SitesBLAST
Comparing WP_076477790.1 NCBI__GCF_900156495.1:WP_076477790.1 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)
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)
51% identity, 95% coverage: 15:400/405 of query aligns to 11:391/654 of P36204
- R36 (= R41) binding substrate
- R118 (= R123) binding substrate
- R151 (= R163) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
50% identity, 95% coverage: 15:400/405 of query aligns to 10:390/398 of 1vpeA
- active site: R35 (= R41), K196 (= K209), G353 (= G362), G376 (= G386)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G207), A195 (≠ S208), K196 (= K209), K200 (= K213), G218 (= G231), A219 (≠ G232), N316 (= N325), P318 (= P327), G320 (= G329), V321 (= V330), E323 (= E332), G352 (= G361), G353 (= G362), D354 (= D363), S355 (= S364)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
47% identity, 98% coverage: 6:403/405 of query aligns to 5:391/394 of P40924
- S183 (≠ D195) modified: Phosphoserine
- T299 (≠ S308) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
48% identity, 96% coverage: 15:404/405 of query aligns to 11:392/394 of 1phpA
- active site: R36 (= R41), K197 (= K209), G351 (= G362), G374 (= G386)
- binding adenosine-5'-diphosphate: G195 (= G207), K201 (= K213), G219 (= G231), G220 (= G232), L237 (= L249), N316 (= N325), P318 (= P327), G320 (= G329), V321 (= V330), E323 (= E332), G350 (= G361), D352 (= D363), S353 (= S364)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
48% identity, 96% coverage: 15:404/405 of query aligns to 11:392/394 of P18912
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
45% identity, 96% coverage: 15:403/405 of query aligns to 11:395/398 of 3zlbA
- active site: R36 (= R41), K204 (= K209), G355 (= G362), G378 (= G386)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G207), S203 (= S208), G226 (= G231), G227 (= G232), N320 (= N325), P322 (= P327), G324 (= G329), V325 (= V330), E327 (= E332), G354 (= G361), G355 (= G362), D356 (= D363), S357 (= S364)
Sites not aligning to the query:
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
43% identity, 97% coverage: 15:405/405 of query aligns to 14:413/414 of O60101
- Y75 (= Y76) modified: Phosphotyrosine
- S76 (= S77) modified: Phosphoserine
- S143 (≠ T137) modified: Phosphoserine
- S172 (≠ A166) modified: Phosphoserine
- S173 (= S167) modified: Phosphoserine
- S183 (≠ A179) modified: Phosphoserine
- S253 (= S248) modified: Phosphoserine
- S260 (vs. gap) modified: Phosphoserine
- T299 (≠ P291) modified: Phosphothreonine
- S328 (≠ A319) modified: Phosphoserine
- S351 (≠ G342) modified: Phosphoserine
- T373 (≠ S364) modified: Phosphothreonine
- S387 (= S379) modified: Phosphoserine
- S390 (= S382) modified: Phosphoserine
- S412 (≠ E404) modified: Phosphoserine
- S413 (= S405) modified: Phosphoserine
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride (see paper)
43% identity, 97% coverage: 15:405/405 of query aligns to 12:406/407 of 4axxA
- active site: R37 (= R41), K206 (= K209), G364 (= G362), G387 (= G386)
- binding adenosine-5'-diphosphate: G204 (= G207), A205 (≠ S208), K210 (= K213), G228 (= G231), G229 (= G232), N327 (= N325), P329 (= P327), G331 (= G329), V332 (= V330), E334 (= E332), G363 (= G361), G364 (= G362), D365 (= D363), T366 (≠ S364)
- binding beryllium trifluoride ion: K206 (= K209), K210 (= K213), G363 (= G361)
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
40% identity, 99% coverage: 6:405/405 of query aligns to 7:415/416 of 6yjeA
- active site: R39 (= R41), K215 (= K209), G373 (= G362), G396 (= G386)
- 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 (= G231), G238 (= G232), Y241 (≠ F235), L256 (= L249), F291 (= F281), M311 (= M300), G312 (= G301), L313 (= L302), G340 (= G329), V341 (= V330)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
43% identity, 97% coverage: 15:405/405 of query aligns to 12:404/405 of 2wzcA
- active site: R37 (= R41), K204 (= K209), G362 (= G362), G385 (= G386)
- binding adenosine-5'-diphosphate: G202 (= G207), A203 (≠ S208), K204 (= K209), K208 (= K213), G226 (= G231), G227 (= G232), N325 (= N325), P327 (= P327), G329 (= G329), V330 (= V330), E332 (= E332), G361 (= G361), D363 (= D363), T364 (≠ S364)
- binding tetrafluoroaluminate ion: R37 (= R41), K204 (= K209), K208 (= K213), G361 (= G361), G362 (= G362), G384 (= G385)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
43% identity, 97% coverage: 15:405/405 of query aligns to 12:404/405 of 2wzbA
- active site: R37 (= R41), K204 (= K209), G362 (= G362), G385 (= G386)
- binding adenosine-5'-diphosphate: G202 (= G207), A203 (≠ S208), K204 (= K209), K208 (= K213), G226 (= G231), G227 (= G232), N325 (= N325), P327 (= P327), G329 (= G329), V330 (= V330), E332 (= E332), G361 (= G361), D363 (= D363), T364 (≠ S364)
- binding trifluoromagnesate: K204 (= K209), K208 (= K213), G361 (= G361), G384 (= G385), G385 (= G386)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 97% coverage: 15:405/405 of query aligns to 12:407/408 of 2x15A
- active site: R37 (= R41), K207 (= K209), G365 (= G362), G388 (= G386)
