SitesBLAST
Comparing BWI76_RS04200 FitnessBrowser__Koxy:BWI76_RS04200 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
31% identity, 94% coverage: 4:206/215 of query aligns to 4:202/207 of 1h2fA
- active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E82 (= E82), H150 (= H150)
- binding phosphate ion: G142 (= G142), E143 (≠ S143)
- binding trivanadate: R8 (= R8), H9 (= H9), N15 (= N15), Q21 (= Q21), R58 (= R58), E82 (= E82), H150 (= H150), G151 (= G151), V152 (≠ M152)
Sites not aligning to the query:
1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
31% identity, 94% coverage: 4:206/215 of query aligns to 4:202/207 of 1h2eA
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)
37% identity, 57% coverage: 6:128/215 of query aligns to 8:131/270 of Q9NQ88
- H11 (= H9) 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 (≠ S95) 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)
32% identity, 69% coverage: 6:154/215 of query aligns to 8:151/257 of Q7ZVE3
- H11 (= H9) active site, Tele-phosphohistidine intermediate
1tipA The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase (see paper)
32% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1tipA
- active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
- binding 6-O-phosphono-beta-D-fructofuranose: I20 (= I20), Y89 (≠ I93), R103 (= R104), K107 (≠ T111), Y118 (≠ M122), R148 (≠ G155)
1c81A Michaelis complex of fructose-2,6-bisphosphatase
32% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c81A
- active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
- binding 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol: R8 (= R8), H9 (= H9), N15 (= N15), I20 (= I20), R58 (= R58), E78 (= E82), H143 (= H150), Q144 (≠ G151), R148 (≠ G155)
1c80A Regulatory complex of fructose-2,6-bisphosphatase
32% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c80A
- active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
- binding guanosine-5'-triphosphate: I20 (= I20), E78 (= E82), I79 (≠ L83), Y89 (≠ I93), F100 (≠ E101), R103 (= R104), Y112 (≠ I116), Y118 (≠ M122), Q144 (≠ G151), A145 (≠ M152), R148 (≠ G155)
1c7zA Regulatory complex of fructose-2,6-bisphosphatase
32% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c7zA
- active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
- binding glyceraldehyde-3-phosphate: Y89 (≠ I93), R103 (= R104), K107 (≠ T111), Y118 (≠ M122), Q144 (≠ G151), A145 (≠ M152), R148 (≠ G155)
1k6mA Crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase (see paper)
30% identity, 74% coverage: 4:162/215 of query aligns to 215:366/432 of 1k6mA
Sites not aligning to the query:
- binding phosphothiophosphoric acid-adenylate ester: 13, 14, 15, 16, 17, 18, 92, 120, 131, 134, 135, 136, 184, 210
1fbtA The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase (see paper)
32% identity, 74% coverage: 4:162/215 of query aligns to 3:154/190 of 1fbtA
- active site: R7 (= R8), H8 (= H9), N14 (= N15), R57 (= R58), E77 (= E82), H142 (= H150)
- binding phosphate ion: R7 (= R8), H8 (= H9), R57 (= R58), E77 (= E82), H142 (= H150), Q143 (≠ G151)
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, 74% coverage: 6:164/215 of query aligns to 12:177/211 of P36623
- T37 (≠ H31) modified: Phosphothreonine
- S62 (= S54) modified: Phosphoserine
- Y96 (≠ M85) modified: Phosphotyrosine
- S166 (≠ A153) modified: Phosphoserine
P07953 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; 6PF-2-K/Fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/Fru-2,6-P2ase liver isozyme; EC 2.7.1.105; EC 3.1.3.46 from Rattus norvegicus (Rat) (see 3 papers)
32% identity, 74% coverage: 4:162/215 of query aligns to 254:405/471 of P07953
- H259 (= H9) active site, Tele-phosphohistidine intermediate
- G271 (≠ Q21) binding
