SitesBLAST
Comparing GFF329 FitnessBrowser__psRCH2:GFF329 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)
71% identity, 100% coverage: 1:385/386 of query aligns to 1:385/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ A84) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
71% identity, 99% coverage: 2:385/386 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
61% identity, 100% coverage: 1:385/386 of query aligns to 1:390/392 of 4feyA
- active site: R36 (= R36), K193 (= K193), G346 (= G341), G369 (= G364)
- binding adenosine-5'-diphosphate: G191 (= G191), S192 (= S192), K197 (= K197), G215 (= G215), G316 (= G311), V317 (= V312), E319 (= E314), D347 (= D342)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
59% identity, 99% coverage: 4:385/386 of query aligns to 3:388/389 of 4ng4B
- active site: R35 (= R36), K191 (= K193), G344 (= G341), G367 (= G364)
- binding adenosine-5'-diphosphate: G189 (= G191), K195 (= K197), G213 (= G215), I286 (= I283), N310 (= N307), G311 (= G308), P312 (= P309), V315 (= V312), E317 (= E314), G343 (= G340), D345 (= D342), T346 (= T343)
- binding magnesium ion: D288 (= D285), G314 (= G311), F321 (= F318), S322 (≠ G319), T325 (= T322)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
47% identity, 99% coverage: 1:384/386 of query aligns to 1:394/394 of P40924
- S183 (≠ K179) modified: Phosphoserine
- T299 (= T290) modified: Phosphothreonine
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)
47% identity, 98% coverage: 1:378/386 of query aligns to 1:391/654 of P36204
- R36 (= R36) binding substrate
- R118 (= R113) binding substrate
- R151 (= R146) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
48% identity, 97% coverage: 5:378/386 of query aligns to 2:390/398 of 1vpeA
- active site: R35 (= R36), K196 (= K193), G353 (= G341), G376 (= G364)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G191), A195 (≠ S192), K196 (= K193), K200 (= K197), G218 (= G215), A219 (≠ G216), N316 (= N307), P318 (= P309), G320 (= G311), V321 (= V312), E323 (= E314), G352 (= G340), G353 (= G341), D354 (= D342), S355 (≠ T343)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
46% identity, 99% coverage: 1:384/386 of query aligns to 1:394/394 of 1phpA
- active site: R36 (= R36), K197 (= K193), G351 (= G341), G374 (= G364)
- binding adenosine-5'-diphosphate: G195 (= G191), K201 (= K197), G219 (= G215), G220 (= G216), L237 (= L233), N316 (= N307), P318 (= P309), G320 (= G311), V321 (= V312), E323 (= E314), G350 (= G340), D352 (= D342), S353 (≠ T343)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
46% identity, 99% coverage: 1:384/386 of query aligns to 1:394/394 of P18912
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
43% identity, 99% coverage: 1:384/386 of query aligns to 1:398/398 of 3zlbA
- active site: R36 (= R36), K204 (= K193), G355 (= G341), G378 (= G364)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G191), S203 (= S192), G226 (= G215), G227 (= G216), N320 (= N307), P322 (= P309), G324 (= G311), V325 (= V312), E327 (= E314), G354 (= G340), G355 (= G341), D356 (= D342), S357 (≠ T343)
- binding magnesium ion: M1 (= M1), D8 (= D8), K398 (≠ R384)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
40% identity, 98% coverage: 6:385/386 of query aligns to 9:420/440 of P07378
- DFN 24:26 (≠ DLN 21:23) binding substrate
- R39 (= R36) binding substrate
- HLGR 62:65 (= HLGR 59:62) binding substrate
- R135 (= R113) binding substrate
- R172 (= R146) binding substrate
- K223 (= K197) binding ATP
- N338 (= N307) binding ATP
- E345 (= E314) binding ATP
- GGDS 375:378 (≠ GGDT 340:343) binding ATP
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
40% identity, 98% coverage: 6:384/386 of query aligns to 5:415/415 of 16pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G341), G395 (= G364)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G191), A214 (≠ S192), K219 (= K197), A238 (≠ G216), Y241 (≠ N219), L311 (= L284), P336 (= P309), G338 (= G311), V339 (= V312), E341 (= E314), G393 (= G362), G394 (= G363), G395 (= G364)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
40% identity, 98% coverage: 6:384/386 of query aligns to 5:415/415 of 13pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G341), G395 (= G364)
- binding adenosine-5'-diphosphate: G213 (= G191), A214 (≠ S192), K219 (= K197), L311 (= L284), P336 (= P309), G338 (= G311), V339 (= V312), E341 (= E314), G371 (= G340), D373 (= D342), S374 (≠ T343)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
43% identity, 99% coverage: 2:384/386 of query aligns to 5:414/414 of O60101
- Y75 (≠ D72) modified: Phosphotyrosine
- S76 (= S73) modified: Phosphoserine
- S143 (≠ L125) modified: Phosphoserine
- S172 (≠ G149) modified: Phosphoserine
- S173 (= S150) modified: Phosphoserine
- S183 (≠ A161) modified: Phosphoserine
- S253 (= S232) modified: Phosphoserine
- S260 (≠ L239) modified: Phosphoserine
- T299 (≠ K272) modified: Phosphothreonine
- S328 (= S301) modified: Phosphoserine
- S351 (≠ V324) modified: Phosphoserine
- T373 (= T343) modified: Phosphothreonine
- S387 (= S357) modified: Phosphoserine
- S390 (= S360) modified: Phosphoserine
- S412 (≠ E382) modified: Phosphoserine
- S413 (≠ Q383) modified: Phosphoserine
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
40% identity, 99% coverage: 4:384/386 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.