- binding adenosine-5'-diphosphate: G205 (= G207), A206 (≠ S208), K207 (= K209), K211 (= K213), G229 (= G231), G230 (= G232), N328 (= N325), P330 (= P327), G332 (= G329), V333 (= V330), E335 (= E332), G364 (= G361), G365 (= G362), D366 (= D363), T367 (≠ S364)
- binding adenosine-5'-triphosphate: G205 (= G207), A206 (≠ S208), K207 (= K209), K211 (= K213), G229 (= G231), G230 (= G232), N328 (= N325), G332 (= G329), V333 (= V330), E335 (= E332), G364 (= G361), G365 (= G362), D366 (= D363), T367 (≠ S364), G387 (= G385), G388 (= G386)
- binding 1,3-bisphosphoglyceric acid: D22 (= D25), N24 (= N27), R37 (= R41), H61 (= H64), R64 (= R67), R121 (= R123), R162 (= R163), K207 (= K209), K211 (= K213), G364 (= G361), G387 (= G385), G388 (= G386)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
43% identity, 95% coverage: 18:403/405 of query aligns to 17:412/416 of P00560
- R22 (= R23) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R41) binding substrate
- R122 (= R123) binding substrate
- R169 (= R163) binding substrate
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
42% identity, 97% coverage: 15:405/405 of query aligns to 12:404/405 of 2wzdA
- active site: R37 (= R41), K204 (= K209), G362 (= G362), G385 (= G386)
- binding adenosine-5'-diphosphate: G202 (= G207), A203 (≠ S208), K204 (= K209), G226 (= G231), G227 (= G232), N325 (= N325), P327 (= P327), G329 (= G329), V330 (= V330), E332 (= E332), G361 (= G361), D363 (= D363), T364 (≠ S364)
- binding aluminum fluoride: R37 (= R41), K204 (= K209), G361 (= G361), G362 (= G362), G384 (= G385)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
43% identity, 95% coverage: 18:403/405 of query aligns to 16:411/415 of 1qpgA
- active site: R38 (= R41), K213 (= K209), G371 (= G362), G394 (= G386)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G231), G236 (= G232), N334 (= N325), P336 (= P327), G338 (= G329), V339 (= V330), F340 (= F331), E341 (= E332), G370 (= G361), G371 (= G362), D372 (= D363), T373 (≠ S364)
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
42% identity, 97% coverage: 15:405/405 of query aligns to 12:414/414 of 2y3iA
- active site: R37 (= R41), K214 (= K209), G372 (= G362), G395 (= G386)
- binding tetrafluoroaluminate ion: K214 (= K209), G371 (= G361), G372 (= G362), G394 (= G385)
- binding l-adenosine-5'-diphosphate: G212 (= G207), A213 (≠ S208), F290 (= F281), N335 (= N325), G339 (= G329), V340 (= V330), E342 (= E332), G371 (= G361), G372 (= G362), D373 (= D363), T374 (≠ S364)
P00558 Phosphoglycerate kinase 1; Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2; EC 2.7.2.3 from Homo sapiens (Human) (see 16 papers)
42% identity, 97% coverage: 15:405/405 of query aligns to 14:416/417 of P00558
- DFN 24:26 (≠ DLN 25:27) binding substrate
- R39 (= R41) binding substrate
- HLGR 63:66 (= HLGR 64:67) binding substrate
- L88 (≠ E88) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ G97) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R123) binding substrate
- K131 (vs. gap) modified: N6-malonyllysine; alternate
- G158 (≠ D150) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D156) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R163) binding substrate
- K191 (≠ A184) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R199) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K209) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K213) binding ATP; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ N244) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ C258) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ G260) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D274) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (= G301) binding ATP
- D315 (= D303) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I304) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ R311) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E332) binding ATP
- T352 (= T340) to N: in dbSNP:rs137852530
- GGDT 373:376 (≠ GGDS 361:364) binding ATP
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
42% identity, 97% coverage: 15:405/405 of query aligns to 14:416/417 of 4o33A
- active site: R39 (= R41), K216 (= K209), G374 (= G362), G397 (= G386)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G231), G239 (= G232), T255 (≠ D247), L257 (= L249), F292 (= F281), M312 (= M300), G313 (= G301), L314 (= L302), G341 (= G329), V342 (= V330)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
41% identity, 97% coverage: 14:405/405 of query aligns to 12:415/416 of 1kf0A
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
41% identity, 97% coverage: 15:405/405 of query aligns to 13:415/416 of 1vjcA
Query Sequence
>WP_076477790.1 NCBI__GCF_900156495.1:WP_076477790.1
MASVPTLTDLLADGVSGRGVLVRSDLNVPLDDHGQITDPGRILASVPTLTALLDAGAKVV
VTAHLGRPKGAPEAKYSLAPVAERLSAELGRNVQLAGDVVGQDALARSEGLTDGDILLVE
NVRFDPRETSKDEAERTALAEALVELVGEDGAFVSDGFGVVHRKQASVYDVAKLLPHYAG
ELVAAEVEVLTKLTDEVERPFAVVLGGSKVSDKIGVIEALAPKVDTLVIGGGMAFTFLAA
EGLNVGDSLLQQDQIEVCKGLLERFGDVIHLPVDVVVASAFAADAESKVVPAQEIPDGWM
GLDIGPESVKRFAAVLSGAKTIFWNGPSGVFEFAKFADGTRGVAEAIIETTRHGAFTVVG
GGDSAAAVRTLGLPEDGFSHISTGGGASLEYLEGKDLPGLQILES
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