SitesBLAST
Comparing WP_025274821.1 NCBI__GCF_000527155.1:WP_025274821.1 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)
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)
53% identity, 96% coverage: 12:393/398 of query aligns to 11:391/654 of P36204
- R36 (= R37) binding substrate
- R118 (= R119) binding substrate
- R151 (= R156) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
52% identity, 96% coverage: 12:393/398 of query aligns to 10:390/398 of 1vpeA
- active site: R35 (= R37), K196 (= K202), G353 (= G355), G376 (= G379)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G200), A195 (= A201), K196 (= K202), K200 (= K206), G218 (= G224), A219 (≠ G225), N316 (= N321), P318 (= P323), G320 (= G325), V321 (= V326), E323 (= E328), G352 (= G354), G353 (= G355), D354 (= D356), S355 (= S357)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
52% identity, 97% coverage: 12:398/398 of query aligns to 11:393/394 of P40924
- S183 (≠ G188) modified: Phosphoserine
- T299 (≠ S304) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
51% identity, 97% coverage: 12:398/398 of query aligns to 11:393/394 of 1phpA
- active site: R36 (= R37), K197 (= K202), G351 (= G355), G374 (= G379)
- binding adenosine-5'-diphosphate: G195 (= G200), K201 (= K206), G219 (= G224), G220 (= G225), L237 (= L242), N316 (= N321), P318 (= P323), G320 (= G325), V321 (= V326), E323 (= E328), G350 (= G354), D352 (= D356), S353 (= S357)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
51% identity, 97% coverage: 12:398/398 of query aligns to 11:393/394 of P18912
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
45% identity, 96% coverage: 15:397/398 of query aligns to 14:387/392 of 4feyA
- active site: R36 (= R37), K193 (= K202), G346 (= G355), G369 (= G379)
- binding adenosine-5'-diphosphate: G191 (= G200), S192 (≠ A201), K197 (= K206), G215 (= G224), G316 (= G325), V317 (= V326), E319 (= E328), D347 (= D356)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
43% identity, 99% coverage: 3:398/398 of query aligns to 6:404/405 of 2wzcA
- active site: R37 (= R37), K204 (= K202), G362 (= G355), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding tetrafluoroaluminate ion: R37 (= R37), K204 (= K202), K208 (= K206), G361 (= G354), G362 (= G355), G384 (= G378)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
43% identity, 99% coverage: 3:398/398 of query aligns to 6:404/405 of 2wzbA
- active site: R37 (= R37), K204 (= K202), G362 (= G355), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding trifluoromagnesate: K204 (= K202), K208 (= K206), G361 (= G354), G384 (= G378), G385 (= G379)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
43% identity, 99% coverage: 3:398/398 of query aligns to 8:416/417 of P09041
- D24 (= D22) binding (2R)-3-phosphoglycerate
- N26 (= N24) binding (2R)-3-phosphoglycerate
- R39 (= R37) binding (2R)-3-phosphoglycerate
- H63 (= H60) binding (2R)-3-phosphoglycerate
- R66 (= R63) binding (2R)-3-phosphoglycerate
- R123 (= R119) binding (2R)-3-phosphoglycerate
- R171 (= R156) binding (2R)-3-phosphoglycerate
- A215 (= A201) binding ATP
- K220 (= K206) binding ATP
- G239 (= G225) binding ATP
- G313 (= G297) binding ATP
- E344 (= E328) binding ATP
- D375 (= D356) binding ATP
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
43% identity, 99% coverage: 3:398/398 of query aligns to 4:412/413 of 2paaA
- active site: R35 (= R37), K212 (= K202), G370 (= G355), G393 (= G379)
