SitesBLAST
Comparing Dsui_1557 FitnessBrowser__PS:Dsui_1557 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)
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
60% identity, 99% coverage: 1:392/394 of query aligns to 1:385/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L85) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
60% identity, 99% coverage: 2:392/394 of query aligns to 1:384/386 of 1zmrA
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
55% identity, 99% coverage: 1:392/394 of query aligns to 1:390/392 of 4feyA
- active site: R36 (= R37), K193 (= K195), G346 (= G348), G369 (= G371)
- binding adenosine-5'-diphosphate: G191 (= G193), S192 (= S194), K197 (= K199), G215 (= G217), G316 (= G318), V317 (= V319), E319 (= E321), D347 (= D349)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
55% identity, 99% coverage: 4:392/394 of query aligns to 3:388/389 of 4ng4B
- active site: R35 (= R37), K191 (= K195), G344 (= G348), G367 (= G371)
- binding adenosine-5'-diphosphate: G189 (= G193), K195 (= K199), G213 (= G217), I286 (= I290), N310 (= N314), G311 (= G315), P312 (= P316), V315 (= V319), E317 (= E321), G343 (= G347), D345 (= D349), T346 (= T350)
- binding magnesium ion: D288 (= D292), G314 (= G318), F321 (= F325), S322 (≠ G326), T325 (= T329)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
48% identity, 99% coverage: 1:391/394 of query aligns to 1:394/394 of P40924
- S183 (≠ E181) modified: Phosphoserine
- T299 (= T297) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
49% identity, 99% coverage: 1:391/394 of query aligns to 1:394/394 of 1phpA
- active site: R36 (= R37), K197 (= K195), G351 (= G348), G374 (= G371)
- binding adenosine-5'-diphosphate: G195 (= G193), K201 (= K199), G219 (= G217), G220 (= G218), L237 (= L235), N316 (= N314), P318 (= P316), G320 (= G318), V321 (= V319), E323 (= E321), G350 (= G347), D352 (= D349), S353 (≠ T350)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
49% identity, 99% coverage: 1:391/394 of query aligns to 1:394/394 of P18912
P36204 Bifunctional PGK/TIM; EC 2.7.2.3; EC 5.3.1.1 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
44% identity, 98% coverage: 1:385/394 of query aligns to 1:391/654 of P36204
- R36 (= R37) binding substrate
- R118 (= R115) binding substrate
- R151 (= R148) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
45% identity, 97% coverage: 4:385/394 of query aligns to 3:390/398 of 1vpeA
- active site: R35 (= R37), K196 (= K195), G353 (= G348), G376 (= G371)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G193), A195 (≠ S194), K196 (= K195), K200 (= K199), G218 (= G217), A219 (≠ G218), N316 (= N314), P318 (= P316), G320 (= G318), V321 (= V319), E323 (= E321), G352 (= G347), G353 (= G348), D354 (= D349), S355 (≠ T350)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
42% identity, 98% coverage: 4:391/394 of query aligns to 7:415/416 of P00560
- R22 (= R19) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- N26 (= N23) binding (2R)-3-phosphoglycerate
- R39 (= R37) binding (2R)-3-phosphoglycerate
- R122 (= R115) binding (2R)-3-phosphoglycerate
- A213 (≠ S194) binding ATP
- K214 (= K195) binding ATP
- L312 (= L291) binding ATP
- N335 (= N314) binding covalent
- E342 (= E321) binding ATP
- G371 (= G347) binding (2R)-3-phosphoglycerate
- D373 (= D349) binding covalent; binding Mg(2+)
- G394 (= G370) binding (2R)-3-phosphoglycerate
- G395 (= G371) binding (2R)-3-phosphoglycerate
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
41% identity, 99% coverage: 2:390/394 of query aligns to 3:404/405 of 2wzcA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (≠ S194), K204 (= K195), K208 (= K199), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding tetrafluoroaluminate ion: R37 (= R37), K204 (= K195), K208 (= K199), G361 (= G347), G362 (= G348), G384 (= G370)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
41% identity, 99% coverage: 2:390/394 of query aligns to 3:404/405 of 2wzbA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (≠ S194), K204 (= K195), K208 (= K199), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding trifluoromagnesate: K204 (= K195), K208 (= K199), G361 (= G347), G384 (= G370), G385 (= G371)
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
41% identity, 98% coverage: 4:391/394 of query aligns to 6:414/415 of 3pgkA
- active site: R38 (= R37), K213 (= K195), G371 (= G348), G394 (= G371)
- binding adenosine-5'-triphosphate: G211 (= G193), A212 (≠ S194), K213 (= K195), F289 (≠ L270), L311 (= L291), N334 (= N314), G335 (= G315), P336 (= P316), G338 (= G318), V339 (= V319), D372 (= D349)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
41% identity, 98% coverage: 4:391/394 of query aligns to 6:414/415 of 1qpgA
- active site: R38 (= R37), K213 (= K195), G371 (= G348), G394 (= G371)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G217), G236 (= G218), N334 (= N314), P336 (= P316), G338 (= G318), V339 (= V319), F340 (= F320), E341 (= E321), G370 (= G347), G371 (= G348), D372 (= D349), T373 (= T350)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
