SitesBLAST
Comparing WP_013706916.1 NCBI__GCF_000195295.1:WP_013706916.1 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)
49% identity, 98% coverage: 2:391/399 of query aligns to 4:393/394 of 1phpA
- active site: R36 (= R35), K197 (= K196), G351 (= G349), G374 (= G372)
- binding adenosine-5'-diphosphate: G195 (= G194), K201 (= K200), G219 (= G218), G220 (≠ A219), L237 (= L236), N316 (= N315), P318 (= P317), G320 (= G319), V321 (≠ A320), E323 (= E322), G350 (= G348), D352 (= D350), S353 (≠ T351)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
49% identity, 98% coverage: 2:391/399 of query aligns to 4:393/394 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)
48% identity, 98% coverage: 4:394/399 of query aligns to 6:399/654 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)
49% identity, 97% coverage: 4:389/399 of query aligns to 5:393/398 of 1vpeA
- active site: R35 (= R35), K196 (= K196), G353 (= G349), G376 (= G372)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G194), A195 (= A195), K196 (= K196), K200 (= K200), G218 (= G218), A219 (= A219), N316 (= N315), P318 (= P317), G320 (= G319), V321 (≠ A320), E323 (= E322), G352 (= G348), G353 (= G349), D354 (= D350), S355 (≠ T351)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
48% identity, 98% coverage: 2:391/399 of query aligns to 4:393/394 of P40924
- S183 (≠ E182) modified: Phosphoserine
- T299 (≠ S298) modified: Phosphothreonine
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
48% identity, 97% coverage: 4:391/399 of query aligns to 9:414/416 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 (= A195) binding ATP
- K214 (= K196) binding ATP
- L312 (≠ A292) binding ATP
- N335 (= N315) binding covalent
- E342 (= E322) binding ATP
- G371 (= G348) binding (2R)-3-phosphoglycerate
- D373 (= D350) binding covalent; binding Mg(2+)
- G394 (= G371) binding (2R)-3-phosphoglycerate
- G395 (= G372) binding (2R)-3-phosphoglycerate
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
47% identity, 97% coverage: 4:391/399 of query aligns to 8:413/415 of 3pgkA
- active site: R38 (= R35), K213 (= K196), G371 (= G349), G394 (= G372)
- binding adenosine-5'-triphosphate: G211 (= G194), A212 (= A195), K213 (= K196), F289 (≠ L271), L311 (≠ A292), N334 (= N315), G335 (= G316), P336 (= P317), G338 (= G319), V339 (≠ A320), D372 (= D350)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
47% identity, 97% coverage: 4:391/399 of query aligns to 8:413/415 of 1qpgA
- active site: R38 (= R35), K213 (= K196), G371 (= G349), G394 (= G372)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G218), G236 (≠ A219), N334 (= N315), P336 (= P317), G338 (= G319), V339 (≠ A320), F340 (= F321), E341 (= E322), G370 (= G348), G371 (= G349), D372 (= D350), T373 (= T351)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
47% identity, 97% coverage: 4:389/399 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R35), K204 (= K196), G362 (= G349), G385 (= G372)
- binding adenosine-5'-diphosphate: G202 (= G194), A203 (= A195), K204 (= K196), K208 (= K200), G226 (= G218), G227 (≠ A219), N325 (= N315), P327 (= P317), G329 (= G319), V330 (≠ A320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (= T351)
- binding tetrafluoroaluminate ion: R37 (= R35), K204 (= K196), K208 (= K200), G361 (= G348), G362 (= G349), G384 (= G371)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
47% identity, 97% coverage: 4:389/399 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R35), K204 (= K196), G362 (= G349), G385 (= G372)