- binding adenosine-5'-triphosphate: G210 (= G200), A211 (= A201), K216 (= K206), G235 (= G225), L253 (= L242), G309 (= G297), L310 (= L298), G334 (= G322), G337 (= G325), V338 (= V326), E340 (= E328), D371 (= D356)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride (see paper)
43% identity, 99% coverage: 3:398/398 of query aligns to 6:406/407 of 4axxA
- active site: R37 (= R37), K206 (= K202), G364 (= G355), G387 (= G379)
- binding adenosine-5'-diphosphate: G204 (= G200), A205 (= A201), K210 (= K206), G228 (= G224), G229 (= G225), N327 (= N321), P329 (= P323), G331 (= G325), V332 (= V326), E334 (= E328), G363 (= G354), G364 (= G355), D365 (= D356), T366 (≠ S357)
- binding beryllium trifluoride ion: K206 (= K202), K210 (= K206), G363 (= G354)
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, 99% coverage: 3:398/398 of query aligns to 6:404/405 of 2wzdA
- active site: R37 (= R37), K204 (= K202), G362 (= G355), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), G226 (= G224), G227 (= G225), N325 (= N321), P327 (= P323), G329 (= G325), V330 (= V326), E332 (= E328), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding aluminum fluoride: R37 (= R37), K204 (= K202), G361 (= G354), G362 (= G355), G384 (= G378)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 99% coverage: 3:398/398 of query aligns to 6:407/408 of 2x15A
- active site: R37 (= R37), K207 (= K202), G365 (= G355), G388 (= G379)
- binding adenosine-5'-diphosphate: G205 (= G200), A206 (= A201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (= G225), N328 (= N321), P330 (= P323), G332 (= G325), V333 (= V326), E335 (= E328), G364 (= G354), G365 (= G355), D366 (= D356), T367 (≠ S357)
- binding adenosine-5'-triphosphate: G205 (= G200), A206 (= A201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (= G225), N328 (= N321), G332 (= G325), V333 (= V326), E335 (= E328), G364 (= G354), G365 (= G355), D366 (= D356), T367 (≠ S357), G387 (= G378), G388 (= G379)
- binding 1,3-bisphosphoglyceric acid: D22 (= D22), N24 (= N24), R37 (= R37), H61 (= H60), R64 (= R63), R121 (= R119), R162 (= R156), K207 (= K202), K211 (= K206), G364 (= G354), G387 (= G378), G388 (= G379)
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, 99% coverage: 3:398/398 of query aligns to 6:414/414 of 2y3iA
- active site: R37 (= R37), K214 (= K202), G372 (= G355), G395 (= G379)
- binding tetrafluoroaluminate ion: K214 (= K202), G371 (= G354), G372 (= G355), G394 (= G378)
- binding l-adenosine-5'-diphosphate: G212 (= G200), A213 (= A201), F290 (= F277), N335 (= N321), G339 (= G325), V340 (= V326), E342 (= E328), G371 (= G354), G372 (= G355), D373 (= D356), T374 (≠ S357)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
45% identity, 96% coverage: 15:396/398 of query aligns to 17:412/416 of P00560
- R22 (= R20) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- N26 (= N24) binding (2R)-3-phosphoglycerate
- R39 (= R37) binding (2R)-3-phosphoglycerate
- R122 (= R119) binding (2R)-3-phosphoglycerate
- A213 (= A201) binding ATP
- K214 (= K202) binding ATP
- L312 (= L298) binding ATP
- N335 (= N321) binding covalent
- E342 (= E328) binding ATP
- G371 (= G354) binding (2R)-3-phosphoglycerate
- D373 (= D356) binding covalent; binding Mg(2+)
- G394 (= G378) binding (2R)-3-phosphoglycerate
- G395 (= G379) binding (2R)-3-phosphoglycerate
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)
42% identity, 99% coverage: 3:398/398 of query aligns to 8:416/417 of P00558
- V23 (≠ A21) binding (2R)-3-phosphoglycerate
- F25 (≠ L23) binding (2R)-3-phosphoglycerate
- Q38 (≠ G36) binding (2R)-3-phosphoglycerate
- QRIKAA 38:43 (≠ GRVRAV 36:41) Mitochondrial targeting region exposed following cis-trans isomerization by PIN1 and recognized by the TOM complex for mitochondrial translocation of the protein
