) modified: Phosphotyrosine
- S166 (≠ T387) modified: Phosphoserine
3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
32% identity, 22% coverage: 233:329/449 of query aligns to 5:113/269 of 3lg2A
Sites not aligning to the query:
P62707 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Escherichia coli (strain K12) (see 6 papers)
34% identity, 24% coverage: 232:339/449 of query aligns to 4:116/250 of P62707
- 10:17 (vs. 238:245, 75% identical) binding
- H11 (= H239) active site, Tele-phosphohistidine intermediate
- K18 (≠ R246) modified: N6-acetyllysine
- TG 23:24 (≠ QG 251:252) binding
- E89 (= E313) active site, Proton donor/acceptor
- ERHY 89:92 (≠ EISH 313:316) binding
- K100 (≠ E324) binding ; modified: N6-acetyllysine
- K106 (≠ E330) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 116:117 binding
- 184 Transition state stabilizer
- 185:186 binding
1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
34% identity, 24% coverage: 232:339/449 of query aligns to 2:114/239 of 1e59A
Sites not aligning to the query:
Query Sequence
>WP_011320358.1 NCBI__GCF_000204075.1:WP_011320358.1
MTRVIIVRHGQSTYNIERRIQGRADVSTLTDRGRSDASKVGKALTNISFNAIYSSPLQRA
KQTAEIIHGELANEAVQSADVQISELLREIDLPLWEKMLTSEVKQKFPEDYRIWHENPQE
LQMLVNDNGVTREHFPVLSLYEQARQFWQNILPHHRGETILIVGHNGINRALISTALGIH
PSRYHSIQQSNCGISVLNFAGGLGDPVQLESMNQTQHTGETLPSLRPGHQGVRLLLVRHG
ETEWNRQTRFQGQIDVPLNDNGRQQAQKAGVFLQNVAIDFAVSSSMLRPKETAEIILRHH
PSINLELQDGLREISHGLWEGKLEAEIEEEFPGELERWRTIPGQVQMPEGENLQQVWERS
TEAWQNIVQTALDNQRQTGLIVAHDATNKTLLCHILGLPTDNFWNFRQGNGAVSVIDYPS
GLNGVPVLQAMNITTHLGGVLDKTAAGAL
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory