SitesBLAST
Comparing Synpcc7942_1116 FitnessBrowser__SynE:Synpcc7942_1116 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)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
62% identity, 100% coverage: 1:400/402 of query aligns to 1:393/394 of 1phpA
- active site: R36 (= R40), K197 (= K202), G351 (= G358), G374 (= G381)
- binding adenosine-5'-diphosphate: G195 (= G200), K201 (= K206), G219 (= G224), G220 (= G225), L237 (= L242), N316 (= N321), P318 (= P323), G320 (= G325), V321 (= V326), E323 (= E328), G350 (= G357), D352 (= D359), S353 (= S360)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
62% identity, 100% coverage: 1:400/402 of query aligns to 1:393/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
59% identity, 100% coverage: 1:400/402 of query aligns to 1:393/394 of P40924
- S183 (≠ D188) modified: Phosphoserine
- T299 (≠ S304) 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)
57% identity, 98% coverage: 8:400/402 of query aligns to 5:396/654 of P36204
- R36 (= R40) binding
- R118 (= R122) binding
- R151 (= R155) binding
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
57% identity, 97% coverage: 8:398/402 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R40), K196 (= K202), G353 (= G358), G376 (= G381)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G200), A195 (≠ S201), K196 (= K202), K200 (= K206), G218 (= G224), A219 (≠ G225), N316 (= N321), P318 (= P323), G320 (= G325), V321 (= V326), E323 (= E328), G352 (= G357), G353 (= G358), D354 (= D359), S355 (= S360)
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
53% identity, 98% coverage: 6:398/402 of query aligns to 1:395/398 of 3zlbA
- active site: R36 (= R40), K204 (= K202), G355 (= G358), G378 (= G381)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G200), S203 (= S201), G226 (= G224), G227 (= G225), N320 (= N321), P322 (= P323), G324 (= G325), V325 (= V326), E327 (= E328), G354 (= G357), G355 (= G358), D356 (= D359), S357 (= S360)
- binding magnesium ion: M1 (≠ L6), D8 (vs. gap)
Sites not aligning to the query:
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
50% identity, 98% coverage: 8:400/402 of query aligns to 4:414/415 of 16pkA
- active site: R35 (= R40), K215 (= K202), G372 (= G358), G395 (= G381)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G200), A214 (≠ S201), K219 (= K206), A238 (≠ G225), Y241 (≠ F228), L311 (= L298), P336 (= P323), G338 (= G325), V339 (= V326), E341 (= E328), G393 (= G379), G394 (= G380), G395 (= G381)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
50% identity, 98% coverage: 8:400/402 of query aligns to 4:414/415 of 13pkA
- active site: R35 (= R40), K215 (= K202), G372 (= G358), G395 (= G381)
- binding adenosine-5'-diphosphate: G213 (= G200), A214 (≠ S201), K219 (= K206), L311 (= L298), P336 (= P323), G338 (= G325), V339 (= V326), E341 (= E328), G371 (= G357), D373 (= D359), S374 (= S360)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
50% identity, 98% coverage: 8:400/402 of query aligns to 8:414/416 of P00560
- R22 (= R22) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R40) binding
- R122 (= R122) binding
- R169 (= R155) binding
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
50% identity, 99% coverage: 1:398/402 of query aligns to 1:411/414 of O60101
- Y75 (≠ M75) modified: Phosphotyrosine
- S76 (≠ R76) modified: Phosphoserine
- S143 (≠ E133) modified: Phosphoserine
- S172 (≠ A158) modified: Phosphoserine
- S173 (= S159) modified: Phosphoserine
- S183 (≠ A172) modified: Phosphoserine
- S253 (= S241) modified: Phosphoserine
- S260 (≠ L248) modified: Phosphoserine
- T299 (≠ V286) modified: Phosphothreonine
- S328 (≠ C315) modified: Phosphoserine
- S351 (≠ A338) modified: Phosphoserine
- T373 (≠ S360) modified: Phosphothreonine
- S387 (= S374) modified: Phosphoserine
- S390 (= S377) modified: Phosphoserine
Sites not aligning to the query:
- 412 modified: Phosphoserine
- 413 modified: Phosphoserine
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
50% identity, 98% coverage: 8:400/402 of query aligns to 7:413/415 of 1qpgA
- active site: R38 (= R40), K213 (= K202), G371 (= G358), G394 (= G381)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G224), G236 (= G225), N334 (= N321), P336 (= P323), G338 (= G325), V339 (= V326), F340 (= F327), E341 (= E328), G370 (= G357), G371 (= G358), D372 (= D359), T373 (≠ S360)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
