SitesBLAST
Comparing RR42_RS03200 FitnessBrowser__Cup4G11:RR42_RS03200 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)
62% identity, 99% coverage: 3:400/402 of query aligns to 2:385/387 of P0A799
- K84 (≠ L90) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
62% identity, 99% coverage: 3:400/402 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
57% identity, 99% coverage: 3:400/402 of query aligns to 2:390/392 of 4feyA
- active site: R36 (= R42), K193 (= K203), G346 (= G356), G369 (= G379)
- binding adenosine-5'-diphosphate: G191 (= G201), S192 (= S202), K197 (= K207), G215 (= G225), G316 (= G326), V317 (= V327), E319 (= E329), D347 (= D357)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
54% identity, 97% coverage: 11:400/402 of query aligns to 5:388/389 of 4ng4B
- active site: R35 (= R42), K191 (= K203), G344 (= G356), G367 (= G379)
- binding adenosine-5'-diphosphate: G189 (= G201), K195 (= K207), G213 (= G225), I286 (= I298), N310 (= N322), G311 (= G323), P312 (= P324), V315 (= V327), E317 (= E329), G343 (= G355), D345 (= D357), T346 (= T358)
- binding magnesium ion: D288 (= D300), G314 (= G326), F321 (= F333), S322 (= S334), T325 (= T337)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
49% identity, 96% coverage: 16:399/402 of query aligns to 11:394/394 of P40924
- S183 (≠ G189) modified: Phosphoserine
- T299 (= T305) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
47% identity, 96% coverage: 16:399/402 of query aligns to 11:394/394 of 1phpA
- active site: R36 (= R42), K197 (= K203), G351 (= G356), G374 (= G379)
- binding adenosine-5'-diphosphate: G195 (= G201), K201 (= K207), G219 (= G225), G220 (= G226), L237 (= L243), N316 (= N322), P318 (= P324), G320 (= G326), V321 (= V327), E323 (= E329), G350 (= G355), D352 (= D357), S353 (≠ T358)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
47% identity, 96% coverage: 16:399/402 of query aligns to 11:394/394 of P18912
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
46% identity, 94% coverage: 16:391/402 of query aligns to 10:388/398 of 1vpeA
- active site: R35 (= R42), K196 (= K203), G353 (= G356), G376 (= G379)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G201), A195 (≠ S202), K196 (= K203), K200 (= K207), G218 (= G225), A219 (≠ G226), N316 (= N322), P318 (= P324), G320 (= G326), V321 (= V327), E323 (= E329), G352 (= G355), G353 (= G356), D354 (= D357), S355 (≠ T358)
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, 94% coverage: 16:391/402 of query aligns to 11:389/654 of P36204
- R36 (= R42) binding
- R118 (= R123) binding
- R151 (= R156) binding
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
41% identity, 97% coverage: 11:401/402 of query aligns to 9:421/440 of P07378
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
41% identity, 97% coverage: 11:399/402 of query aligns to 5:415/415 of 16pkA
- active site: R35 (= R42), K215 (= K203), G372 (= G356), G395 (= G379)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G201), A214 (≠ S202), K219 (= K207), A238 (≠ G226), Y241 (≠ N229), L311 (= L299), P336 (= P324), G338 (= G326), V339 (= V327), E341 (= E329), G393 (= G377), G394 (= G378), G395 (= G379)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
41% identity, 97% coverage: 11:399/402 of query aligns to 5:415/415 of 13pkA
- active site: R35 (= R42), K215 (= K203), G372 (= G356), G395 (= G379)
- binding adenosine-5'-diphosphate: G213 (= G201), A214 (≠ S202), K219 (= K207), L311 (= L299), P336 (= P324), G338 (= G326), V339 (= V327), E341 (= E329), G371 (= G355), D373 (= D357), S374 (≠ T358)
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
40% identity, 99% coverage: 1:399/402 of query aligns to 2:414/415 of 3pgkA
- active site: R38 (= R42), K213 (= K203), G371 (= G356), G394 (= G379)
- binding adenosine-5'-triphosphate: G211 (= G201), A212 (≠ S202), K213 (= K203), F289 (= F278), L311 (= L299), N334 (= N322), G335 (= G323), P336 (= P324), G338 (= G326), V339 (= V327), D372 (= D357)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
41% identity, 99% coverage: 1:399/402 of query aligns to 3:415/416 of P00560
- R22 (= R24) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R42) binding
