SitesBLAST
Comparing WP_014026822.1 NCBI__GCF_000223395.1:WP_014026822.1 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)
O58965 Phosphoglycerate kinase; EC 2.7.2.3 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
43% identity, 97% coverage: 11:420/423 of query aligns to 4:405/410 of O58965
- R34 (= R48) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
37% identity, 94% coverage: 21:418/423 of query aligns to 10:398/398 of 1vpeA
- active site: R35 (= R48), K196 (= K214), G353 (= G369), G376 (= G396)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G212), A195 (≠ G213), K196 (= K214), K200 (≠ S218), G218 (= G238), A219 (≠ L239), N316 (≠ R335), P318 (= P337), G320 (= G339), V321 (= V340), E323 (= E342), G352 (= G368), G353 (= G369), D354 (≠ H370), S355 (≠ L371)
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)
38% identity, 93% coverage: 21:413/423 of query aligns to 11:394/654 of P36204
- R36 (= R48) binding substrate
- R118 (= R128) binding substrate
- R151 (= R168) binding substrate
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 14:411/414 of O60101
- Y75 (≠ I81) modified: Phosphotyrosine
- S76 (≠ T82) modified: Phosphoserine
- S143 (≠ H142) modified: Phosphoserine
- S172 (≠ P171) modified: Phosphoserine
- S173 (= S172) modified: Phosphoserine
- S183 (≠ A184) modified: Phosphoserine
- S253 (≠ K255) modified: Phosphoserine
- S260 (= S262) modified: Phosphoserine
- T299 (≠ N302) modified: Phosphothreonine
- S328 (≠ A329) modified: Phosphoserine
- S351 (≠ E352) modified: Phosphoserine
- T373 (≠ L371) modified: Phosphothreonine
- S387 (≠ P385) modified: Phosphoserine
- S390 (= S392) modified: Phosphoserine
Sites not aligning to the query:
- 412 modified: Phosphoserine
- 413 modified: Phosphoserine
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
36% identity, 93% coverage: 21:413/423 of query aligns to 10:410/413 of 2paaA
- active site: R35 (= R48), K212 (= K214), G370 (= G369), G393 (= G396)
- binding adenosine-5'-triphosphate: G210 (= G212), A211 (≠ G213), K216 (≠ S218), G235 (= G238), L253 (≠ N256), G309 (≠ I311), L310 (≠ R312), G334 (= G336), G337 (= G339), V338 (= V340), E340 (= E342), D371 (≠ H370)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
36% identity, 93% coverage: 21:413/423 of query aligns to 14:414/417 of P09041
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
36% identity, 95% coverage: 11:413/423 of query aligns to 9:412/416 of P00560
- R22 (= R29) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R48) binding substrate
- R122 (= R128) binding substrate
- R169 (= R168) binding substrate
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
36% identity, 95% coverage: 11:413/423 of query aligns to 8:411/415 of 1qpgA
- active site: R38 (= R48), K213 (= K214), G371 (= G369), G394 (= G396)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G237), G236 (= G238), N334 (≠ R335), P336 (= P337), G338 (= G339), V339 (= V340), F340 (≠ M341), E341 (= E342), G370 (= G368), G371 (= G369), D372 (≠ H370), T373 (≠ L371)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
34% identity, 93% coverage: 21:413/423 of query aligns to 12:404/407 of 4axxA
- active site: R37 (= R48), K206 (= K214), G364 (= G369), G387 (= G396)
- binding adenosine-5'-diphosphate: G204 (= G212), A205 (≠ G213), K210 (≠ S218), G228 (= G237), G229 (= G238), N327 (≠ R335), P329 (= P337), G331 (= G339), V332 (= V340), E334 (= E342), G363 (= G368), G364 (= G369), D365 (≠ H370), T366 (≠ L371)
- binding beryllium trifluoride ion: K206 (= K214), K210 (≠ S218), G363 (= G368)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 12:402/405 of 2wzdA
- active site: R37 (= R48), K204 (= K214), G362 (= G369), G385 (= G396)
- binding adenosine-5'-diphosphate: G202 (= G212), A203 (≠ G213), K204 (= K214), G226 (= G237), G227 (= G238), N325 (≠ R335), P327 (= P337), G329 (= G339), V330 (= V340), E332 (= E342), G361 (= G368), D363 (≠ H370), T364 (≠ L371)
- binding aluminum fluoride: R37 (= R48), K204 (= K214), G361 (= G368), G362 (= G369), G384 (= G395)
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
36% identity, 93% coverage: 21:413/423 of query aligns to 14:413/416 of 6yjeA
- active site: R39 (= R48), K215 (= K214), G373 (= G369), G396 (= G396)
