SitesBLAST
Comparing WP_012852549.1 NCBI__GCF_000024385.1:WP_012852549.1 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)
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)
55% identity, 99% coverage: 3:395/395 of query aligns to 5:396/654 of P36204
- R36 (= R34) binding substrate
- R118 (= R116) binding substrate
- R151 (= R153) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
55% identity, 99% coverage: 3:393/395 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R34), K196 (= K199), G353 (= G352), G376 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G197), A195 (≠ S198), K196 (= K199), K200 (= K203), G218 (= G221), A219 (≠ G222), N316 (= N318), P318 (= P320), G320 (= G322), V321 (= V323), E323 (= E325), G352 (= G351), G353 (= G352), D354 (= D353), S355 (= S354)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
53% identity, 100% coverage: 2:395/395 of query aligns to 4:393/394 of 1phpA
- active site: R36 (= R34), K197 (= K199), G351 (= G352), G374 (= G376)
- binding adenosine-5'-diphosphate: G195 (= G197), K201 (= K203), G219 (= G221), G220 (= G222), L237 (= L239), N316 (= N318), P318 (= P320), G320 (= G322), V321 (= V323), E323 (= E325), G350 (= G351), D352 (= D353), S353 (= S354)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
53% identity, 100% coverage: 2:395/395 of query aligns to 4:393/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
48% identity, 100% coverage: 2:395/395 of query aligns to 4:393/394 of P40924
- S183 (≠ E185) modified: Phosphoserine
- T299 (≠ S301) modified: Phosphothreonine
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
45% identity, 99% coverage: 3:395/395 of query aligns to 6:406/407 of 4axxA
- active site: R37 (= R34), K206 (= K199), G364 (= G352), G387 (= G376)
- binding adenosine-5'-diphosphate: G204 (= G197), A205 (≠ S198), K210 (= K203), G228 (= G221), G229 (= G222), N327 (= N318), P329 (= P320), G331 (= G322), V332 (= V323), E334 (= E325), G363 (= G351), G364 (= G352), D365 (= D353), T366 (≠ S354)
- binding beryllium trifluoride ion: K206 (= K199), K210 (= K203), G363 (= G351)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
45% identity, 99% coverage: 3:395/395 of query aligns to 6:404/405 of 2wzcA
- active site: R37 (= R34), K204 (= K199), G362 (= G352), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G197), A203 (≠ S198), K204 (= K199), K208 (= K203), G226 (= G221), G227 (= G222), N325 (= N318), P327 (= P320), G329 (= G322), V330 (= V323), E332 (= E325), G361 (= G351), D363 (= D353), T364 (≠ S354)
- binding tetrafluoroaluminate ion: R37 (= R34), K204 (= K199), K208 (= K203), G361 (= G351), G362 (= G352), 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, 99% coverage: 3:395/395 of query aligns to 6:404/405 of 2wzbA
- active site: R37 (= R34), K204 (= K199), G362 (= G352), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G197), A203 (≠ S198), K204 (= K199), K208 (= K203), G226 (= G221), G227 (= G222), N325 (= N318), P327 (= P320), G329 (= G322), V330 (= V323), E332 (= E325), G361 (= G351), D363 (= D353), T364 (≠ S354)
- binding trifluoromagnesate: K204 (= K199), K208 (= K203), G361 (= G351), G384 (= G375), G385 (= G376)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
44% identity, 99% coverage: 3:395/395 of query aligns to 6:407/408 of 2x15A
- active site: R37 (= R34), K207 (= K199), G365 (= G352), G388 (= G376)
- binding adenosine-5'-diphosphate: G205 (= G197), A206 (≠ S198), K207 (= K199), K211 (= K203), G229 (= G221), G230 (= G222), N328 (= N318), P330 (= P320), G332 (= G322), V333 (= V323), E335 (= E325), G364 (= G351), G365 (= G352), D366 (= D353), T367 (≠ S354)
- binding adenosine-5'-triphosphate: G205 (= G197), A206 (≠ S198), K207 (= K199), K211 (= K203), G229 (= G221), G230 (= G222), N328 (= N318), G332 (= G322), V333 (= V323), E335 (= E325), G364 (= G351), G365 (= G352), D366 (= D353), T367 (≠ S354), G387 (= G375), G388 (= G376)
- binding 1,3-bisphosphoglyceric acid: D22 (= D19), N24 (= N21), R37 (= R34), H61 (= H57), R64 (= R60), R121 (= R116), R162 (= R153), K207 (= K199), K211 (= K203), G364 (= G351), G387 (= G375), G388 (= G376)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
44% identity, 99% coverage: 3:395/395 of query aligns to 7:415/416 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)
45% identity, 99% coverage: 3:395/395 of query aligns to 6:404/405 of 2wzdA
- active site: R37 (= R34), K204 (= K199), G362 (= G352), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G197), A203 (≠ S198), K204 (= K199), G226 (= G221), G227 (= G222), N325 (= N318), P327 (= P320), G329 (= G322), V330 (= V323), E332 (= E325), G361 (= G351), D363 (= D353), T364 (≠ S354)
- binding aluminum fluoride: R37 (= R34), K204 (= K199), G361 (= G351), G362 (= G352), G384 (= G375)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
45% 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.
