SitesBLAST
Comparing Ac3H11_4404 FitnessBrowser__acidovorax_3H11:Ac3H11_4404 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)
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
59% identity, 99% coverage: 1:395/399 of query aligns to 1:385/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L89) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
59% identity, 99% coverage: 2:395/399 of query aligns to 1:384/386 of 1zmrA
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
56% identity, 99% coverage: 1:395/399 of query aligns to 1:390/392 of 4feyA
- active site: R36 (= R41), K193 (= K198), G346 (= G351), G369 (= G374)
- binding adenosine-5'-diphosphate: G191 (= G196), S192 (= S197), K197 (= K202), G215 (= G220), G316 (= G321), V317 (= V322), E319 (= E324), D347 (= D352)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
56% identity, 95% coverage: 16:395/399 of query aligns to 11:388/389 of 4ng4B
- active site: R35 (= R41), K191 (= K198), G344 (= G351), G367 (= G374)
- binding adenosine-5'-diphosphate: G189 (= G196), K195 (= K202), G213 (= G220), I286 (= I293), N310 (= N317), G311 (= G318), P312 (= P319), V315 (= V322), E317 (= E324), G343 (= G350), D345 (= D352), T346 (= T353)
- binding magnesium ion: D288 (= D295), G314 (= G321), F321 (= F328), S322 (≠ E329), T325 (= T332)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
46% identity, 97% coverage: 1:386/399 of query aligns to 1:386/394 of P40924
- S183 (≠ A184) modified: Phosphoserine
- T299 (= T300) 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)
46% identity, 93% coverage: 16:386/399 of query aligns to 12:389/654 of P36204
- R36 (= R41) binding
- R118 (= R118) binding
- R151 (= R151) binding
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
46% identity, 93% coverage: 16:386/399 of query aligns to 11:388/398 of 1vpeA
- active site: R35 (= R41), K196 (= K198), G353 (= G351), G376 (= G374)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G196), A195 (≠ S197), K196 (= K198), K200 (= K202), G218 (= G220), A219 (≠ G221), N316 (= N317), P318 (= P319), G320 (= G321), V321 (= V322), E323 (= E324), G352 (= G350), G353 (= G351), D354 (= D352), S355 (≠ T353)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
46% identity, 95% coverage: 16:394/399 of query aligns to 12:394/394 of 1phpA
- active site: R36 (= R41), K197 (= K198), G351 (= G351), G374 (= G374)
- binding adenosine-5'-diphosphate: G195 (= G196), K201 (= K202), G219 (= G220), G220 (= G221), L237 (= L238), N316 (= N317), P318 (= P319), G320 (= G321), V321 (= V322), E323 (= E324), G350 (= G350), D352 (= D352), S353 (≠ T353)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
46% identity, 95% coverage: 16:394/399 of query aligns to 12:394/394 of P18912
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
39% identity, 95% coverage: 16:394/399 of query aligns to 11:415/415 of 16pkA
- active site: R35 (= R41), K215 (= K198), G372 (= G351), G395 (= G374)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G196), A214 (≠ S197), K219 (= K202), A238 (≠ G221), Y241 (≠ N224), L311 (= L294), P336 (= P319), G338 (= G321), V339 (= V322), E341 (= E324), G393 (= G372), G394 (= G373), G395 (= G374)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
39% identity, 95% coverage: 16:394/399 of query aligns to 11:415/415 of 13pkA
- active site: R35 (= R41), K215 (= K198), G372 (= G351), G395 (= G374)
- binding adenosine-5'-diphosphate: G213 (= G196), A214 (≠ S197), K219 (= K202), L311 (= L294), P336 (= P319), G338 (= G321), V339 (= V322), E341 (= E324), G371 (= G350), D373 (= D352), S374 (≠ T353)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
39% identity, 95% coverage: 16:396/399 of query aligns to 15:421/440 of P07378
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
41% identity, 95% coverage: 16:394/399 of query aligns to 15:415/416 of P00560
- R22 (= R23) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R41) binding
- R122 (= R118) binding
- R169 (= R151) binding
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
41% identity, 94% coverage: 18:394/399 of query aligns to 16:414/415 of 1qpgA
- active site: R38 (= R41), K213 (= K198), G371 (= G351), G394 (= G374)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G220), G236 (= G221), N334 (= N317), P336 (= P319), G338 (= G321), V339 (= V322), F340 (= F323), E341 (= E324), G370 (= G350), G371 (= G351), D372 (= D352), T373 (= T353)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