- S62 (= S59) binding (2R)-3-phosphoglycerate
- G65 (= G62) binding (2R)-3-phosphoglycerate
- L88 (≠ V84) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ T93) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- L122 (= L118) binding (2R)-3-phosphoglycerate
- K131 (≠ P122) modified: N6-malonyllysine; alternate
- G158 (= G143) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D149) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- H170 (= H155) binding (2R)-3-phosphoglycerate
- K191 (≠ S177) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- S203 (≠ G189) modified: Phosphoserine; by MAPK1
- R206 (≠ K192) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- G214 (= G200) binding ADP; binding CDP
- A215 (= A201) binding Mg(2+)
- K216 (= K202) modified: N6-(2-hydroxyisobutyryl)lysine
- A218 (≠ S204) binding Mg(2+)
- D219 (= D205) binding CDP; binding Mg(2+)
- K220 (= K206) modified: N6-(2-hydroxyisobutyryl)lysine
- G238 (= G224) binding ADP; binding CDP
- E252 (= E237) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ C251) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ R253) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D270) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- D315 (= D299) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I300) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ V307) modified: N6-(2-hydroxyisobutyryl)lysine
- G338 (= G322) binding CDP
- V340 (≠ M324) binding CDP
- F343 (= F327) binding ADP; binding CDP
- T352 (= T336) to N: in dbSNP:rs137852530
- T378 (≠ A359) mutation to P: Loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
41% identity, 97% coverage: 12:398/398 of query aligns to 10:414/415 of 16pkA
- active site: R35 (= R37), K215 (= K202), G372 (= G355), G395 (= G379)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G200), A214 (= A201), K219 (= K206), A238 (≠ G225), Y241 (= Y228), L311 (= L298), P336 (= P323), G338 (= G325), V339 (= V326), E341 (= E328), G393 (= G377), G394 (= G378), G395 (= G379)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
41% identity, 97% coverage: 12:398/398 of query aligns to 10:414/415 of 13pkA
- active site: R35 (= R37), K215 (= K202), G372 (= G355), G395 (= G379)
- binding adenosine-5'-diphosphate: G213 (= G200), A214 (= A201), K219 (= K206), L311 (= L298), P336 (= P323), G338 (= G325), V339 (= V326), E341 (= E328), G371 (= G354), D373 (= D356), S374 (= S357)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
42% identity, 99% coverage: 3:398/398 of query aligns to 7:415/416 of 1kf0A
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
42% identity, 99% coverage: 3:398/398 of query aligns to 8:416/417 of 4o33A
- active site: R39 (= R37), K216 (= K202), G374 (= G355), G397 (= G379)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G224), G239 (= G225), T255 (≠ N240), L257 (= L242), F292 (= F277), M312 (= M296), G313 (= G297), L314 (= L298), G341 (= G325), V342 (= V326)
Query Sequence
>WP_025274821.1 NCBI__GCF_000527155.1:WP_025274821.1
MQTLDELLSEGVSGRRVLLRADLNVPLDGSTITDDGRVRAVAPTIKALADAGARVTVCSH
LGRPKGEPDPQYSLAPVARRLGEVLESTVAFATDTVGDDADEKNAALDDGDVLLLENLRF
NPGETSKNDTQRAEFAGELAAYGDVYVDDAFGAVHRKHASVYDVATMLPHYAGFLISNEV
SVLSRLTGGADKPYVVILGGAKVSDKLAVIENLLSKVDTLIIGGGMAYTFLAAEGHEVGN
SLLEKDQIETCQRYLEEAARLGVELLLPVDVASAAEFSASAEPQVVTADSIPSDRMGLDI
GPDSARVFADRINTAATVFWNGPMGVFEFPEYAKGTKAVAQSLVDSEAFTVVGGGDSAAA
VRTLGLPEDDFGHISTGGGASLEYLEGKTLPGLEVLEN
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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