- R39 (= R34) binding substrate
- R122 (= R116) binding substrate
- R169 (= R153) binding substrate
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, 99% coverage: 3:395/395 of query aligns to 6:414/414 of 2y3iA
- active site: R37 (= R34), K214 (= K199), G372 (= G352), G395 (= G376)
- binding tetrafluoroaluminate ion: K214 (= K199), G371 (= G351), G372 (= G352), G394 (= G375)
- binding l-adenosine-5'-diphosphate: G212 (= G197), A213 (≠ S198), F290 (= F274), N335 (= N318), G339 (= G322), V340 (= V323), E342 (= E325), G371 (= G351), G372 (= G352), D373 (= D353), T374 (≠ S354)
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, 99% coverage: 3:395/395 of query aligns to 8:416/417 of P00558
- DFN 24:26 (≠ DLN 19:21) binding substrate
- R39 (= R34) binding substrate
- HLGR 63:66 (= HLGR 57:60) binding substrate
- L88 (= L81) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ S90) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R116) binding substrate
- K131 (= K124) modified: N6-malonyllysine; alternate
- G158 (≠ A140) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D146) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R153) binding substrate
- K191 (≠ A175) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R189) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K199) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K203) binding ATP; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ Q234) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (= V248) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ E250) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D267) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (= G294) binding ATP
- D315 (= D296) to N: in PGK1D; with rhabdomyolysis; variant Creteil; dbSNP:rs2149136994
- C316 (≠ I297) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ L304) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E325) binding ATP
- T352 (= T333) to N: in dbSNP:rs137852530
- GGDT 373:376 (≠ GGDS 351:354) binding ATP
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
44% identity, 99% coverage: 3:395/395 of query aligns to 7:413/415 of 1qpgA
- active site: R38 (= R34), K213 (= K199), G371 (= G352), G394 (= G376)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G221), G236 (= G222), N334 (= N318), P336 (= P320), G338 (= G322), V339 (= V323), F340 (= F324), E341 (= E325), G370 (= G351), G371 (= G352), D372 (= D353), T373 (≠ S354)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
44% identity, 99% coverage: 3:395/395 of query aligns to 8:416/417 of 4o33A
- active site: R39 (= R34), K216 (= K199), G374 (= G352), G397 (= G376)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G221), G239 (= G222), T255 (≠ K237), L257 (= L239), F292 (= F274), M312 (= M293), G313 (= G294), L314 (= L295), G341 (= G322), V342 (= V323)
Q7SIB7 Phosphoglycerate kinase 1; EC 2.7.2.3 from Sus scrofa (Pig) (see 2 papers)
44% identity, 99% coverage: 3:395/395 of query aligns to 8:416/417 of Q7SIB7
- DFN 24:26 (≠ DLN 19:21) binding substrate
- R39 (= R34) binding substrate
- HLGR 63:66 (= HLGR 57:60) binding substrate
- R123 (= R116) binding substrate
- R171 (= R153) binding substrate
- K220 (= K203) binding ATP
- G313 (= G294) binding ATP
- E344 (= E325) binding ATP
- GGDT 373:376 (≠ GGDS 351:354) binding ATP
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
43% identity, 99% coverage: 3:395/395 of query aligns to 7:415/416 of 5m1rA
- active site: R38 (= R34), K215 (= K199), G373 (= G352), G396 (= G376)
- binding adenosine-5'-diphosphate: G213 (= G197), A214 (≠ S198), K219 (= K203), G237 (= G221), G238 (= G222), L256 (= L239), G340 (= G322), V341 (= V323), E343 (= E325), D374 (= D353), T375 (≠ S354)
- binding magnesium ion: R150 (≠ A133), A151 (≠ D134), G372 (= G351), T375 (≠ S354)
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
42% identity, 100% coverage: 2:395/395 of query aligns to 3:414/415 of 16pkA
- active site: R35 (= R34), K215 (= K199), G372 (= G352), G395 (= G376)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G197), A214 (≠ S198), K219 (= K203), A238 (≠ G222), Y241 (≠ F225), L311 (= L295), P336 (= P320), G338 (= G322), V339 (= V323), E341 (= E325), G393 (= G374), G394 (= G375), G395 (= G376)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
42% identity, 100% coverage: 2:395/395 of query aligns to 3:414/415 of 13pkA
- active site: R35 (= R34), K215 (= K199), G372 (= G352), G395 (= G376)
- binding adenosine-5'-diphosphate: G213 (= G197), A214 (≠ S198), K219 (= K203), L311 (= L295), P336 (= P320), G338 (= G322), V339 (= V323), E341 (= E325), G371 (= G351), D373 (= D353), S374 (= S354)
Query Sequence
>WP_012852549.1 NCBI__GCF_000024385.1:WP_012852549.1
MRTIDDLDVRGKRVLVRSDLNVPLDGDRITDDGRIRASLPTINTLRERGAKVIVCAHLGR
PKGQVKPEFSLAPVARRLGELLGTEVAFASDVVGESAARTVAGLADGQVALLENLRFEPG
ETSKDDAERGAFADKLAALADLYVGDGFGAVHRKHASVYDVPRRLPHAAGGLIVAEVDVL
RKLTEEVERPYAVVLGGSKVSDKLGVIDNLLNKADRILIGGGMVFTFLAAQGHQVGKSLL
EQDQLDTVREYLARAEKNGVELVLPVDIVAATAFAADADHQVVPADAIPADRMGLDIGPA
SGRLFAERLAGAKTVFWNGPMGVFEMEPYSHGTRAVAQGLIDSGAFTVVGGGDSAAAVRS
LGFDESAFSHISTGGGASLEYLEGKTLPGLAALED
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