49% identity, 98% coverage: 8:402/402 of query aligns to 8:420/440 of P07378
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
49% identity, 97% coverage: 13:400/402 of query aligns to 21:423/424 of 1ltkC
- active site: R47 (= R40), K223 (= K202), G381 (= G358), G404 (= G381)
- binding adenosine monophosphate: G221 (= G200), A222 (≠ S201), K223 (= K202), G245 (= G224), G246 (= G225), G348 (= G325), V349 (= V326), E351 (= E328), D382 (= D359)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
49% identity, 98% coverage: 8:400/402 of query aligns to 6:404/405 of 2wzcA
- active site: R37 (= R40), K204 (= K202), G362 (= G358), G385 (= G381)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (≠ S201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G357), D363 (= D359), T364 (≠ S360)
- binding tetrafluoroaluminate ion: R37 (= R40), K204 (= K202), K208 (= K206), G361 (= G357), G362 (= G358), G384 (= G380)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
49% identity, 98% coverage: 8:400/402 of query aligns to 6:404/405 of 2wzbA
- active site: R37 (= R40), K204 (= K202), G362 (= G358), G385 (= G381)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (≠ S201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G357), D363 (= D359), T364 (≠ S360)
- binding trifluoromagnesate: K204 (= K202), K208 (= K206), G361 (= G357), G384 (= G380), G385 (= G381)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
49% identity, 98% coverage: 8:400/402 of query aligns to 6:406/407 of 4axxA
- active site: R37 (= R40), K206 (= K202), G364 (= G358), G387 (= G381)
- binding adenosine-5'-diphosphate: G204 (= G200), A205 (≠ S201), K210 (= K206), G228 (= G224), G229 (= G225), N327 (= N321), P329 (= P323), G331 (= G325), V332 (= V326), E334 (= E328), G363 (= G357), G364 (= G358), D365 (= D359), T366 (≠ S360)
- binding beryllium trifluoride ion: K206 (= K202), K210 (= K206), G363 (= G357)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
48% identity, 98% coverage: 8:400/402 of query aligns to 6:407/408 of 2x15A
- active site: R37 (= R40), K207 (= K202), G365 (= G358), G388 (= G381)
- binding adenosine-5'-diphosphate: G205 (= G200), A206 (≠ S201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (= G225), N328 (= N321), P330 (= P323), G332 (= G325), V333 (= V326), E335 (= E328), G364 (= G357), G365 (= G358), D366 (= D359), T367 (≠ S360)
- binding adenosine-5'-triphosphate: G205 (= G200), A206 (≠ S201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (= G225), N328 (= N321), G332 (= G325), V333 (= V326), E335 (= E328), G364 (= G357), G365 (= G358), D366 (= D359), T367 (≠ S360), G387 (= G380), G388 (= G381)
- binding 1,3-bisphosphoglyceric acid: D22 (= D24), N24 (= N26), R37 (= R40), H61 (= H63), R64 (= R66), R121 (= R122), R162 (= R155), K207 (= K202), K211 (= K206), G364 (= G357), G387 (= G380), G388 (= G381)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
48% identity, 98% coverage: 8:400/402 of query aligns to 7:415/416 of 1vjcA
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
46% identity, 98% coverage: 8:400/402 of query aligns to 8:416/417 of P09041
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
49% identity, 98% coverage: 8:400/402 of query aligns to 6:404/405 of 2wzdA
- active site: R37 (= R40), K204 (= K202), G362 (= G358), G385 (= G381)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (≠ S201), K204 (= K202), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G357), D363 (= D359), T364 (≠ S360)
- binding aluminum fluoride: R37 (= R40), K204 (= K202), G361 (= G357), G362 (= G358), G384 (= G380)
Query Sequence
>Synpcc7942_1116 FitnessBrowser__SynE:Synpcc7942_1116
VSKRTLASLTAADLEGKRVLVRVDFNVPLDGNGKITDDTRIRAALPTIRYLSESGAKVIL
VSHFGRPKGKPVESMRLTPVAERLSELLGRPVVKTTDAVGAGAEAQVAATSNGQVVLLEN
VRFHAEEEANDAEFAKALASLADIYVNDAFGAAHRAHASTAGVTEYLSPCVAGYLLEKEL
QYLQAAIDNPQRPLAAIVGGSKVSSKIGVIETLLDKCDKLLIGGGMIFTFYKAQGLSVGG
SLVEEDKLDLARSLMAKAQEKGVQLLLPVDVVVADKFAPDANAKTVAIDAIPDGWMGLDI
GPESVKQFEEALADCRSVIWNGPMGVFEFDQFAVGTEAIARSLAGLTRKGATTIIGGGDS
VAAVEKVGVASEMSHISTGGGASLELLEGKVLPGVAALDDAA
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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