SitesBLAST
Comparing WP_078210855.1 NCBI__GCF_002017945.1:WP_078210855.1 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)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
50% identity, 99% coverage: 2:393/395 of query aligns to 4:391/394 of 1phpA
- active site: R36 (= R35), K197 (= K197), G351 (= G353), G374 (= G376)
- binding adenosine-5'-diphosphate: G195 (= G195), K201 (= K201), G219 (= G219), G220 (= G220), L237 (≠ I237), N316 (= N316), P318 (= P318), G320 (= G320), V321 (= V321), E323 (= E323), G350 (= G352), D352 (= D354), S353 (= S355)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
50% identity, 99% coverage: 2:393/395 of query aligns to 4:391/394 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)
51% identity, 99% coverage: 3:393/395 of query aligns to 5:394/654 of P36204
- R36 (= R35) binding substrate
- R118 (= R116) binding substrate
- R151 (= R149) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
51% identity, 99% coverage: 3:393/395 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R35), K196 (= K197), G353 (= G353), G376 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G195), A195 (≠ S196), K196 (= K197), K200 (= K201), G218 (= G219), A219 (≠ G220), N316 (= N316), P318 (= P318), G320 (= G320), V321 (= V321), E323 (= E323), G352 (= G352), G353 (= G353), D354 (= D354), S355 (= S355)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
49% identity, 99% coverage: 2:393/395 of query aligns to 4:391/394 of P40924
- S183 (≠ K183) modified: Phosphoserine
- T299 (≠ S299) modified: Phosphothreonine
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
48% identity, 97% coverage: 12:393/395 of query aligns to 17:413/416 of 6yjeA
- active site: R39 (= R35), K215 (= K197), G373 (= G353), G396 (= G376)
- 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 (= G219), G238 (= G220), Y241 (≠ F223), L256 (≠ I237), F291 (= F272), M311 (≠ Q291), G312 (= G292), L313 (= L293), G340 (= G320), V341 (= V321)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
47% identity, 98% coverage: 8:393/395 of query aligns to 21:421/424 of 1ltkC
- active site: R47 (= R35), K223 (= K197), G381 (= G353), G404 (= G376)
- binding adenosine monophosphate: G221 (= G195), A222 (≠ S196), K223 (= K197), G245 (= G219), G246 (= G220), G348 (= G320), V349 (= V321), E351 (= E323), D382 (= D354)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
45% identity, 99% coverage: 3:393/395 of query aligns to 7:413/416 of 1kf0A
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
46% identity, 99% coverage: 3:395/395 of query aligns to 8:414/416 of P00560
- R22 (= R17) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- N26 (= N21) binding (2R)-3-phosphoglycerate
- R39 (= R35) binding (2R)-3-phosphoglycerate
- R122 (= R116) binding (2R)-3-phosphoglycerate
- A213 (≠ S196) binding ATP
- K214 (= K197) binding ATP
- L312 (= L293) binding ATP
- N335 (= N316) binding covalent
- E342 (= E323) binding ATP
- G371 (= G352) binding (2R)-3-phosphoglycerate
- D373 (= D354) binding covalent; binding Mg(2+)
- G394 (= G375) binding (2R)-3-phosphoglycerate
- G395 (= G376) binding (2R)-3-phosphoglycerate
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
46% identity, 99% coverage: 3:393/395 of query aligns to 6:402/405 of 2wzcA
- active site: R37 (= R35), K204 (= K197), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (≠ S196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (= V321), E332 (= E323), G361 (= G352), D363 (= D354), T364 (≠ S355)
- binding tetrafluoroaluminate ion: R37 (= R35), K204 (= K197), K208 (= K201), 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)
46% identity, 99% coverage: 3:393/395 of query aligns to 6:402/405 of 2wzbA
