SitesBLAST
Comparing WP_013834654.1 NCBI__GCF_000214825.1:WP_013834654.1 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)
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
71% identity, 100% coverage: 1:392/392 of query aligns to 1:386/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (= K84) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
71% identity, 100% coverage: 2:392/392 of query aligns to 1:385/386 of 1zmrA
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
61% identity, 100% coverage: 1:391/392 of query aligns to 1:390/392 of 4feyA
- active site: R36 (= R36), K193 (= K194), G346 (= G347), G369 (= G370)
- binding adenosine-5'-diphosphate: G191 (= G192), S192 (= S193), K197 (= K198), G215 (= G216), G316 (= G317), V317 (= V318), E319 (= E320), D347 (= D348)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
55% identity, 99% coverage: 3:392/392 of query aligns to 2:389/389 of 4ng4B
- active site: R35 (= R36), K191 (= K194), G344 (= G347), G367 (= G370)
- binding adenosine-5'-diphosphate: G189 (= G192), K195 (= K198), G213 (= G216), I286 (= I289), N310 (= N313), G311 (= G314), P312 (= P315), V315 (= V318), E317 (= E320), G343 (= G346), D345 (= D348), T346 (= T349)
- binding magnesium ion: D288 (= D291), G314 (= G317), F321 (= F324), S322 (≠ G325), T325 (= T328)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
47% identity, 98% coverage: 6:390/392 of query aligns to 6:394/394 of P40924
- S183 (≠ K180) modified: Phosphoserine
- T299 (≠ S296) modified: Phosphothreonine
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)
44% identity, 100% coverage: 1:392/392 of query aligns to 1:399/654 of P36204
- R36 (= R36) binding substrate
- R118 (= R114) binding substrate
- R151 (= R147) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
45% identity, 97% coverage: 6:384/392 of query aligns to 5:390/398 of 1vpeA
- active site: R35 (= R36), K196 (= K194), G353 (= G347), G376 (= G370)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G192), A195 (≠ S193), K196 (= K194), K200 (= K198), G218 (= G216), A219 (≠ G217), N316 (= N313), P318 (= P315), G320 (= G317), V321 (= V318), E323 (= E320), G352 (= G346), G353 (= G347), D354 (= D348), S355 (≠ T349)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
45% identity, 98% coverage: 6:390/392 of query aligns to 6:394/394 of 1phpA
- active site: R36 (= R36), K197 (= K194), G351 (= G347), G374 (= G370)
- binding adenosine-5'-diphosphate: G195 (= G192), K201 (= K198), G219 (= G216), G220 (= G217), L237 (= L234), N316 (= N313), P318 (= P315), G320 (= G317), V321 (= V318), E323 (= E320), G350 (= G346), D352 (= D348), S353 (≠ T349)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 98% coverage: 6:390/392 of query aligns to 6:394/394 of P18912
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
40% identity, 98% coverage: 8:391/392 of query aligns to 11:420/440 of P07378
- DFN 24:26 (≠ DLN 21:23) binding substrate
- R39 (= R36) binding substrate
- HLGR 62:65 (= HLGR 59:62) binding substrate
- R135 (= R114) binding substrate
- R172 (= R147) binding substrate
- K223 (= K198) binding ATP
- N338 (= N313) binding ATP
- E345 (= E320) binding ATP
- GGDS 375:378 (≠ GGDT 346:349) binding ATP
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
40% identity, 98% coverage: 8:390/392 of query aligns to 7:415/415 of 16pkA
- active site: R35 (= R36), K215 (= K194), G372 (= G347), G395 (= G370)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G192), A214 (≠ S193), K219 (= K198), A238 (≠ G217), Y241 (≠ N220), L311 (≠ F290), P336 (= P315), G338 (= G317), V339 (= V318), E341 (= E320), G393 (= G368), G394 (= G369), G395 (= G370)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
40% identity, 98% coverage: 8:390/392 of query aligns to 7:415/415 of 13pkA
- active site: R35 (= R36), K215 (= K194), G372 (= G347), G395 (= G370)
- binding adenosine-5'-diphosphate: G213 (= G192), A214 (≠ S193), K219 (= K198), L311 (≠ F290), P336 (= P315), G338 (= G317), V339 (= V318), E341 (= E320), G371 (= G346), D373 (= D348), S374 (≠ T349)
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
42% identity, 99% coverage: 1:390/392 of query aligns to 1:398/398 of 3zlbA
- active site: R36 (= R36), K204 (= K194), G355 (= G347), G378 (= G370)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G192), S203 (= S193), G226 (= G216), G227 (= G217), N320 (= N313), P322 (= P315), G324 (= G317), V325 (= V318), E327 (= E320), G354 (= G346), G355 (= G347), D356 (= D348), S357 (≠ T349)
