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Comparing WP_057687355.1 NCBI__GCF_001431535.1:WP_057687355.1 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)
64% identity, 99% coverage: 1:389/391 of query aligns to 1:384/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L84) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
64% identity, 99% coverage: 2:389/391 of query aligns to 1:383/386 of 1zmrA
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
57% identity, 99% coverage: 3:389/391 of query aligns to 2:387/389 of 4ng4B
- active site: R35 (= R36), K191 (= K193), G344 (= G346), G367 (= G369)
- binding adenosine-5'-diphosphate: G189 (= G191), K195 (= K197), G213 (= G215), I286 (= I288), N310 (= N312), G311 (= G313), P312 (= P314), V315 (= V317), E317 (= E319), G343 (= G345), D345 (= D347), T346 (= T348)
- binding magnesium ion: D288 (= D290), G314 (= G316), F321 (= F323), S322 (= S324), T325 (= T327)
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
56% identity, 99% coverage: 1:389/391 of query aligns to 1:389/392 of 4feyA
- active site: R36 (= R36), K193 (= K193), G346 (= G346), G369 (= G369)
- binding adenosine-5'-diphosphate: G191 (= G191), S192 (= S192), K197 (= K197), G215 (= G215), G316 (= G316), V317 (= V317), E319 (= E319), D347 (= D347)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
46% identity, 99% coverage: 1:389/391 of query aligns to 1:394/394 of P40924
- S183 (≠ K179) modified: Phosphoserine
- T299 (= T295) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
48% identity, 99% coverage: 1:389/391 of query aligns to 1:394/394 of 1phpA
- active site: R36 (= R36), K197 (= K193), G351 (= G346), G374 (= G369)
- binding adenosine-5'-diphosphate: G195 (= G191), K201 (= K197), G219 (= G215), G220 (= G216), L237 (= L233), N316 (= N312), P318 (= P314), G320 (= G316), V321 (= V317), E323 (= E319), G350 (= G345), D352 (= D347), S353 (≠ T348)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
48% identity, 99% coverage: 1:389/391 of query aligns to 1:394/394 of P18912
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
46% identity, 99% coverage: 5:391/391 of query aligns to 2:398/398 of 1vpeA
- active site: R35 (= R36), K196 (= K193), G353 (= G346), G376 (= G369)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G191), A195 (≠ S192), K196 (= K193), K200 (= K197), G218 (= G215), A219 (≠ G216), N316 (= N312), P318 (= P314), G320 (= G316), V321 (= V317), E323 (= E319), G352 (= G345), G353 (= G346), D354 (= D347), S355 (≠ T348)
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)
45% identity, 99% coverage: 1:386/391 of query aligns to 1:394/654 of P36204
- R36 (= R36) binding
- R118 (= R113) binding
- R151 (= R146) binding
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
41% identity, 98% coverage: 6:389/391 of query aligns to 5:415/415 of 16pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G346), G395 (= G369)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G191), A214 (≠ S192), K219 (= K197), A238 (≠ G216), Y241 (≠ N219), L311 (= L289), P336 (= P314), G338 (= G316), V339 (= V317), E341 (= E319), G393 (= G367), G394 (= G368), G395 (= G369)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
41% identity, 98% coverage: 6:389/391 of query aligns to 5:415/415 of 13pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G346), G395 (= G369)
- binding adenosine-5'-diphosphate: G213 (= G191), A214 (≠ S192), K219 (= K197), L311 (= L289), P336 (= P314), G338 (= G316), V339 (= V317), E341 (= E319), G371 (= G345), D373 (= D347), S374 (≠ T348)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
41% identity, 99% coverage: 6:391/391 of query aligns to 9:421/440 of P07378
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: 6:386/391 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K193), K208 (= K197), G361 (= G345), G362 (= G346), G384 (= G368)
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: 6:386/391 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding trifluoromagnesate: K204 (= K193), K208 (= K197), G361 (= G345), G384 (= G368), G385 (= G369)
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: 6:386/391 of query aligns to 9:414/417 of P00558