- active site: R37 (= R35), K204 (= K197), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (≠ S196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (= V321), E332 (= E323), G361 (= G352), D363 (= D354), T364 (≠ S355)
- binding trifluoromagnesate: K204 (= K197), K208 (= K201), G361 (= G352), G384 (= G375), G385 (= G376)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride (see paper)
45% identity, 99% coverage: 3:393/395 of query aligns to 6:404/407 of 4axxA
- active site: R37 (= R35), K206 (= K197), G364 (= G353), G387 (= G376)
- binding adenosine-5'-diphosphate: G204 (= G195), A205 (≠ S196), K210 (= K201), G228 (= G219), G229 (= G220), N327 (= N316), P329 (= P318), G331 (= G320), V332 (= V321), E334 (= E323), G363 (= G352), G364 (= G353), D365 (= D354), T366 (≠ S355)
- binding beryllium trifluoride ion: K206 (= K197), K210 (= K201), G363 (= G352)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
45% identity, 99% coverage: 3:393/395 of query aligns to 6:405/408 of 2x15A
- active site: R37 (= R35), K207 (= K197), G365 (= G353), G388 (= G376)
- binding adenosine-5'-diphosphate: G205 (= G195), A206 (≠ S196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), P330 (= P318), G332 (= G320), V333 (= V321), E335 (= E323), G364 (= G352), G365 (= G353), D366 (= D354), T367 (≠ S355)
- binding adenosine-5'-triphosphate: G205 (= G195), A206 (≠ S196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), G332 (= G320), V333 (= V321), E335 (= E323), G364 (= G352), G365 (= G353), D366 (= D354), T367 (≠ S355), G387 (= G375), G388 (= G376)
- binding 1,3-bisphosphoglyceric acid: D22 (= D19), N24 (= N21), R37 (= R35), H61 (= H58), R64 (= R61), R121 (= R116), R162 (= R149), K207 (= K197), K211 (= K201), G364 (= G352), G387 (= G375), G388 (= G376)
P00558 Phosphoglycerate kinase 1; Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2; EC 2.7.11.1; EC 2.7.2.3 from Homo sapiens (Human) (see 17 papers)
45% identity, 99% coverage: 3:393/395 of query aligns to 8:414/417 of P00558
- V23 (= V18) binding (2R)-3-phosphoglycerate
- F25 (= F20) binding (2R)-3-phosphoglycerate
- Q38 (≠ N34) binding (2R)-3-phosphoglycerate
- QRIKAA 38:43 (≠ NRIEAA 34:39) Mitochondrial targeting region exposed following cis-trans isomerization by PIN1 and recognized by the TOM complex for mitochondrial translocation of the protein
- S62 (= S57) binding (2R)-3-phosphoglycerate
- G65 (= G60) binding (2R)-3-phosphoglycerate
- L88 (≠ V81) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ S90) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- L122 (= L115) binding (2R)-3-phosphoglycerate
- K131 (≠ G124) modified: N6-malonyllysine; alternate
- G158 (= G136) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D142) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- H170 (= H148) binding (2R)-3-phosphoglycerate
- K191 (≠ A172) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- S203 (≠ N184) modified: Phosphoserine; by MAPK1
- R206 (≠ K187) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- G214 (= G195) binding ADP; binding CDP
- A215 (≠ S196) binding Mg(2+)
- K216 (= K197) modified: N6-(2-hydroxyisobutyryl)lysine
- A218 (≠ S199) binding Mg(2+)
- D219 (≠ S200) binding CDP; binding Mg(2+)
- K220 (= K201) modified: N6-(2-hydroxyisobutyryl)lysine
- G238 (= G219) binding ADP; binding CDP
- E252 (≠ S232) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A246) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ E248) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D265) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- D315 (= D294) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ A295) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ N302) modified: N6-(2-hydroxyisobutyryl)lysine
- G338 (= G317) binding CDP
- V340 (≠ L319) binding CDP
- F343 (= F322) binding ADP; binding CDP
- T352 (= T331) to N: in dbSNP:rs137852530
- T378 (≠ A357) mutation to P: Loss of activity.
