SitesBLAST
Comparing BPHYT_RS16270 FitnessBrowser__BFirm:BPHYT_RS16270 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)
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
62% identity, 99% coverage: 4:397/397 of query aligns to 2:384/386 of 1zmrA
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
62% identity, 99% coverage: 4:397/397 of query aligns to 3:385/387 of P0A799
- K84 (≠ L90) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
59% identity, 96% coverage: 16:397/397 of query aligns to 11:390/392 of 4feyA
- active site: R36 (= R42), K193 (= K200), G346 (= G353), G369 (= G376)
- binding adenosine-5'-diphosphate: G191 (= G198), S192 (= S199), K197 (= K204), G215 (= G222), G316 (= G323), V317 (= V324), E319 (= E326), D347 (= D354)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
54% identity, 99% coverage: 5:397/397 of query aligns to 3:388/389 of 4ng4B
- active site: R35 (= R42), K191 (= K200), G344 (= G353), G367 (= G376)
- binding adenosine-5'-diphosphate: G189 (= G198), K195 (= K204), G213 (= G222), I286 (= I295), N310 (= N319), G311 (= G320), P312 (= P321), V315 (= V324), E317 (= E326), G343 (= G352), D345 (= D354), T346 (= T355)
- binding magnesium ion: D288 (= D297), G314 (= G323), F321 (= F330), S322 (≠ G331), T325 (= T334)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
48% identity, 96% coverage: 16:396/397 of query aligns to 11:394/394 of P40924
- S183 (≠ G186) modified: Phosphoserine
- T299 (= T302) modified: Phosphothreonine
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
47% identity, 94% coverage: 16:390/397 of query aligns to 10:390/398 of 1vpeA
- active site: R35 (= R42), K196 (= K200), G353 (= G353), G376 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G198), A195 (≠ S199), K196 (= K200), K200 (= K204), G218 (= G222), A219 (≠ G223), N316 (= N319), P318 (= P321), G320 (= G323), V321 (= V324), E323 (= E326), G352 (= G352), G353 (= G353), D354 (= D354), S355 (≠ T355)
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, 94% coverage: 16:390/397 of query aligns to 11:391/654 of P36204
- R36 (= R42) binding
- R118 (= R120) binding
- R151 (= R153) binding
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
47% identity, 97% coverage: 11:396/397 of query aligns to 6:394/394 of 1phpA
- active site: R36 (= R42), K197 (= K200), G351 (= G353), G374 (= G376)
- binding adenosine-5'-diphosphate: G195 (= G198), K201 (= K204), G219 (= G222), G220 (= G223), L237 (= L240), N316 (= N319), P318 (= P321), G320 (= G323), V321 (= V324), E323 (= E326), G350 (= G352), D352 (= D354), S353 (≠ T355)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
47% identity, 97% coverage: 11:396/397 of query aligns to 6:394/394 of P18912
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
44% identity, 96% coverage: 16:396/397 of query aligns to 13:414/415 of 3pgkA
- active site: R38 (= R42), K213 (= K200), G371 (= G353), G394 (= G376)
- binding adenosine-5'-triphosphate: G211 (= G198), A212 (≠ S199), K213 (= K200), F289 (= F275), L311 (= L296), N334 (= N319), G335 (= G320), P336 (= P321), G338 (= G323), V339 (= V324), D372 (= D354)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
44% identity, 96% coverage: 16:396/397 of query aligns to 14:415/416 of P00560
- R22 (= R24) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R42) binding
- R122 (= R120) binding
- R169 (= R153) binding
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
43% identity, 96% coverage: 16:395/397 of query aligns to 12:404/405 of 2wzcA
- active site: R37 (= R42), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (≠ S199), K204 (= K200), K208 (= K204), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding tetrafluoroaluminate ion: R37 (= R42), K204 (= K200), K208 (= K204), G361 (= G352), G362 (= G353), G384 (= G375)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
43% identity, 96% coverage: 16:395/397 of query aligns to 12:404/405 of 2wzbA
- active site: R37 (= R42), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (≠ S199), K204 (= K200), K208 (= K204), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding trifluoromagnesate: K204 (= K200), K208 (= K204), G361 (= G352), G384 (= G375), G385 (= G376)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
44% identity, 96% coverage: 16:396/397 of query aligns to 13:414/415 of 1qpgA