- R39 (= R36) binding substrate
- R122 (= R113) binding substrate
- R169 (= R146) binding substrate
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
40% identity, 99% coverage: 4:384/386 of query aligns to 6:414/415 of 1qpgA
- active site: R38 (= R36), K213 (= K193), G371 (= G341), G394 (= G364)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G215), G236 (= G216), N334 (= N307), P336 (= P309), G338 (= G311), V339 (= V312), F340 (= F313), E341 (= E314), G370 (= G340), G371 (= G341), D372 (= D342), T373 (= T343)
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
40% identity, 99% coverage: 4:384/386 of query aligns to 6:414/415 of 3pgkA
- active site: R38 (= R36), K213 (= K193), G371 (= G341), G394 (= G364)
- binding adenosine-5'-triphosphate: G211 (= G191), A212 (≠ S192), K213 (= K193), F289 (= F263), L311 (= L284), N334 (= N307), G335 (= G308), P336 (= P309), G338 (= G311), V339 (= V312), D372 (= D342)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
38% identity, 98% coverage: 4:383/386 of query aligns to 5:404/405 of 2wzcA
- active site: R37 (= R36), K204 (= K193), G362 (= G341), G385 (= G364)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N307), P327 (= P309), G329 (= G311), V330 (= V312), E332 (= E314), G361 (= G340), D363 (= D342), T364 (= T343)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K193), K208 (= K197), G361 (= G340), G362 (= G341), G384 (= G363)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
38% identity, 98% coverage: 4:383/386 of query aligns to 5:404/405 of 2wzbA
- active site: R37 (= R36), K204 (= K193), G362 (= G341), G385 (= G364)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N307), P327 (= P309), G329 (= G311), V330 (= V312), E332 (= E314), G361 (= G340), D363 (= D342), T364 (= T343)
- binding trifluoromagnesate: K204 (= K193), K208 (= K197), G361 (= G340), G384 (= G363), G385 (= G364)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
38% identity, 98% coverage: 4:383/386 of query aligns to 5:404/405 of 2wzdA
- active site: R37 (= R36), K204 (= K193), G362 (= G341), G385 (= G364)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), G226 (= G215), G227 (= G216), N325 (= N307), P327 (= P309), G329 (= G311), V330 (= V312), E332 (= E314), G361 (= G340), D363 (= D342), T364 (= T343)
- binding aluminum fluoride: R37 (= R36), K204 (= K193), G361 (= G340), G362 (= G341), G384 (= G363)
Query Sequence
>GFF329 FitnessBrowser__psRCH2:GFF329
MTVLKMTDLDLQGKRVLIREDLNVPVKDGAVKSDARILASLPTIKLALEKGAAVLVCSHL
GRPEEGVYSEEDSLKPVADYLSKALGREVPLIKDYLDGVEVQPGELVLLENVRFNKGEKK
NTDELAQKYAALCDVFVMDAFGTAHRAQGSTHGVAKFAKVACAGPLLAAELDALGKALKT
PAKPMVAIVAGSKVSTKLDVLTSLADVCDQLIVGGGIANTFLAAAGYNVGKSLHEADLLD
TAKAIAAKVAVPLPVDVVVAKEFAETADATVKAIADVADDDMILDIGPKTAAMFGEMLKS
SQTILWNGPVGVFEFDQFGNGTKVLAQAIAQSPAFSIAGGGDTLAAIDKYGVAEQISYIS
TGGGAFLEFVEGKVLPAVEVLEQRAG
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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