SitesBLAST
Comparing WP_013459152.1 NCBI__GCF_000183725.1:WP_013459152.1 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)
50% identity, 99% coverage: 1:391/396 of query aligns to 1:391/654 of P36204
- R36 (= R37) binding substrate
- R118 (= R119) binding substrate
- R151 (= R152) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
51% identity, 98% coverage: 4:391/396 of query aligns to 3:390/398 of 1vpeA
- active site: R35 (= R37), K196 (= K201), G353 (= G354), G376 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G199), A195 (≠ S200), K196 (= K201), K200 (= K205), G218 (= G223), A219 (≠ G224), N316 (= N320), P318 (= P322), G320 (= G324), V321 (= V325), E323 (= E327), G352 (= G353), G353 (= G354), D354 (= D355), S355 (≠ T356)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
51% identity, 99% coverage: 1:394/396 of query aligns to 1:391/394 of 1phpA
- active site: R36 (= R37), K197 (= K201), G351 (= G354), G374 (= G377)
- binding adenosine-5'-diphosphate: G195 (= G199), K201 (= K205), G219 (= G223), G220 (= G224), L237 (= L241), N316 (= N320), P318 (= P322), G320 (= G324), V321 (= V325), E323 (= E327), G350 (= G353), D352 (= D355), S353 (≠ T356)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
51% identity, 99% coverage: 1:394/396 of query aligns to 1:391/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
49% identity, 99% coverage: 1:394/396 of query aligns to 1:391/394 of P40924
- S183 (≠ E187) modified: Phosphoserine
- T299 (= T303) modified: Phosphothreonine
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
46% identity, 98% coverage: 4:391/396 of query aligns to 6:408/415 of 3pgkA
- active site: R38 (= R37), K213 (= K201), G371 (= G354), G394 (= G377)
- binding adenosine-5'-triphosphate: G211 (= G199), A212 (≠ S200), K213 (= K201), F289 (= F276), L311 (= L297), N334 (= N320), G335 (= G321), P336 (= P322), G338 (= G324), V339 (= V325), D372 (= D355)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
46% identity, 98% coverage: 4:391/396 of query aligns to 7:409/416 of P00560
- R22 (= R19) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R37) binding substrate
- R122 (= R119) binding substrate
- R169 (= R152) binding substrate
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
46% identity, 98% coverage: 4:391/396 of query aligns to 6:408/415 of 1qpgA
- active site: R38 (= R37), K213 (= K201), G371 (= G354), G394 (= G377)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G223), G236 (= G224), N334 (= N320), P336 (= P322), G338 (= G324), V339 (= V325), F340 (≠ Y326), E341 (= E327), G370 (= G353), G371 (= G354), D372 (= D355), T373 (= T356)
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
45% identity, 99% coverage: 1:394/396 of query aligns to 1:386/392 of 4feyA
- active site: R36 (= R37), K193 (= K201), G346 (= G354), G369 (= G377)
- binding adenosine-5'-diphosphate: G191 (= G199), S192 (= S200), K197 (= K205), G215 (= G223), G316 (= G324), V317 (= V325), E319 (= E327), D347 (= D355)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 99% coverage: 4:394/396 of query aligns to 5:404/407 of 4axxA
- active site: R37 (= R37), K206 (= K201), G364 (= G354), G387 (= G377)
- binding adenosine-5'-diphosphate: G204 (= G199), A205 (≠ S200), K210 (= K205), G228 (= G223), G229 (= G224), N327 (= N320), P329 (= P322), G331 (= G324), V332 (= V325), E334 (= E327), G363 (= G353), G364 (= G354), D365 (= D355), T366 (= T356)
- binding beryllium trifluoride ion: K206 (= K201), K210 (= K205), G363 (= G353)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
43% identity, 99% coverage: 4:394/396 of query aligns to 7:414/417 of P09041
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
43% identity, 99% coverage: 4:394/396 of query aligns to 3:410/413 of 2paaA
- active site: R35 (= R37), K212 (= K201), G370 (= G354), G393 (= G377)
- binding adenosine-5'-triphosphate: G210 (= G199), A211 (≠ S200), K216 (= K205), G235 (= G224), L253 (= L241), G309 (= G296), L310 (= L297), G334 (= G321), G337 (= G324), V338 (= V325), E340 (= E327), D371 (= D355)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 99% coverage: 4:394/396 of query aligns to 7:411/414 of O60101
- Y75 (= Y72) modified: Phosphotyrosine
- S76 (= S73) modified: Phosphoserine
- S143 (= S132) modified: Phosphoserine
- S172 (≠ A155) modified: Phosphoserine
- S173 (= S156) modified: Phosphoserine
- S183 (≠ A171) modified: Phosphoserine
- S253 (= S240) modified: Phosphoserine
- S260 (≠ I247) modified: Phosphoserine
- T299 (≠ S286) modified: Phosphothreonine
- S328 (≠ V314) modified: Phosphoserine
- S351 (≠ K337) modified: Phosphoserine
- T373 (= T356) modified: Phosphothreonine
- S387 (≠ T370) modified: Phosphoserine
- S390 (= S373) modified: Phosphoserine