- DFN 24:26 (≠ DLN 21:23) binding
- R39 (= R36) binding
- HLGR 63:66 (= HLGR 59:62) binding
- L88 (= L84) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ R93) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R113) binding
- K131 (≠ E118) modified: N6-malonyllysine; alternate
- G158 (≠ C133) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D139) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R146) binding
- K191 (≠ M168) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (≠ K183) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K193) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K197) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ P228) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A242) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ K244) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D261) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (≠ I288) binding
- D315 (= D290) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I291) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ R298) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E319) binding
- T352 (= T327) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 345:348) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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: 6:386/391 of query aligns to 7:412/414 of 2y3iA
- active site: R37 (= R36), K214 (= K193), G372 (= G346), G395 (= G369)
- binding tetrafluoroaluminate ion: K214 (= K193), G371 (= G345), G372 (= G346), G394 (= G368)
- binding l-adenosine-5'-diphosphate: G212 (= G191), A213 (≠ S192), F290 (= F268), N335 (= N312), G339 (= G316), V340 (= V317), E342 (= E319), G371 (= G345), G372 (= G346), D373 (= D347), T374 (= T348)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 97% coverage: 6:386/391 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R36), K207 (= K193), G365 (= G346), G388 (= G369)
- binding adenosine-5'-diphosphate: G205 (= G191), A206 (≠ S192), K207 (= K193), K211 (= K197), G229 (= G215), G230 (= G216), N328 (= N312), P330 (= P314), G332 (= G316), V333 (= V317), E335 (= E319), G364 (= G345), G365 (= G346), D366 (= D347), T367 (= T348)
- binding adenosine-5'-triphosphate: G205 (= G191), A206 (≠ S192), K207 (= K193), K211 (= K197), G229 (= G215), G230 (= G216), N328 (= N312), G332 (= G316), V333 (= V317), E335 (= E319), G364 (= G345), G365 (= G346), D366 (= D347), T367 (= T348), G387 (= G368), G388 (= G369)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R36), H61 (= H59), R64 (= R62), R121 (= R113), R162 (= R146), K207 (= K193), K211 (= K197), G364 (= G345), G387 (= G368), G388 (= G369)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
42% identity, 97% coverage: 6:386/391 of query aligns to 8:413/416 of 1vjcA
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 97% coverage: 6:386/391 of query aligns to 7:404/407 of 4axxA
- active site: R37 (= R36), K206 (= K193), G364 (= G346), G387 (= G369)
- binding adenosine-5'-diphosphate: G204 (= G191), A205 (≠ S192), K210 (= K197), G228 (= G215), G229 (= G216), N327 (= N312), P329 (= P314), G331 (= G316), V332 (= V317), E334 (= E319), G363 (= G345), G364 (= G346), D365 (= D347), T366 (= T348)
- binding beryllium trifluoride ion: K206 (= K193), K210 (= K197), G363 (= G345)
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: 6:386/391 of query aligns to 7:402/405 of 2wzdA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding aluminum fluoride: R37 (= R36), K204 (= K193), G361 (= G345), G362 (= G346), G384 (= G368)
Query Sequence
>WP_057687355.1 NCBI__GCF_001431535.1:WP_057687355.1
MSIVRMTDLDLSGKRVLIRQDLNVPIENGQISSEQRITASLPTLKRALEQGAAVMVTSHL
GRPKEGQWSEENSLQPVARRLSELLGRDVPLLRDWVGGVDVQPGQIVLLENCRMNVGEGK
DDEALARQYAALCDVFVMDAFGTAHRAQASTHGVIRFAPVAAGGPLLMAELDALAKALKE
PAKPLLAIVAGSKVSTKLELLASLVGKVDQLIVGGGIANTFIAAAGYPVGKSLYEPDLLE
TAKKIVADAKARGADIPLPTDVVVAKQFLPDAEATVKALADVAEDDLILDIGPDTAQRYA
ALINQAGTVVWNGPVGVFEFEAFSKGTEALARAIAGSRAFSIAGGGDTLAAVDKFDIAGD
VSYISTGGGAFLEFLEGKTLPAVAALEARGA
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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