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Comparing WP_011766565.1 NCBI__GCF_000061505.1:WP_011766565.1 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)
59% identity, 99% coverage: 1:391/394 of query aligns to 1:384/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L85) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
59% identity, 99% coverage: 2:391/394 of query aligns to 1:383/386 of 1zmrA
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
54% identity, 99% coverage: 1:391/394 of query aligns to 1:389/392 of 4feyA
- active site: R36 (= R37), K193 (= K195), G346 (= G348), G369 (= G371)
- binding adenosine-5'-diphosphate: G191 (= G193), S192 (≠ A194), K197 (= K199), G215 (= G217), G316 (= G318), V317 (= V319), E319 (= E321), D347 (= D349)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
54% identity, 98% coverage: 6:391/394 of query aligns to 5:387/389 of 4ng4B
- active site: R35 (= R37), K191 (= K195), G344 (= G348), G367 (= G371)
- binding adenosine-5'-diphosphate: G189 (= G193), K195 (= K199), G213 (= G217), I286 (= I290), N310 (= N314), G311 (= G315), P312 (= P316), V315 (= V319), E317 (= E321), G343 (= G347), D345 (= D349), T346 (= T350)
- binding magnesium ion: D288 (= D292), G314 (= G318), F321 (= F325), S322 (≠ A326), T325 (= T329)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
49% identity, 99% coverage: 1:391/394 of query aligns to 1:394/394 of P40924
- S183 (≠ H181) modified: Phosphoserine
- T299 (= T297) 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: 1:391/394 of query aligns to 1:394/394 of 1phpA
- active site: R36 (= R37), K197 (= K195), G351 (= G348), G374 (= G371)
- binding adenosine-5'-diphosphate: G195 (= G193), K201 (= K199), G219 (= G217), G220 (= G218), L237 (= L235), N316 (= N314), P318 (= P316), G320 (= G318), V321 (= V319), E323 (= E321), G350 (= G347), D352 (= D349), S353 (≠ T350)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
48% identity, 99% coverage: 1:391/394 of query aligns to 1:394/394 of P18912
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)
46% identity, 98% coverage: 1:388/394 of query aligns to 1:394/654 of P36204
- R36 (= R37) binding substrate
- R118 (= R115) binding substrate
- R151 (= R148) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
46% identity, 98% coverage: 6:391/394 of query aligns to 5:396/398 of 1vpeA
- active site: R35 (= R37), K196 (= K195), G353 (= G348), G376 (= G371)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G193), A195 (= A194), K196 (= K195), K200 (= K199), G218 (= G217), A219 (≠ G218), N316 (= N314), P318 (= P316), G320 (= G318), V321 (= V319), E323 (= E321), G352 (= G347), G353 (= G348), D354 (= D349), S355 (≠ T350)
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: 6:388/394 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (= A194), K204 (= K195), K208 (= K199), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding tetrafluoroaluminate ion: R37 (= R37), K204 (= K195), K208 (= K199), G361 (= G347), G362 (= G348), G384 (= G370)
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: 6:388/394 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (= A194), K204 (= K195), K208 (= K199), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding trifluoromagnesate: K204 (= K195), K208 (= K199), G361 (= G347), G384 (= G370), G385 (= G371)
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, 97% coverage: 6:388/394 of query aligns to 7:402/405 of 2wzdA
- active site: R37 (= R37), K204 (= K195), G362 (= G348), G385 (= G371)
- binding adenosine-5'-diphosphate: G202 (= G193), A203 (= A194), K204 (= K195), G226 (= G217), G227 (= G218), N325 (= N314), P327 (= P316), G329 (= G318), V330 (= V319), E332 (= E321), G361 (= G347), D363 (= D349), T364 (= T350)
- binding aluminum fluoride: R37 (= R37), K204 (= K195), G361 (= G347), G362 (= G348), G384 (= G370)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
42% identity, 98% coverage: 6:391/394 of query aligns to 9:414/414 of O60101
- Y75 (≠ D72) modified: Phosphotyrosine
- S76 (≠ T74) modified: Phosphoserine
- S143 (≠ K122) modified: Phosphoserine
- S172 (≠ A151) modified: Phosphoserine
- S173 (≠ T152) modified: Phosphoserine
- S183 (≠ A165) modified: Phosphoserine
- S253 (= S234) modified: Phosphoserine
- S260 (≠ V241) modified: Phosphoserine
- T299 (≠ S280) modified: Phosphothreonine
- S328 (≠ A308) modified: Phosphoserine
- S351 (vs. gap) modified: Phosphoserine
- T373 (= T350) modified: Phosphothreonine
- S387 (≠ G364) modified: Phosphoserine
- S390 (= S367) modified: Phosphoserine