- active site: R38 (= R42), K213 (= K200), G371 (= G353), G394 (= G376)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G222), G236 (= G223), N334 (= N319), P336 (= P321), G338 (= G323), V339 (= V324), F340 (= F325), E341 (= E326), G370 (= G352), G371 (= G353), D372 (= D354), T373 (= T355)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
43% identity, 96% coverage: 16:395/397 of query aligns to 12:404/405 of 2wzdA
- active site: R37 (= R42), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (≠ S199), K204 (= K200), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding aluminum fluoride: R37 (= R42), K204 (= K200), G361 (= G352), G362 (= G353), G384 (= G375)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 96% coverage: 16:395/397 of query aligns to 12:406/407 of 4axxA
- active site: R37 (= R42), K206 (= K200), G364 (= G353), G387 (= G376)
- binding adenosine-5'-diphosphate: G204 (= G198), A205 (≠ S199), K210 (= K204), G228 (= G222), G229 (= G223), N327 (= N319), P329 (= P321), G331 (= G323), V332 (= V324), E334 (= E326), G363 (= G352), G364 (= G353), D365 (= D354), T366 (= T355)
- binding beryllium trifluoride ion: K206 (= K200), K210 (= K204), G363 (= G352)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 96% coverage: 16:395/397 of query aligns to 12:407/408 of 2x15A
- active site: R37 (= R42), K207 (= K200), G365 (= G353), G388 (= G376)
- binding adenosine-5'-diphosphate: G205 (= G198), A206 (≠ S199), K207 (= K200), K211 (= K204), G229 (= G222), G230 (= G223), N328 (= N319), P330 (= P321), G332 (= G323), V333 (= V324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355)
- binding adenosine-5'-triphosphate: G205 (= G198), A206 (≠ S199), K207 (= K200), K211 (= K204), G229 (= G222), G230 (= G223), N328 (= N319), G332 (= G323), V333 (= V324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355), G387 (= G375), G388 (= G376)
- binding 1,3-bisphosphoglyceric acid: D22 (= D26), N24 (= N28), R37 (= R42), H61 (= H65), R64 (= R68), R121 (= R120), R162 (= R153), K207 (= K200), K211 (= K204), G364 (= G352), G387 (= G375), G388 (= G376)
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, 96% coverage: 16:395/397 of query aligns to 12:414/414 of 2y3iA
- active site: R37 (= R42), K214 (= K200), G372 (= G353), G395 (= G376)
- binding tetrafluoroaluminate ion: K214 (= K200), G371 (= G352), G372 (= G353), G394 (= G375)
- binding l-adenosine-5'-diphosphate: G212 (= G198), A213 (≠ S199), F290 (= F275), N335 (= N319), G339 (= G323), V340 (= V324), E342 (= E326), G371 (= G352), G372 (= G353), D373 (= D354), T374 (= T355)
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, 96% coverage: 16:395/397 of query aligns to 14:416/417 of P00558
- DFN 24:26 (≠ DLN 26:28) binding
- R39 (= R42) binding
- HLGR 63:66 (= HLGR 65:68) binding
- L88 (= L90) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ A99) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R120) binding
- K131 (≠ E125) modified: N6-malonyllysine; alternate
- G158 (≠ C140) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D146) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R153) binding
- K191 (≠ A175) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R190) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K200) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K204) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ K235) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A249) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ A251) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D268) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (≠ I295) binding
- D315 (= D297) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I298) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ V305) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E326) binding
- T352 (= T334) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 352:355) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
41% identity, 96% coverage: 16:395/397 of query aligns to 14:416/417 of P09041
Query Sequence
>BPHYT_RS16270 FitnessBrowser__BFirm:BPHYT_RS16270
MNKVLRLSDLIAEGQLSGKRVFIRADLNVPQDDQGNITEDTRIRASVPAIKASLDAGAAV
MVTSHLGRPTEGDFKPEDSLAPVAKRLAELLGRDVPLVANWVENGVNVAPGSVVLLENCR
VNKGEKKDSDELAQKMAKLCDIYVNDAFGTAHRAEATTHGIAKYAPVACAGPLLAAELEA
LGKALGAPKRPLVAIVAGSKVSTKLTILKSLADKVDQLIVGGGIANTFMLAAGLKIGKSL
AEADLVNEAKAIIDAAKARGASVPIPTDVVTAKEFSPTAKAEIKAVADVQDDDMILDIGP
ETAKVLAAQLEKAGTIVWNGPVGVFEFDQFGNGTKTLADAIAKSSAFSIAGGGDTLAAIA
KYGIHDKVSYISTGGGAFLEFLEGKKLPAVDVLESRA
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