- R122 (= R123) binding
- R169 (= R156) binding
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
41% identity, 99% coverage: 1:399/402 of query aligns to 2:414/415 of 1qpgA
- active site: R38 (= R42), K213 (= K203), G371 (= G356), G394 (= G379)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G225), G236 (= G226), N334 (= N322), P336 (= P324), G338 (= G326), V339 (= V327), F340 (= F328), E341 (= E329), G370 (= G355), G371 (= G356), D372 (= D357), T373 (= T358)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
41% identity, 95% coverage: 16:398/402 of query aligns to 12:404/405 of 2wzcA
- active site: R37 (= R42), K204 (= K203), G362 (= G356), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G201), A203 (≠ S202), K204 (= K203), K208 (= K207), G226 (= G225), G227 (= G226), N325 (= N322), P327 (= P324), G329 (= G326), V330 (= V327), E332 (= E329), G361 (= G355), D363 (= D357), T364 (= T358)
- binding tetrafluoroaluminate ion: R37 (= R42), K204 (= K203), K208 (= K207), G361 (= G355), G362 (= G356), G384 (= G378)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
41% identity, 95% coverage: 16:398/402 of query aligns to 12:404/405 of 2wzbA
- active site: R37 (= R42), K204 (= K203), G362 (= G356), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G201), A203 (≠ S202), K204 (= K203), K208 (= K207), G226 (= G225), G227 (= G226), N325 (= N322), P327 (= P324), G329 (= G326), V330 (= V327), E332 (= E329), G361 (= G355), D363 (= D357), T364 (= T358)
- binding trifluoromagnesate: K204 (= K203), K208 (= K207), G361 (= G355), G384 (= G378), G385 (= G379)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
40% identity, 95% coverage: 16:398/402 of query aligns to 12:404/405 of 2wzdA
- active site: R37 (= R42), K204 (= K203), G362 (= G356), G385 (= G379)
- binding adenosine-5'-diphosphate: G202 (= G201), A203 (≠ S202), K204 (= K203), G226 (= G225), G227 (= G226), N325 (= N322), P327 (= P324), G329 (= G326), V330 (= V327), E332 (= E329), G361 (= G355), D363 (= D357), T364 (= T358)
- binding aluminum fluoride: R37 (= R42), K204 (= K203), G361 (= G355), G362 (= G356), G384 (= G378)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
40% identity, 95% coverage: 16:398/402 of query aligns to 12:406/407 of 4axxA
- active site: R37 (= R42), K206 (= K203), G364 (= G356), G387 (= G379)
- binding adenosine-5'-diphosphate: G204 (= G201), A205 (≠ S202), K210 (= K207), G228 (= G225), G229 (= G226), N327 (= N322), P329 (= P324), G331 (= G326), V332 (= V327), E334 (= E329), G363 (= G355), G364 (= G356), D365 (= D357), T366 (= T358)
- binding beryllium trifluoride ion: K206 (= K203), K210 (= K207), G363 (= G355)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
40% identity, 95% coverage: 16:398/402 of query aligns to 12:407/408 of 2x15A
- active site: R37 (= R42), K207 (= K203), G365 (= G356), G388 (= G379)
- binding adenosine-5'-diphosphate: G205 (= G201), A206 (≠ S202), K207 (= K203), K211 (= K207), G229 (= G225), G230 (= G226), N328 (= N322), P330 (= P324), G332 (= G326), V333 (= V327), E335 (= E329), G364 (= G355), G365 (= G356), D366 (= D357), T367 (= T358)
- binding adenosine-5'-triphosphate: G205 (= G201), A206 (≠ S202), K207 (= K203), K211 (= K207), G229 (= G225), G230 (= G226), N328 (= N322), G332 (= G326), V333 (= V327), E335 (= E329), G364 (= G355), G365 (= G356), D366 (= D357), T367 (= T358), G387 (= G378), G388 (= G379)
- binding 1,3-bisphosphoglyceric acid: D22 (= D26), N24 (= N28), R37 (= R42), H61 (= H65), R64 (= R68), R121 (= R123), R162 (= R156), K207 (= K203), K211 (= K207), G364 (= G355), G387 (= G378), G388 (= G379)
Query Sequence
>RR42_RS03200 FitnessBrowser__Cup4G11:RR42_RS03200
MTSVLRLSDLISQGKIAGKRVFIRADLNVPQDDAGQITEDTRIRASVPAIEACLQAGAAV
MVTSHLGRPTEGEFKPEDSLAPVAARLAELLGKPVKLVQNWVDGNGEVSAVKPGEVVLLE
NCRVNKGEKKNSDELAQKMAKLCDVYVNDAFGTAHRAEATTHGIAKYAPIACAGPLLAAE
IDALGKALGQPARPLVAIVAGSKVSTKLTILKTLAGKVDNLIVGGGIANTFMLAAGLKIG
KSLAEADLVADARTIIDLMAARGASVPIPVDVVCAKEFSATAVATVKDAKDVADDDMILD
IGPKTAQMLADQLKLAGTIVWNGPVGVFEFDQFSNGTKVLAQAIAESKAFSIAGGGDTLA
AIAKYGIADQVGYISTGGGAFLEFLEGKKLPAFEVLEQRAAG
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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