41% identity, 95% coverage: 16:393/399 of query aligns to 13:406/407 of 4axxA
- active site: R37 (= R41), K206 (= K198), G364 (= G351), G387 (= G374)
- binding adenosine-5'-diphosphate: G204 (= G196), A205 (≠ S197), K210 (= K202), G228 (= G220), G229 (= G221), N327 (= N317), P329 (= P319), G331 (= G321), V332 (= V322), E334 (= E324), G363 (= G350), G364 (= G351), D365 (= D352), T366 (= T353)
- binding beryllium trifluoride ion: K206 (= K198), K210 (= K202), G363 (= G350)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
40% identity, 95% coverage: 16:393/399 of query aligns to 13:404/405 of 2wzcA
- active site: R37 (= R41), K204 (= K198), G362 (= G351), G385 (= G374)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (≠ S197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (= V322), E332 (= E324), G361 (= G350), D363 (= D352), T364 (= T353)
- binding tetrafluoroaluminate ion: R37 (= R41), K204 (= K198), K208 (= K202), G361 (= G350), G362 (= G351), G384 (= G373)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
40% identity, 95% coverage: 16:393/399 of query aligns to 13:404/405 of 2wzbA
- active site: R37 (= R41), K204 (= K198), G362 (= G351), G385 (= G374)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (≠ S197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (= V322), E332 (= E324), G361 (= G350), D363 (= D352), T364 (= T353)
- binding trifluoromagnesate: K204 (= K198), K208 (= K202), G361 (= G350), G384 (= G373), G385 (= G374)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
40% identity, 95% coverage: 16:393/399 of query aligns to 13:407/408 of 2x15A
- active site: R37 (= R41), K207 (= K198), G365 (= G351), G388 (= G374)
- binding adenosine-5'-diphosphate: G205 (= G196), A206 (≠ S197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), P330 (= P319), G332 (= G321), V333 (= V322), E335 (= E324), G364 (= G350), G365 (= G351), D366 (= D352), T367 (= T353)
- binding adenosine-5'-triphosphate: G205 (= G196), A206 (≠ S197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), G332 (= G321), V333 (= V322), E335 (= E324), G364 (= G350), G365 (= G351), D366 (= D352), T367 (= T353), G387 (= G373), G388 (= G374)
- binding 1,3-bisphosphoglyceric acid: D22 (= D25), N24 (= N27), R37 (= R41), H61 (= H64), R64 (= R67), R121 (= R118), R162 (= R151), K207 (= K198), K211 (= K202), G364 (= G350), G387 (= G373), G388 (= G374)
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)
40% identity, 95% coverage: 16:393/399 of query aligns to 15:416/417 of P00558
- DFN 24:26 (≠ DMN 25:27) binding
- R39 (= R41) binding
- HLGR 63:66 (= HLGR 64:67) binding
- L88 (= L89) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ A98) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R118) binding
- K131 (= K125) modified: N6-malonyllysine; alternate
- G158 (≠ C138) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D144) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R151) binding
- K191 (≠ S173) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R188) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K198) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K202) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ P233) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A247) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ S249) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D266) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (≠ I293) binding
- D315 (= D295) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I296) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ R303) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E324) binding
- T352 (= T332) to N: in dbSNP:rs137852530
- GGDT 373:376 (= GGDT 350:353) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
39% identity, 95% coverage: 16:393/399 of query aligns to 14:415/416 of 1kf0A
Query Sequence
>Ac3H11_4404 FitnessBrowser__acidovorax_3H11:Ac3H11_4404
MNILRFSDLCAQGKAQGQRVFIRADMNVPQDDAGQITEDTRIRASIPCIRMALDAGAAVM
VTSHLGRPTEGEFKPEDSLAPVAQRLSELLGRDVPLVANWVDGVTVAPGQVVLLENCRLN
VGEKKNKDELARKLAALCDIFVNDAFGTAHRAEGTTYGIAQFAPVACAGPLLSAEIDALT
KALAQPQRPLAAIVAGSKVSTKLTILQSLADKVDQLIVGGGIANTFMLAAGLPIGKSLAE
PDLLDAAKSVMAAMKARGAEVPIPTDVVVAKAFAADAPATVKAATDVAPDDLILDIGPDT
AARLAAQLKSAGTIVWNGPVGVFEFAAFENGTRALAAAIAESPAFSIAGGGDTLAAIAKY
GIEKQVGYISTGGGAFLEVLEGKKLPAFDILEQRAAAAV
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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