- binding (2~{S})-2-(5-nitrofuran-2-yl)-2,3,5,6,7,8-hexahydro-1~{H}-[1]benzothiolo[2,3-d]pyrimidin-4-one: G237 (= G237), G238 (= G238), Y241 (≠ A241), L256 (≠ N256), F291 (≠ I294), M311 (≠ Y310), G312 (≠ I311), L313 (≠ R312), G340 (= G339), V341 (= V340)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 12:402/405 of 2wzcA
- active site: R37 (= R48), K204 (= K214), G362 (= G369), G385 (= G396)
- binding adenosine-5'-diphosphate: G202 (= G212), A203 (≠ G213), K204 (= K214), K208 (≠ S218), G226 (= G237), G227 (= G238), N325 (≠ R335), P327 (= P337), G329 (= G339), V330 (= V340), E332 (= E342), G361 (= G368), D363 (≠ H370), T364 (≠ L371)
- binding tetrafluoroaluminate ion: R37 (= R48), K204 (= K214), K208 (≠ S218), G361 (= G368), G362 (= G369), G384 (= G395)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 12:402/405 of 2wzbA
- active site: R37 (= R48), K204 (= K214), G362 (= G369), G385 (= G396)
- binding adenosine-5'-diphosphate: G202 (= G212), A203 (≠ G213), K204 (= K214), K208 (≠ S218), G226 (= G237), G227 (= G238), N325 (≠ R335), P327 (= P337), G329 (= G339), V330 (= V340), E332 (= E342), G361 (= G368), D363 (≠ H370), T364 (≠ L371)
- binding trifluoromagnesate: K204 (= K214), K208 (≠ S218), G361 (= G368), G384 (= G395), G385 (= G396)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
34% identity, 93% coverage: 21:414/423 of query aligns to 11:392/394 of P40924
- S183 (≠ N200) modified: Phosphoserine
- T299 (= T318) modified: Phosphothreonine
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
34% identity, 93% coverage: 21:413/423 of query aligns to 12:405/408 of 2x15A
- active site: R37 (= R48), K207 (= K214), G365 (= G369), G388 (= G396)
- binding adenosine-5'-diphosphate: G205 (= G212), A206 (≠ G213), K207 (= K214), K211 (≠ S218), G229 (= G237), G230 (= G238), N328 (≠ R335), P330 (= P337), G332 (= G339), V333 (= V340), E335 (= E342), G364 (= G368), G365 (= G369), D366 (≠ H370), T367 (≠ L371)
- binding adenosine-5'-triphosphate: G205 (= G212), A206 (≠ G213), K207 (= K214), K211 (≠ S218), G229 (= G237), G230 (= G238), N328 (≠ R335), G332 (= G339), V333 (= V340), E335 (= E342), G364 (= G368), G365 (= G369), D366 (≠ H370), T367 (≠ L371), G387 (= G395), G388 (= G396)
- binding 1,3-bisphosphoglyceric acid: D22 (= D31), N24 (= N33), R37 (= R48), H61 (= H71), R64 (≠ K74), R121 (= R128), R162 (= R168), K207 (= K214), K211 (≠ S218), G364 (= G368), G387 (= G395), G388 (= G396)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
34% identity, 93% coverage: 21:414/423 of query aligns to 11:392/394 of 1phpA
- active site: R36 (= R48), K197 (= K214), G351 (= G369), G374 (= G396)
- binding adenosine-5'-diphosphate: G195 (= G212), K201 (≠ S218), G219 (= G238), G220 (≠ L239), L237 (≠ N256), N316 (≠ R335), P318 (= P337), G320 (= G339), V321 (= V340), E323 (= E342), G350 (= G368), D352 (≠ H370), S353 (≠ L371)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
34% identity, 93% coverage: 21:414/423 of query aligns to 11:392/394 of P18912
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 13:413/416 of 1vjcA
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
35% identity, 93% coverage: 21:413/423 of query aligns to 13:413/416 of 1kf0A
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
34% identity, 93% coverage: 21:413/423 of query aligns to 12:412/414 of 2y3iA
- active site: R37 (= R48), K214 (= K214), G372 (= G369), G395 (= G396)
- binding tetrafluoroaluminate ion: K214 (= K214), G371 (= G368), G372 (= G369), G394 (= G395)
- binding l-adenosine-5'-diphosphate: G212 (= G212), A213 (≠ G213), F290 (≠ E297), N335 (≠ R335), G339 (= G339), V340 (= V340), E342 (= E342), G371 (= G368), G372 (= G369), D373 (≠ H370), T374 (≠ L371)
Query Sequence
>WP_014026822.1 NCBI__GCF_000223395.1:WP_014026822.1
MGSGAARLPLIEDLENHLGGLKGKKLLVRVDFNSPVNPQTGEIIDYSRIEAHVPTLRELL
ERGAALVVISHQGKPGSSDFITLEQHASILSKLLGVDVAFVDDVIGPAAREAIKKLEPGS
ILMLDNTRLLSEEVIEAPPEKHAKTIFVKRLAPLFDGYINDAFAAIHRSQPSIVGFPMLL
PSAAGRLVQREMDALSKIFNPSVAPKVFVLGGGKVTDSVKIVEALLERKVADYILTGGLL
ATLLLHAKGVDIGEKNVEVLKSAGVNELVIEKARRLIEAHKDVIVTPVDFKVEIDGEVET
VNVGEPIRGYIRDIGPETVKLYQERMEGAKLIVMRGPMGVMEDERFRAGTEELVEYALKS
GAYVIFGGGHLASVARRVIRSEGIPAARYHISSGGGALLLYLSGKPLPGIEALKLSAAKF
YGW
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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