- binding adenosine-5'-diphosphate: G202 (= G194), A203 (= A195), K204 (= K196), K208 (= K200), G226 (= G218), G227 (≠ A219), N325 (= N315), P327 (= P317), G329 (= G319), V330 (≠ A320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (= T351)
- binding trifluoromagnesate: K204 (= K196), K208 (= K200), G361 (= G348), G384 (= G371), G385 (= G372)
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
46% identity, 97% coverage: 4:389/399 of query aligns to 7:412/414 of 2y3iA
- active site: R37 (= R35), K214 (= K196), G372 (= G349), G395 (= G372)
- binding tetrafluoroaluminate ion: K214 (= K196), G371 (= G348), G372 (= G349), G394 (= G371)
- binding l-adenosine-5'-diphosphate: G212 (= G194), A213 (= A195), F290 (≠ L271), N335 (= N315), G339 (= G319), V340 (≠ A320), E342 (= E322), G371 (= G348), G372 (= G349), D373 (= D350), T374 (= T351)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
47% identity, 97% coverage: 4:389/399 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R35), K207 (= K196), G365 (= G349), G388 (= G372)
- binding adenosine-5'-diphosphate: G205 (= G194), A206 (= A195), K207 (= K196), K211 (= K200), G229 (= G218), G230 (≠ A219), N328 (= N315), P330 (= P317), G332 (= G319), V333 (≠ A320), E335 (= E322), G364 (= G348), G365 (= G349), D366 (= D350), T367 (= T351)
- binding adenosine-5'-triphosphate: G205 (= G194), A206 (= A195), K207 (= K196), K211 (= K200), G229 (= G218), G230 (≠ A219), N328 (= N315), G332 (= G319), V333 (≠ A320), E335 (= E322), G364 (= G348), G365 (= G349), D366 (= D350), T367 (= T351), G387 (= G371), G388 (= G372)
- binding 1,3-bisphosphoglyceric acid: D22 (= D19), N24 (= N21), R37 (= R35), H61 (= H58), R64 (= R61), R121 (= R116), R162 (= R149), K207 (= K196), K211 (= K200), G364 (= G348), G387 (= G371), G388 (= G372)
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)
46% identity, 97% coverage: 4:389/399 of query aligns to 9:414/417 of P00558
- V23 (= V18) binding (2R)-3-phosphoglycerate
- F25 (= F20) binding (2R)-3-phosphoglycerate
- Q38 (≠ T34) binding (2R)-3-phosphoglycerate
- QRIKAA 38:43 (≠ TRIRAV 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 (= L81) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ P90) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- L122 (= L115) binding (2R)-3-phosphoglycerate
- K131 (≠ N124) modified: N6-malonyllysine; alternate
- G158 (≠ V136) 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 (≠ R171) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- S203 (≠ D183) modified: Phosphoserine; by MAPK1
- R206 (= R186) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- G214 (= G194) binding ADP; binding CDP
- A215 (= A195) binding Mg(2+)
- K216 (= K196) modified: N6-(2-hydroxyisobutyryl)lysine
- A218 (≠ S198) binding Mg(2+)
- D219 (≠ S199) binding CDP; binding Mg(2+)
- K220 (= K200) modified: N6-(2-hydroxyisobutyryl)lysine
- G238 (= G218) binding ADP; binding CDP
- E252 (≠ Q231) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A245) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ E247) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D264) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- D315 (= D293) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I294) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ L301) modified: N6-(2-hydroxyisobutyryl)lysine
- G338 (= G316) binding CDP
- V340 (≠ M318) binding CDP
- F343 (= F321) binding ADP; binding CDP
- T352 (= T330) to N: in dbSNP:rs137852530
- T378 (≠ V353) mutation to P: Loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride (see paper)