40% identity, 99% coverage: 2:390/394 of query aligns to 4:415/416 of 1kf0A
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
40% identity, 99% coverage: 2:390/394 of query aligns to 3:404/405 of 2wzdA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (≠ S194), K204 (= K195), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding aluminum fluoride: R37 (= R37), K204 (= K195), G361 (= G347), G362 (= G348), G384 (= G370)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride (see paper)
40% identity, 99% coverage: 2:390/394 of query aligns to 3:406/407 of 4axxA
- active site: R37 (= R37), K206 (= K195), G364 (= G348), G387 (= G371)
- binding adenosine-5'-diphosphate: G204 (= G193), A205 (≠ S194), K210 (= K199), G228 (= G217), G229 (= G218), N327 (= N314), P329 (= P316), G331 (= G318), V332 (= V319), E334 (= E321), G363 (= G347), G364 (= G348), D365 (= D349), T366 (= T350)
- binding beryllium trifluoride ion: K206 (= K195), K210 (= K199), G363 (= G347)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
40% identity, 99% coverage: 2:390/394 of query aligns to 3:407/408 of 2x15A
- active site: R37 (= R37), K207 (= K195), G365 (= G348), G388 (= G371)
- binding adenosine-5'-diphosphate: G205 (= G193), A206 (≠ S194), K207 (= K195), K211 (= K199), G229 (= G217), G230 (= G218), N328 (= N314), P330 (= P316), G332 (= G318), V333 (= V319), E335 (= E321), G364 (= G347), G365 (= G348), D366 (= D349), T367 (= T350)
- binding adenosine-5'-triphosphate: G205 (= G193), A206 (≠ S194), K207 (= K195), K211 (= K199), G229 (= G217), G230 (= G218), N328 (= N314), G332 (= G318), V333 (= V319), E335 (= E321), G364 (= G347), G365 (= G348), D366 (= D349), T367 (= T350), G387 (= G370), G388 (= G371)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R37), H61 (= H60), R64 (= R63), R121 (= R115), R162 (= R148), K207 (= K195), K211 (= K199), G364 (= G347), G387 (= G370), G388 (= G371)
P00558 Phosphoglycerate kinase 1; Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2; EC 2.7.11.1; EC 2.7.2.3 from Homo sapiens (Human) (see 17 papers)
39% identity, 99% coverage: 2:390/394 of query aligns to 5:416/417 of P00558
- V23 (≠ A20) binding (2R)-3-phosphoglycerate
- F25 (≠ L22) binding (2R)-3-phosphoglycerate
- Q38 (≠ T36) binding (2R)-3-phosphoglycerate
- QRIKAA 38:43 (≠ TRIRAS 36:41) Mitochondrial targeting region exposed following cis-trans isomerization by PIN1 and recognized by the TOM complex for mitochondrial translocation of the protein
- S62 (= S59) binding (2R)-3-phosphoglycerate
- G65 (= G62) binding (2R)-3-phosphoglycerate
- L88 (= L85) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ D94) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- L122 (≠ C114) binding (2R)-3-phosphoglycerate
- K131 (vs. gap) modified: N6-malonyllysine; alternate
- G158 (≠ C135) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D141) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- H170 (= H147) binding (2R)-3-phosphoglycerate
- K191 (≠ G170) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- S203 (≠ N182) modified: Phosphoserine; by MAPK1
- R206 (= R185) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- G214 (= G193) binding ADP; binding CDP
- A215 (≠ S194) binding Mg(2+)
- K216 (= K195) modified: N6-(2-hydroxyisobutyryl)lysine
- A218 (≠ S197) binding Mg(2+)
- D219 (≠ T198) binding CDP; binding Mg(2+)
- K220 (= K199) modified: N6-(2-hydroxyisobutyryl)lysine
- G238 (= G217) binding ADP; binding CDP
- E252 (≠ P230) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A244) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ N246) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D263) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- D315 (= D292) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I293) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (= K300) modified: N6-(2-hydroxyisobutyryl)lysine
- G338 (= G315) binding CDP
- V340 (= V317) binding CDP
- F343 (= F320) binding ADP; binding CDP
- T352 (= T329) to N: in dbSNP:rs137852530
- T378 (≠ A352) mutation to P: Loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
39% identity, 99% coverage: 2:390/394 of query aligns to 3:414/414 of 2y3iA
- active site: R37 (= R37), K214 (= K195), G372 (= G348), G395 (= G371)
- binding tetrafluoroaluminate ion: K214 (= K195), G371 (= G347), G372 (= G348), G394 (= G370)
- binding l-adenosine-5'-diphosphate: G212 (= G193), A213 (≠ S194), F290 (≠ L270), N335 (= N314), G339 (= G318), V340 (= V319), E342 (= E321), G371 (= G347), G372 (= G348), D373 (= D349), T374 (= T350)
Query Sequence
>Dsui_1557 FitnessBrowser__PS:Dsui_1557
MNVLKLADLDVKGKRVFIRADLNVPQDETGRITDDTRIRASVPAIQMALEKGAAVMVTSH
LGRPTEGEMKPEDSLAPIAHRLAELLGRKVPVIDNWVDGGFEVKPGDVVLLENCRVNKGE
KKNNDELAQKLAKLCDVYVNDAFGTAHRAEATTHGIAKYAPVACAGPLLGAELDALGRAL
ENPKRPLVAIVAGSKVSTKLTILKSLAGKVDQLIVGGGIANTFMVADDLPIGESLAELDL
VEEARNIMDMMDERGASVPIPEDVVVANELSVHARANRVDANDVQPDDMILDIGPKTSAK
LASIIAHAGTIVWNGPVGVFEFDQFGGGTKMLAAAIAHSPAFSIAGGGDTLAAIAKYGIE
KQIDYISTGGGAFLEFLEGKKLPAVEVLEQRANG
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