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Comparing WP_035076104.1 NCBI__GCF_000425265.1:WP_035076104.1 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)
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
49% identity, 97% coverage: 6:394/399 of query aligns to 5:394/398 of 1vpeA
- active site: R35 (= R36), K196 (= K202), G353 (= G353), G376 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G200), A195 (= A201), K196 (= K202), K200 (= K206), G218 (= G224), A219 (= A225), N316 (= N319), P318 (= P321), G320 (= G323), V321 (≠ L324), E323 (= E326), G352 (= G352), G353 (= G353), D354 (= D354), S355 (≠ T355)
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)
49% identity, 97% coverage: 6:393/399 of query aligns to 6:394/654 of P36204
- R36 (= R36) binding
- R118 (= R118) binding
- R151 (= R155) binding
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
46% identity, 99% coverage: 1:395/399 of query aligns to 1:393/394 of 1phpA
- active site: R36 (= R36), K197 (= K202), G351 (= G353), G374 (= G376)
- binding adenosine-5'-diphosphate: G195 (= G200), K201 (= K206), G219 (= G224), G220 (≠ A225), L237 (= L242), N316 (= N319), P318 (= P321), G320 (= G323), V321 (≠ L324), E323 (= E326), G350 (= G352), D352 (= D354), S353 (≠ T355)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
46% identity, 99% coverage: 1:395/399 of query aligns to 1:393/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
44% identity, 99% coverage: 1:395/399 of query aligns to 1:393/394 of P40924
- S183 (≠ K188) modified: Phosphoserine
- T299 (≠ S302) modified: Phosphothreonine
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
46% identity, 97% coverage: 9:395/399 of query aligns to 9:388/392 of 4feyA
- active site: R36 (= R36), K193 (= K202), G346 (= G353), G369 (= G376)
- binding adenosine-5'-diphosphate: G191 (= G200), S192 (≠ A201), K197 (= K206), G215 (= G224), G316 (= G323), V317 (≠ L324), E319 (= E326), D347 (= D354)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
44% identity, 98% coverage: 6:395/399 of query aligns to 9:414/416 of P00560
- R22 (= R19) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R36) binding
- R122 (= R118) binding
- R169 (= R155) binding
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
45% identity, 97% coverage: 6:393/399 of query aligns to 7:404/407 of 4axxA
- active site: R37 (= R36), K206 (= K202), G364 (= G353), G387 (= G376)
- binding adenosine-5'-diphosphate: G204 (= G200), A205 (= A201), K210 (= K206), G228 (= G224), G229 (≠ A225), N327 (= N319), P329 (= P321), G331 (= G323), V332 (≠ L324), E334 (= E326), G363 (= G352), G364 (= G353), D365 (= D354), T366 (= T355)
- binding beryllium trifluoride ion: K206 (= K202), K210 (= K206), G363 (= G352)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
44% identity, 98% coverage: 6:395/399 of query aligns to 8:413/415 of 1qpgA
- active site: R38 (= R36), K213 (= K202), G371 (= G353), G394 (= G376)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G224), G236 (≠ A225), N334 (= N319), P336 (= P321), G338 (= G323), V339 (≠ L324), F340 (= F325), E341 (= E326), G370 (= G352), G371 (= G353), D372 (= D354), T373 (= T355)
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
44% identity, 97% coverage: 6:393/399 of query aligns to 7:412/414 of 2y3iA
- active site: R37 (= R36), K214 (= K202), G372 (= G353), G395 (= G376)
- binding tetrafluoroaluminate ion: K214 (= K202), G371 (= G352), G372 (= G353), G394 (= G375)
- binding l-adenosine-5'-diphosphate: G212 (= G200), A213 (= A201), F290 (≠ I277), N335 (= N319), G339 (= G323), V340 (≠ L324), E342 (= E326), G371 (= G352), G372 (= G353), D373 (= D354), T374 (= T355)
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)
44% identity, 97% coverage: 6:393/399 of query aligns to 9:414/417 of P00558
- DFN 24:26 (= DFN 21:23) binding
- R39 (= R36) binding
- HLGR 63:66 (≠ HLGK 59:62) binding
- L88 (≠ Y83) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ P92) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R118) binding
- K131 (= K126) modified: N6-malonyllysine; alternate
- G158 (≠ A142) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D148) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R155) binding
- K191 (= K177) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R192) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K202) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K206) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ D237) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A251) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ K253) 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
- G313 (≠ L295) binding