47% identity, 97% coverage: 4:389/399 of query aligns to 7:404/407 of 4axxA
- active site: R37 (= R35), K206 (= K196), G364 (= G349), G387 (= G372)
- binding adenosine-5'-diphosphate: G204 (= G194), A205 (= A195), K210 (= K200), G228 (= G218), G229 (≠ A219), N327 (= N315), P329 (= P317), G331 (= G319), V332 (≠ A320), E334 (= E322), G363 (= G348), G364 (= G349), D365 (= D350), T366 (= T351)
- binding beryllium trifluoride ion: K206 (= K196), K210 (= K200), G363 (= G348)
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
46% identity, 97% coverage: 4:389/399 of query aligns to 8:413/416 of 5m1rA
- active site: R38 (= R35), K215 (= K196), G373 (= G349), G396 (= G372)
- binding adenosine-5'-diphosphate: G213 (= G194), A214 (= A195), K219 (= K200), G237 (= G218), G238 (≠ A219), L256 (= L236), G340 (= G319), V341 (≠ A320), E343 (= E322), D374 (= D350), T375 (= T351)
- binding magnesium ion: R150 (≠ A129), A151 (≠ R130), G372 (= G348), T375 (= T351)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
46% identity, 97% coverage: 4:389/399 of query aligns to 8:413/416 of 1vjcA
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
47% identity, 97% coverage: 4:389/399 of query aligns to 7:402/405 of 2wzdA
- active site: R37 (= R35), K204 (= K196), G362 (= G349), G385 (= G372)
- binding adenosine-5'-diphosphate: G202 (= G194), A203 (= A195), K204 (= K196), G226 (= G218), G227 (≠ A219), N325 (= N315), P327 (= P317), G329 (= G319), V330 (≠ A320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (= T351)
- binding aluminum fluoride: R37 (= R35), K204 (= K196), G361 (= G348), G362 (= G349), G384 (= G371)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
46% identity, 97% coverage: 4:389/399 of query aligns to 9:414/417 of 4o33A
- active site: R39 (= R35), K216 (= K196), G374 (= G349), G397 (= G372)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G218), G239 (≠ A219), T255 (≠ K234), L257 (= L236), F292 (≠ L271), M312 (≠ I290), G313 (≠ I291), L314 (≠ A292), G341 (= G319), V342 (≠ A320)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
45% identity, 97% coverage: 4:389/399 of query aligns to 9:414/417 of P09041
- D24 (= D19) binding (2R)-3-phosphoglycerate
- N26 (= N21) binding (2R)-3-phosphoglycerate
- R39 (= R35) binding (2R)-3-phosphoglycerate
- H63 (= H58) binding (2R)-3-phosphoglycerate
- R66 (= R61) binding (2R)-3-phosphoglycerate
- R123 (= R116) binding (2R)-3-phosphoglycerate
- R171 (= R149) binding (2R)-3-phosphoglycerate
- A215 (= A195) binding ATP
- K220 (= K200) binding ATP
- G239 (≠ A219) binding ATP
- G313 (≠ I291) binding ATP
- E344 (= E322) binding ATP
- D375 (= D350) binding ATP
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
45% identity, 97% coverage: 4:391/399 of query aligns to 6:388/392 of 4feyA
- active site: R36 (= R35), K193 (= K196), G346 (= G349), G369 (= G372)
- binding adenosine-5'-diphosphate: G191 (= G194), S192 (≠ A195), K197 (= K200), G215 (= G218), G316 (= G319), V317 (≠ A320), E319 (= E322), D347 (= D350)
Query Sequence
>WP_013706916.1 NCBI__GCF_000195295.1:WP_013706916.1
MKYLQDVDIREKTVFIRVDFNVPLDRNRNITDDTRIRAVLPTINHCLDEHARVILASHLG
RPKGPDPNKSLEPVSRRLSRLIHKTVEFVPDCIGPEVQKIKQKMQPGDVLLLENLRFYPE
EEKNDQDFARQLMEGVDVYINDAFAVGHRAHASVHAVTLFAPICAAGFLLRDEILYFHKS
MEDPARPLVAIIGGAKISSKLTALINLLKHVDKLIIGGAMANTFIKAMGYQVGKSLVDDS
LLDEAKELMSTALQKGVKFYLPVDVIVADSLDNRAENRVTTIQEVPADWIIADIGPASIT
LFNEALQDARTVVWNGPMGAFEIEAFSRGTLAMVHNVANSFALTIVGGGDTDVAIHKAGE
VNKFSYISTGGGAFLELLEGKKLPGILALEEWHKKHQSA
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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