SitesBLAST
Comparing WP_052669802.1 NCBI__GCF_000969705.1:WP_052669802.1 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)
52% identity, 99% coverage: 3:390/392 of query aligns to 4:394/398 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 (= V320), E323 (= E322), G352 (= G348), G353 (= G349), D354 (= D350), S355 (= S351)
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)
51% identity, 99% coverage: 3:389/392 of query aligns to 5:394/654 of P36204
- R36 (= R35) binding substrate
- R118 (= R117) binding substrate
- R151 (= R150) binding substrate
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
51% identity, 99% coverage: 2:390/392 of query aligns to 4:392/394 of P40924
- S183 (≠ A182) modified: Phosphoserine
- T299 (= T298) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
50% identity, 99% coverage: 2:389/392 of query aligns to 4:391/394 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 (≠ R236), N316 (= N315), P318 (= P317), G320 (= G319), V321 (= V320), E323 (= E322), G350 (= G348), D352 (= D350), S353 (= S351)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
50% identity, 99% coverage: 2:389/392 of query aligns to 4:391/394 of P18912
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: 3:391/392 of query aligns to 6:404/405 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 (= V320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (≠ S351)
- 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)
45% identity, 99% coverage: 3:391/392 of query aligns to 6:404/405 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 (= V320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (≠ S351)
- binding trifluoromagnesate: K204 (= K196), K208 (= K200), G361 (= G348), G384 (= G371), G385 (= G372)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
45% identity, 99% coverage: 3:391/392 of query aligns to 6:406/407 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 (= V320), E334 (= E322), G363 (= G348), G364 (= G349), D365 (= D350), T366 (≠ S351)
- binding beryllium trifluoride ion: K206 (= K196), K210 (= K200), G363 (= G348)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
44% identity, 99% coverage: 3:391/392 of query aligns to 6:404/405 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 (= V320), E332 (= E322), G361 (= G348), D363 (= D350), T364 (≠ S351)
- binding aluminum fluoride: R37 (= R35), K204 (= K196), G361 (= G348), G362 (= G349), G384 (= G371)
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
43% identity, 99% coverage: 3:391/392 of query aligns to 5:388/392 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 (= V320), E319 (= E322), D347 (= D350)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
44% identity, 99% coverage: 3:391/392 of query aligns to 6:407/408 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 (= V320), E335 (= E322), G364 (= G348), G365 (= G349), D366 (= D350), T367 (≠ S351)
- binding adenosine-5'-triphosphate: G205 (= G194), A206 (= A195), K207 (= K196), K211 (= K200), G229 (= G218), G230 (≠ A219), N328 (= N315), G332 (= G319), V333 (= V320), E335 (= E322), G364 (= G348), G365 (= G349), D366 (= D350), T367 (≠ S351), G387 (= G371), G388 (= G372)
- binding 1,3-bisphosphoglyceric acid: D22 (= D20), N24 (= N22), R37 (= R35), H61 (= H58), R64 (= R61), R121 (= R117), R162 (= R150), 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 2.7.2.3 from Homo sapiens (Human) (see 16 papers)
44% identity, 99% coverage: 3:391/392 of query aligns to 8:416/417 of P00558
- DFN 24:26 (≠ DLN 20:22) binding substrate
- R39 (= R35) binding substrate
- HLGR 63:66 (= HLGR 58:61) binding substrate
- L88 (= L82) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ T91) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R117) binding substrate
- K131 (= K124) modified: N6-malonyllysine; alternate
- G158 (≠ A137) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D143) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R150) binding substrate