- E328 (= E82) active site, Proton donor/acceptor
- Y339 (≠ I93) binding
- FALR 350:353 (≠ EGWR 101:104) binding
- R353 (= R104) binding
- K357 (≠ T111) binding
- Y368 (≠ M122) binding
- Q394 (≠ G151) binding
- QAVMR 394:398 (≠ GMALG 151:155) binding
- R398 (≠ G155) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 33 modified: Phosphoserine; by PKA
P16118 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; 6PF-2-K/Fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/Fru-2,6-P2ase liver isozyme; EC 2.7.1.105; EC 3.1.3.46 from Homo sapiens (Human) (see paper)
30% identity, 74% coverage: 4:162/215 of query aligns to 254:405/471 of P16118
Sites not aligning to the query:
- 49:57 binding
- 170:175 binding
- 430 binding
3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
30% identity, 76% coverage: 1:164/215 of query aligns to 1:196/230 of 3fdzA
- active site: H9 (= H9), R60 (= R58), E87 (= E82), H182 (= H150)
- binding (2R)-2,3-diphosphoglyceric acid: R8 (= R8), H9 (= H9), N15 (= N15), T21 (≠ Q21), R60 (= R58), E87 (= E82), Y90 (≠ M85), K98 (= K90), R114 (= R104), R115 (= R105), H182 (= H150), G183 (= G151), N184 (≠ M152)
3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
30% identity, 76% coverage: 1:164/215 of query aligns to 1:196/229 of 3gp3A
- active site: H9 (= H9), R60 (= R58), E87 (= E82), H182 (= H150)
- binding phosphite ion: R8 (= R8), H9 (= H9), R60 (= R58), E87 (= E82), H182 (= H150), G183 (= G151)
- binding phosphoserine: T21 (≠ Q21), E87 (= E82), Y90 (≠ M85), K98 (= K90), R114 (= R104), R115 (= R105), N184 (≠ M152)
3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
30% identity, 76% coverage: 1:164/215 of query aligns to 1:196/248 of 3gp5A
4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
27% identity, 76% coverage: 1:164/215 of query aligns to 1:164/207 of 4ij6A
- active site: R8 (= R8), A9 (≠ H9), N15 (= N15), R58 (= R58), E82 (= E82), H150 (= H150)
- binding phosphoserine: R8 (= R8), Q21 (= Q21), R58 (= R58), E82 (= E82), H85 (≠ M85), H150 (= H150), T151 (≠ G151)
Q3JWH7 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Burkholderia pseudomallei (strain 1710b) (see paper)
30% identity, 76% coverage: 1:164/215 of query aligns to 1:196/249 of Q3JWH7
- 8:15 (vs. 8:15, 75% identical) binding
- H9 (= H9) active site, Tele-phosphohistidine intermediate
- TG 21:22 (≠ QG 21:22) binding
- R60 (= R58) binding
- ERHY 87:90 (≠ ELDM 82:85) binding
- K98 (= K90) binding
- RR 114:115 (= RR 104:105) binding
- GN 183:184 (≠ GM 151:152) binding
Q9HIJ2 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (see paper)
25% identity, 88% coverage: 6:195/215 of query aligns to 6:187/200 of Q9HIJ2
- H9 (= H9) mutation to A: Loss of activity.
5htkA Human heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
31% identity, 91% coverage: 4:198/215 of query aligns to 222:404/425 of 5htkA
- active site: R226 (= R8), H227 (= H9), N233 (= N15), R276 (= R58), E296 (= E82), H361 (= H150)
- binding adenosine-5'-triphosphate: A397 (= A191), Y398 (≠ S192)
- binding 6-O-phosphono-beta-D-fructofuranose: H227 (= H9), I238 (= I20), G239 (≠ Q21), E296 (= E82), Y307 (vs. gap), R321 (= R104), K325 (≠ T111), Y336 (≠ M122), Q362 (≠ G151), R366 (≠ G155)
Sites not aligning to the query:
- binding adenosine-5'-triphosphate: 17, 18, 19, 20, 21, 22, 140, 144, 145, 146
- binding citrate anion: 48, 61, 72, 99, 100, 167
Query Sequence
>BWI76_RS04200 FitnessBrowser__Koxy:BWI76_RS04200
MLQVYLVRHGETQWNAERRIQGQSDSPLTAHGERQAWQVGERARTLGITHIIASDLGRTR
RTAEIIAEACGCSVVTDSRLRELDMGVLEKRHIDSLSEEEEGWRRQLVNGTPDGRIPQGE
SMQELSERMHAALTSCLELPAGSRPLLVSHGMALGCLVSTILGLPAYAERRLRLRNCSIS
RVDYQQSPWLASGWVVETAGDVSHLDAPAMDELQR
Or try a new SitesBLAST search
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