- S412 (≠ E389) modified: Phosphoserine
- S413 (≠ A390) modified: Phosphoserine
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 97% coverage: 6:388/394 of query aligns to 7:404/407 of 4axxA
- active site: R37 (= R37), K206 (= K195), G364 (= G348), G387 (= G371)
- binding adenosine-5'-diphosphate: G204 (= G193), A205 (= A194), K210 (= K199), G228 (= G217), G229 (= G218), N327 (= N314), P329 (= P316), G331 (= G318), V332 (= V319), E334 (= E321), G363 (= G347), G364 (= G348), D365 (= D349), T366 (= T350)
- binding beryllium trifluoride ion: K206 (= K195), K210 (= K199), G363 (= G347)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 97% coverage: 6:388/394 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R37), K207 (= K195), G365 (= G348), G388 (= G371)
- binding adenosine-5'-diphosphate: G205 (= G193), A206 (= A194), K207 (= K195), K211 (= K199), G229 (= G217), G230 (= G218), N328 (= N314), P330 (= P316), G332 (= G318), V333 (= V319), E335 (= E321), G364 (= G347), G365 (= G348), D366 (= D349), T367 (= T350)
- binding adenosine-5'-triphosphate: G205 (= G193), A206 (= A194), K207 (= K195), K211 (= K199), G229 (= G217), G230 (= G218), N328 (= N314), G332 (= G318), V333 (= V319), E335 (= E321), G364 (= G347), G365 (= G348), D366 (= D349), T367 (= T350), G387 (= G370), G388 (= G371)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R37), H61 (= H60), R64 (= R63), R121 (= R115), R162 (= R148), K207 (= K195), K211 (= K199), G364 (= G347), G387 (= G370), G388 (= G371)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
42% identity, 97% coverage: 6:388/394 of query aligns to 8:413/416 of 1vjcA
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: 6:388/394 of query aligns to 7:412/414 of 2y3iA
- active site: R37 (= R37), K214 (= K195), G372 (= G348), G395 (= G371)
- binding tetrafluoroaluminate ion: K214 (= K195), G371 (= G347), G372 (= G348), G394 (= G370)
- binding l-adenosine-5'-diphosphate: G212 (= G193), A213 (= A194), F290 (≠ V270), N335 (= N314), G339 (= G318), V340 (= V319), E342 (= E321), G371 (= G347), G372 (= G348), D373 (= D349), T374 (= T350)
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: 6:388/394 of query aligns to 9:414/417 of P00558
- DFN 24:26 (≠ DLN 21:23) binding substrate
- R39 (= R37) binding substrate
- HLGR 63:66 (= HLGR 60:63) binding substrate
- L88 (= L85) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ A94) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R115) binding substrate
- K131 (≠ E120) modified: N6-malonyllysine; alternate
- G158 (≠ C135) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D141) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R148) binding substrate
- K191 (≠ G170) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R185) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K195) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K199) binding ATP; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ R230) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A244) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ Q246) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D263) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (vs. gap) binding ATP
- D315 (= D292) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ F293) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (= K300) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E321) binding ATP
- T352 (= T329) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 347:350) 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: 6:388/394 of query aligns to 9:414/417 of 4o33A
- active site: R39 (= R37), K216 (= K195), G374 (= G348), G397 (= G371)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G217), G239 (= G218), T255 (≠ E233), L257 (= L235), F292 (≠ V270), M312 (≠ I290), G313 (vs. gap), L314 (= L291), G341 (= G318), V342 (= V319)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
42% identity, 97% coverage: 6:388/394 of query aligns to 8:413/416 of 1kf0A
Query Sequence
>WP_011766565.1 NCBI__GCF_000061505.1:WP_011766565.1
MQVKKLTDLDVRGKKVFIRADLNVPQDEAGNITEDTRIRASIPSIQYCLDNGAAVMVTSH
LGRPTEGEVGPDDTLAPVAVRLGQLLHKPVKLIANWVEGGFEVKPGEVVLLENCRCNKGE
KKDNEELAKKMAALCDVYVNDAFGTAHRAEATTHGIARFAPVSCAGILMGAEIDALSKAL
HQPARPLVAIVGGAKVSTKLTILKTLADKVDQLIVGGGIANTFLLAAGKRIGESLAEPEM
VREAQQVMDIMKSRGAEVPLPIDVVVADEVSALARANRISVDEVGPHDRILDFGPKTSAK
LADIIAHAGTIVWNGPVGVFEHAQFAGGTKMMASAIAHSEAFSIAGGGDTLAAIAKFHIA
DDVGYISTGGGAFLEFLEGKKLPAIAALEARYEG
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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