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)
45% identity, 99% coverage: 3:393/395 of query aligns to 6:412/414 of 2y3iA
- active site: R37 (= R35), K214 (= K197), G372 (= G353), G395 (= G376)
- binding tetrafluoroaluminate ion: K214 (= K197), G371 (= G352), G372 (= G353), G394 (= G375)
- binding l-adenosine-5'-diphosphate: G212 (= G195), A213 (≠ S196), F290 (= F272), N335 (= N316), G339 (= G320), V340 (= V321), E342 (= E323), G371 (= G352), G372 (= G353), D373 (= D354), T374 (≠ S355)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
46% identity, 99% coverage: 3:395/395 of query aligns to 7:413/415 of 1qpgA
- active site: R38 (= R35), K213 (= K197), G371 (= G353), G394 (= G376)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G219), G236 (= G220), N334 (= N316), P336 (= P318), G338 (= G320), V339 (= V321), F340 (= F322), E341 (= E323), G370 (= G352), G371 (= G353), D372 (= D354), T373 (≠ S355)
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
42% identity, 99% coverage: 2:393/395 of query aligns to 3:412/415 of 16pkA
- active site: R35 (= R35), K215 (= K197), G372 (= G353), G395 (= G376)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G195), A214 (≠ S196), K219 (= K201), A238 (≠ G220), Y241 (≠ F223), L311 (= L293), P336 (= P318), G338 (= G320), V339 (= V321), E341 (= E323), G393 (= G374), G394 (= G375), G395 (= G376)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
42% identity, 99% coverage: 2:393/395 of query aligns to 3:412/415 of 13pkA
- active site: R35 (= R35), K215 (= K197), G372 (= G353), G395 (= G376)
- binding adenosine-5'-diphosphate: G213 (= G195), A214 (≠ S196), K219 (= K201), L311 (= L293), P336 (= P318), G338 (= G320), V339 (= V321), E341 (= E323), G371 (= G352), D373 (= D354), S374 (= S355)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
45% identity, 99% coverage: 3:393/395 of query aligns to 8:414/417 of 4o33A
- active site: R39 (= R35), K216 (= K197), G374 (= G353), G397 (= G376)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G219), G239 (= G220), T255 (≠ N235), L257 (≠ I237), F292 (= F272), M312 (≠ Q291), G313 (= G292), L314 (= L293), G341 (= G320), V342 (= V321)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
45% identity, 99% coverage: 3:393/395 of query aligns to 6:402/405 of 2wzdA
- active site: R37 (= R35), K204 (= K197), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (≠ S196), K204 (= K197), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (= V321), E332 (= E323), G361 (= G352), D363 (= D354), T364 (≠ S355)
- binding aluminum fluoride: R37 (= R35), K204 (= K197), G361 (= G352), G362 (= G353), G384 (= G375)
Query Sequence
>WP_078210855.1 NCBI__GCF_002017945.1:WP_078210855.1
MRTLNDFNFKDKKAIIRVDFNVPLDENFNVTDANRIEAAKPTIDKILADGGSVILMSHLG
RPKGAEDKYSLRHIVAKVSEVFGVPVQFASDCIGEPATTAAANLQPGQVLLLENLRFYKE
EEAGDVDFAKQLAALGDIYVNDAFGTAHRAHASTTIIAQFFATSKCFGTLLAKEIESLNK
VLKNSEKPVTAVLGGSKVSSKITVIENILDKVDHMIIGGGMTFTFVKALGGSVGNSICED
DKQELALEILRLAKEKGVQIHIPVDVVAADDFSNTANTQIVDVKAIPDGWQGLDAGPKSL
ANFKEVILASKTILWNGPLGVFEMPTFAAGTIALGDYIAEATANGAFSLVGGGDSVAAVK
QFGFEEKMSYVSTGGGAMLEMLEGRTLPGIAAILE
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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