- binding magnesium ion: M1 (= M1), D8 (= D8), K398 (≠ R390)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 99% coverage: 4:390/392 of query aligns to 7:414/414 of O60101
- Y75 (≠ N72) modified: Phosphotyrosine
- S76 (= S73) modified: Phosphoserine
- S143 (vs. gap) modified: Phosphoserine
- S172 (≠ G150) modified: Phosphoserine
- S173 (= S151) modified: Phosphoserine
- S183 (≠ A164) modified: Phosphoserine
- S253 (= S233) modified: Phosphoserine
- S260 (≠ V240) modified: Phosphoserine
- T299 (≠ S279) modified: Phosphothreonine
- S328 (≠ A307) modified: Phosphoserine
- S351 (≠ T330) modified: Phosphoserine
- T373 (= T349) modified: Phosphothreonine
- S387 (= S363) modified: Phosphoserine
- S390 (= S366) modified: Phosphoserine
- S412 (≠ E388) modified: Phosphoserine
- S413 (≠ Q389) modified: Phosphoserine
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
40% identity, 98% coverage: 4:387/392 of query aligns to 7:414/417 of P09041
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
40% identity, 97% coverage: 9:387/392 of query aligns to 8:410/413 of 2paaA
- active site: R35 (= R36), K212 (= K194), G370 (= G347), G393 (= G370)
- binding adenosine-5'-triphosphate: G210 (= G192), A211 (≠ S193), K216 (= K198), G235 (= G217), L253 (= L234), G309 (≠ I289), L310 (≠ F290), G334 (= G314), G337 (= G317), V338 (= V318), E340 (= E320), D371 (= D348)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
40% identity, 98% coverage: 4:387/392 of query aligns to 5:402/405 of 2wzcA
- active site: R37 (= R36), K204 (= K194), G362 (= G347), G385 (= G370)
- binding adenosine-5'-diphosphate: G202 (= G192), A203 (≠ S193), K204 (= K194), K208 (= K198), G226 (= G216), G227 (= G217), N325 (= N313), P327 (= P315), G329 (= G317), V330 (= V318), E332 (= E320), G361 (= G346), D363 (= D348), T364 (= T349)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K194), K208 (= K198), G361 (= G346), G362 (= G347), G384 (= G369)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
40% identity, 98% coverage: 4:387/392 of query aligns to 5:402/405 of 2wzbA
- active site: R37 (= R36), K204 (= K194), G362 (= G347), G385 (= G370)
- binding adenosine-5'-diphosphate: G202 (= G192), A203 (≠ S193), K204 (= K194), K208 (= K198), G226 (= G216), G227 (= G217), N325 (= N313), P327 (= P315), G329 (= G317), V330 (= V318), E332 (= E320), G361 (= G346), D363 (= D348), T364 (= T349)
- binding trifluoromagnesate: K204 (= K194), K208 (= K198), G361 (= G346), G384 (= G369), G385 (= G370)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
39% identity, 98% coverage: 4:387/392 of query aligns to 5:405/408 of 2x15A
- active site: R37 (= R36), K207 (= K194), G365 (= G347), G388 (= G370)
- binding adenosine-5'-diphosphate: G205 (= G192), A206 (≠ S193), K207 (= K194), K211 (= K198), G229 (= G216), G230 (= G217), N328 (= N313), P330 (= P315), G332 (= G317), V333 (= V318), E335 (= E320), G364 (= G346), G365 (= G347), D366 (= D348), T367 (= T349)
- binding adenosine-5'-triphosphate: G205 (= G192), A206 (≠ S193), K207 (= K194), K211 (= K198), G229 (= G216), G230 (= G217), N328 (= N313), G332 (= G317), V333 (= V318), E335 (= E320), G364 (= G346), G365 (= G347), D366 (= D348), T367 (= T349), G387 (= G369), G388 (= G370)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R36), H61 (= H59), R64 (= R62), R121 (= R114), R162 (= R147), K207 (= K194), K211 (= K198), G364 (= G346), G387 (= G369), G388 (= G370)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
40% identity, 98% coverage: 4:387/392 of query aligns to 5:404/407 of 4axxA
- active site: R37 (= R36), K206 (= K194), G364 (= G347), G387 (= G370)
- binding adenosine-5'-diphosphate: G204 (= G192), A205 (≠ S193), K210 (= K198), G228 (= G216), G229 (= G217), N327 (= N313), P329 (= P315), G331 (= G317), V332 (= V318), E334 (= E320), G363 (= G346), G364 (= G347), D365 (= D348), T366 (= T349)
- binding beryllium trifluoride ion: K206 (= K194), K210 (= K198), G363 (= G346)
Query Sequence
>WP_013834654.1 NCBI__GCF_000214825.1:WP_013834654.1
MSFIRMADLDLKGKRVLIRADLNVPVKNGVVTSDARIRASMKTFEAAMKAGAKVMVMSHL
GRPVEGEFSAENSLAPVAANLSEKLGKNVRLIKDYLNGGFDVADGELVLLENVRFNVGEG
KNTEELSKKYAALCDVYVMDAFGTAHRAQGSTHGAGVYAPVACAGLLLTEELDALTKALK
EPARPLVAIVGGSKVSTKLTVLESLSQVVDQLVVGGGIANTFIKAAGHNVGKSLCEDDLV
PTANKLNEIMNARNASIPVAVDVVTGKEFSETAAAETKSVADVADDDMIFDIGPKSAAEL
AEIIKNAGTVVWNGPVGVFEFDQFGAGTKTISKAIAESKAFSIAGGGDTLAAIDKYGIAD
QVSYISTGGGAFLEFLEGKKLPAVEMLEQRAK
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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