Sites not aligning to the query:
- 412 modified: Phosphoserine
- 413 modified: Phosphoserine
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: 4:394/396 of query aligns to 5:402/405 of 2wzcA
- active site: R37 (= R37), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (≠ S200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (= T356)
- binding tetrafluoroaluminate ion: R37 (= R37), K204 (= K201), K208 (= K205), G361 (= G353), G362 (= G354), G384 (= G376)
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: 4:394/396 of query aligns to 5:402/405 of 2wzbA
- active site: R37 (= R37), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (≠ S200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (= T356)
- binding trifluoromagnesate: K204 (= K201), K208 (= K205), G361 (= G353), G384 (= G376), G385 (= G377)
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: 4:394/396 of query aligns to 5:402/405 of 2wzdA
- active site: R37 (= R37), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (≠ S200), K204 (= K201), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (= T356)
- binding aluminum fluoride: R37 (= R37), K204 (= K201), G361 (= G353), G362 (= G354), G384 (= G376)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 99% coverage: 4:394/396 of query aligns to 5:405/408 of 2x15A
- active site: R37 (= R37), K207 (= K201), G365 (= G354), G388 (= G377)
- binding adenosine-5'-diphosphate: G205 (= G199), A206 (≠ S200), K207 (= K201), K211 (= K205), G229 (= G223), G230 (= G224), N328 (= N320), P330 (= P322), G332 (= G324), V333 (= V325), E335 (= E327), G364 (= G353), G365 (= G354), D366 (= D355), T367 (= T356)
- binding adenosine-5'-triphosphate: G205 (= G199), A206 (≠ S200), K207 (= K201), K211 (= K205), G229 (= G223), G230 (= G224), N328 (= N320), G332 (= G324), V333 (= V325), E335 (= E327), G364 (= G353), G365 (= G354), D366 (= D355), T367 (= T356), G387 (= G376), G388 (= G377)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R37), H61 (= H60), R64 (= R63), R121 (= R119), R162 (= R152), K207 (= K201), K211 (= K205), G364 (= G353), G387 (= G376), G388 (= G377)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
42% identity, 99% coverage: 4:394/396 of query aligns to 6:413/416 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, 99% coverage: 4:394/396 of query aligns to 5:412/414 of 2y3iA
- active site: R37 (= R37), K214 (= K201), G372 (= G354), G395 (= G377)
- binding tetrafluoroaluminate ion: K214 (= K201), G371 (= G353), G372 (= G354), G394 (= G376)
- binding l-adenosine-5'-diphosphate: G212 (= G199), A213 (≠ S200), F290 (= F276), N335 (= N320), G339 (= G324), V340 (= V325), E342 (= E327), G371 (= G353), G372 (= G354), D373 (= D355), T374 (= T356)
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, 99% coverage: 4:394/396 of query aligns to 7:414/417 of P00558
- DFN 24:26 (= DFN 21:23) binding substrate
- R39 (= R37) binding substrate
- HLGR 63:66 (≠ HFGR 60:63) binding substrate
- L88 (= L84) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ D93) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R119) binding substrate
- K131 (≠ N127) modified: N6-malonyllysine; alternate
- G158 (≠ A139) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D145) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R152) binding substrate
- K191 (≠ Q176) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R191) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K201) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K205) binding ATP; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ D236) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A250) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ K252) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D269) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (= G296) binding ATP
- D315 (= D298) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I299) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ L306) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E327) binding ATP
- T352 (≠ S335) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 353:356) binding ATP
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_013459152.1 NCBI__GCF_000183725.1:WP_013459152.1
MQLLGIKECDIHGKKVFIRCDFNVPMDDYGNITDDRRIRSALATINYCLDQKCAIILASH
FGRPKGEPDEKYSLAPIARRLHQLLKIDVQVADDVVGESALKLAHELKNGEVLLLENLRF
EKGETKNDPDLSAALASMAEVYINDAFGVSHRAHASVEGITAHFDNAHKAAGFLLQKEIQ
FFGTLLEHPVRPFAAIVGGSKVSGKLEALINLLPKVDKMLIGGGMAFTFLKALGHDVGNS
LVEDDLIPEALKIMEEAKRLGVKFYLPVDVVAAEKFAPDSASRLCSVQEIPSGWMGLDIG
PATVRLYRQVLGDVQTILWNGPMGVYEMDRYARGSNKIAHFVADSYATSVVGGGDTADLV
QRVGLDEEITFISTGGGASLELLEGKILPGVKPLLK
Or try a new SitesBLAST search
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