- K191 (≠ A171) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (≠ S186) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K196) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K200) binding ATP; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (= E231) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (= V245) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (= D247) 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
- G313 (= G291) binding ATP
- D315 (= D293) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ V294) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ A301) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E322) binding ATP
- T352 (= T330) to N: in dbSNP:rs137852530
- GGDT 373:376 (≠ GGDS 348:351) binding ATP
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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: 3:391/392 of query aligns to 6:414/414 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 (= F271), N335 (= N315), G339 (= G319), V340 (= V320), E342 (= E322), G371 (= G348), G372 (= G349), D373 (= D350), T374 (≠ S351)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
44% identity, 99% coverage: 3:391/392 of query aligns to 7:415/416 of 1vjcA
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
43% identity, 99% coverage: 3:391/392 of query aligns to 7:415/416 of 1kf0A
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
43% identity, 99% coverage: 3:391/392 of query aligns to 8:416/417 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 (= T234), L257 (≠ R236), F292 (= F271), M312 (= M290), G313 (= G291), L314 (= L292), G341 (= G319), V342 (= V320)
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
43% identity, 99% coverage: 3:391/392 of query aligns to 7:415/416 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 (≠ R236), G340 (= G319), V341 (= V320), E343 (= E322), D374 (= D350), T375 (≠ S351)
- binding magnesium ion: R150 (vs. gap), A151 (vs. gap), G372 (= G348), T375 (≠ S351)
Q7SIB7 Phosphoglycerate kinase 1; EC 2.7.2.3 from Sus scrofa (Pig) (see 2 papers)
43% identity, 99% coverage: 3:391/392 of query aligns to 8:416/417 of Q7SIB7
- DFN 24:26 (≠ DLN 20:22) binding substrate
- R39 (= R35) binding substrate
- HLGR 63:66 (= HLGR 58:61) binding substrate
- R123 (= R117) binding substrate
- R171 (= R150) binding substrate
- K220 (= K200) binding ATP
- G313 (= G291) binding ATP
- E344 (= E322) binding ATP
- GGDT 373:376 (≠ GGDS 348:351) binding ATP
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
44% identity, 96% coverage: 14:391/392 of query aligns to 14:386/389 of 4ng4B
- active site: R35 (= R35), K191 (= K196), G344 (= G349), G367 (= G372)
- binding adenosine-5'-diphosphate: G189 (= G194), K195 (= K200), G213 (= G218), I286 (≠ G291), N310 (= N315), G311 (= G316), P312 (= P317), V315 (= V320), E317 (= E322), G343 (= G348), D345 (= D350), T346 (≠ S351)
- binding magnesium ion: D288 (= D293), G314 (= G319), F321 (= F326), S322 (≠ A327), T325 (= T330)
1hdiA Pig muscle 3-phosphoglycerate kinase complexed with 3-pg and mgadp. (see paper)
44% identity, 99% coverage: 3:391/392 of query aligns to 4:412/413 of 1hdiA
- active site: R35 (= R35), K212 (= K196), G370 (= G349), G393 (= G372)
- binding adenosine monophosphate: A211 (= A195), G234 (= G218), G235 (≠ A219), L310 (= L292), G337 (= G319), V338 (= V320), E340 (= E322), D371 (= D350)
Query Sequence
>WP_052669802.1 NCBI__GCF_000969705.1:WP_052669802.1
MRTLDDLEVRPGLRVFVRADLNVPLRDGRVTDDLRVRSSVPTLRRLLDGGARVVVASHLG
RPKGEPDPASSMAPVGALLEELLGAPVMVATDVVGDDARAKADALEDGEVLLLENLRWDA
GETKNDDALADALAAFADVYVDDAFGAAHRAHASISGVPARIPGYAGLLLARELEVLGGL
QADPASPYVAVLGGAKVSDKLLVLEQLLQRVDAIAVGGAMAFTFLVAEGFEVGTSRVEED
QVDTVRDLVAQARERGVDVLLPTDVVVAPAFEQDAPATTVPVAAMPADQMGLDVGPDTAA
AYAAAIADAGSVFWNGPMGVFEWEAFAAGTRTVAQAVADAQGFTIVGGGDSAAAIRAFGL
DDAVDHVSTGGGASLELLEGKTLPGVAALRQA
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