- D315 (= D297) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I298) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (= K305) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E326) binding
- T352 (≠ S334) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 352:355) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
45% identity, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R36), K204 (= K202), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (≠ A225), N325 (= N319), P327 (= P321), G329 (= G323), V330 (≠ L324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K202), K208 (= K206), 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)
45% identity, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R36), K204 (= K202), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), K208 (= K206), G226 (= G224), G227 (≠ A225), N325 (= N319), P327 (= P321), G329 (= G323), V330 (≠ L324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding trifluoromagnesate: K204 (= K202), K208 (= K206), G361 (= G352), G384 (= G375), G385 (= G376)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
44% identity, 97% coverage: 6:393/399 of query aligns to 9:414/417 of 4o33A
- active site: R39 (= R36), K216 (= K202), G374 (= G353), G397 (= G376)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G224), G239 (≠ A225), T255 (≠ K240), L257 (= L242), F292 (≠ I277), M312 (= M294), G313 (≠ L295), L314 (= L296), G341 (= G323), V342 (≠ L324)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
43% identity, 97% coverage: 6:393/399 of query aligns to 8:413/416 of 1kf0A
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 97% coverage: 6:393/399 of query aligns to 9:411/414 of O60101
- Y75 (≠ L71) modified: Phosphotyrosine
- S76 (= S72) modified: Phosphoserine
- S143 (≠ K126) modified: Phosphoserine
- S172 (≠ A158) modified: Phosphoserine
- S173 (= S159) modified: Phosphoserine
- S183 (≠ A172) modified: Phosphoserine
- S253 (= S241) modified: Phosphoserine
- S260 (≠ V248) modified: Phosphoserine
- T299 (≠ C284) modified: Phosphothreonine
- S328 (≠ A313) modified: Phosphoserine
- S351 (vs. gap) modified: Phosphoserine
- T373 (= T355) modified: Phosphothreonine
- S387 (= S369) modified: Phosphoserine
- S390 (= S372) modified: Phosphoserine
Sites not aligning to the query:
- 412 modified: Phosphoserine
- 413 modified: Phosphoserine
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
44% identity, 97% coverage: 6:393/399 of query aligns to 8:413/416 of 1vjcA
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
45% identity, 97% coverage: 6:393/399 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R36), K207 (= K202), G365 (= G353), G388 (= G376)
- binding adenosine-5'-diphosphate: G205 (= G200), A206 (= A201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (≠ A225), N328 (= N319), P330 (= P321), G332 (= G323), V333 (≠ L324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355)
- binding adenosine-5'-triphosphate: G205 (= G200), A206 (= A201), K207 (= K202), K211 (= K206), G229 (= G224), G230 (≠ A225), N328 (= N319), G332 (= G323), V333 (≠ L324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355), G387 (= G375), G388 (= G376)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R36), H61 (= H59), R64 (≠ K62), R121 (= R118), R162 (= R155), K207 (= K202), K211 (= K206), G364 (= G352), G387 (= G375), G388 (= G376)
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, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzdA
- active site: R37 (= R36), K204 (= K202), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G200), A203 (= A201), K204 (= K202), G226 (= G224), G227 (≠ A225), N325 (= N319), P327 (= P321), G329 (= G323), V330 (≠ L324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding aluminum fluoride: R37 (= R36), K204 (= K202), G361 (= G352), G362 (= G353), G384 (= G375)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
43% identity, 97% coverage: 7:393/399 of query aligns to 18:421/424 of 1ltkC
- active site: R47 (= R36), K223 (= K202), G381 (= G353), G404 (= G376)
- binding adenosine monophosphate: G221 (= G200), A222 (= A201), K223 (= K202), G245 (= G224), G246 (≠ A225), G348 (= G323), V349 (≠ L324), E351 (= E326), D382 (= D354)
Query Sequence
>WP_035076104.1 NCBI__GCF_000425265.1:WP_035076104.1
MIMRFIDQLDIAGKKLLMRVDFNVPLDGETITDDNRIKAAVPTIRYALEQGAAIIVMAHL
GKPKGKRVEELSLKPVAKRLGEYLDMEVTLAPDCIGAEVEKMAAGLKAGQVMMLENLRFH
AEEQAKTVEERGDFGAKLAALADIYVNDAFGVAHRPNASVVDVPYAAKQCCAGFLLKLEW
EYLGEALKNPKRPYIAVSGGAKVSSKLGILNNLIGKVDHFIIGGAMANTFLLAQGKDVGK
SLVEASLVDTAKKIITKAEGSGTTLHLPVDFIWGKDIENAGGICDADNVPTDGMLLDIGP
VSAQKFCDVIKEAKTIVWNGPMGLFEQPAFAEGSLKVCKAMADSDGTTIVGGGDTDAVVH
QAGLADKFSFISTGGGSFLEFLEGKELPAFKALKENIDK
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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