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Comparing WP_011735584.1 NCBI__GCF_000015045.1:WP_011735584.1 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)
53% identity, 99% coverage: 1:396/399 of query aligns to 3:396/398 of 1vpeA
- active site: R35 (= R38), K196 (= K200), G353 (= G353), G376 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G198), A195 (= A199), K196 (= K200), K200 (= K204), G218 (= G222), A219 (≠ G223), N316 (= N319), P318 (= P321), G320 (= G323), V321 (= V324), E323 (= E326), G352 (= G352), G353 (= G353), D354 (= D354), S355 (≠ T355)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
54% identity, 97% coverage: 11:396/399 of query aligns to 10:394/394 of P40924
- S183 (≠ Q186) modified: Phosphoserine
- T299 (≠ S302) 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)
53% identity, 97% coverage: 11:398/399 of query aligns to 10:399/654 of P36204
- R36 (= R38) binding substrate
- R118 (= R120) binding substrate
- R151 (= R153) binding substrate
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
55% identity, 97% coverage: 11:396/399 of query aligns to 10:394/394 of 1phpA
- active site: R36 (= R38), K197 (= K200), G351 (= G353), G374 (= G376)
- binding adenosine-5'-diphosphate: G195 (= G198), K201 (= K204), G219 (= G222), G220 (= G223), L237 (≠ K240), N316 (= N319), P318 (= P321), G320 (= G323), V321 (= V324), E323 (= E326), G350 (= G352), D352 (= D354), S353 (≠ T355)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
55% identity, 97% coverage: 11:396/399 of query aligns to 10:394/394 of P18912
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
49% identity, 97% coverage: 8:396/399 of query aligns to 9:414/415 of 3pgkA
- active site: R38 (= R38), K213 (= K200), G371 (= G353), G394 (= G376)
- binding adenosine-5'-triphosphate: G211 (= G198), A212 (= A199), K213 (= K200), F289 (= F275), L311 (= L296), N334 (= N319), G335 (= G320), P336 (= P321), G338 (= G323), V339 (= V324), D372 (= D354)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
50% identity, 97% coverage: 8:396/399 of query aligns to 10:415/416 of P00560
- R22 (= R20) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R38) binding substrate
- R122 (= R120) binding substrate
- R169 (= R153) binding substrate
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
49% identity, 97% coverage: 8:396/399 of query aligns to 9:414/415 of 1qpgA
- active site: R38 (= R38), K213 (= K200), G371 (= G353), G394 (= G376)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G222), G236 (= G223), N334 (= N319), P336 (= P321), G338 (= G323), V339 (= V324), F340 (= F325), E341 (= E326), G370 (= G352), G371 (= G353), D372 (= D354), T373 (= T355)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
47% identity, 97% coverage: 11:396/399 of query aligns to 13:414/414 of O60101
- Y75 (= Y73) modified: Phosphotyrosine
- S76 (= S74) modified: Phosphoserine
- S143 (vs. gap) modified: Phosphoserine
- S172 (≠ A156) modified: Phosphoserine
- S173 (= S157) modified: Phosphoserine
- S183 (≠ A170) modified: Phosphoserine
- S253 (= S239) modified: Phosphoserine
- S260 (≠ L246) modified: Phosphoserine
- T299 (= T285) modified: Phosphothreonine
- S328 (≠ A313) modified: Phosphoserine
- S351 (≠ A336) modified: Phosphoserine
- T373 (= T355) modified: Phosphothreonine
- S387 (= S369) modified: Phosphoserine
- S390 (= S372) modified: Phosphoserine
- S412 (≠ D394) modified: Phosphoserine
- S413 (≠ I395) modified: Phosphoserine
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
45% identity, 97% coverage: 10:396/399 of query aligns to 8:415/415 of 16pkA
- active site: R35 (= R38), K215 (= K200), G372 (= G353), G395 (= G376)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G198), A214 (= A199), K219 (= K204), A238 (≠ G223), Y241 (≠ F226), L311 (= L296), P336 (= P321), G338 (= G323), V339 (= V324), E341 (= E326), G393 (= G374), G394 (= G375), G395 (= G376)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
45% identity, 97% coverage: 10:396/399 of query aligns to 8:415/415 of 13pkA
- active site: R35 (= R38), K215 (= K200), G372 (= G353), G395 (= G376)
- binding adenosine-5'-diphosphate: G213 (= G198), A214 (= A199), K219 (= K204), L311 (= L296), P336 (= P321), G338 (= G323), V339 (= V324), E341 (= E326), G371 (= G352), D373 (= D354), S374 (≠ T355)
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
46% identity, 96% coverage: 11:393/399 of query aligns to 10:386/392 of 4feyA
- active site: R36 (= R38), K193 (= K200), G346 (= G353), G369 (= G376)
- binding adenosine-5'-diphosphate: G191 (= G198), S192 (≠ A199), K197 (= K204), G215 (= G222), G316 (= G323), V317 (= V324), E319 (= E326), D347 (= D354)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
45% identity, 97% coverage: 10:396/399 of query aligns to 12:419/440 of P07378
- DFN 24:26 (= DFN 22:24) binding substrate
- R39 (= R38) binding substrate
- HLGR 62:65 (= HLGR 61:64) binding substrate
- R135 (= R120) binding substrate
- R172 (= R153) binding substrate
- K223 (= K204) binding ATP
- N338 (= N319) binding ATP
- E345 (= E326) binding ATP
- GGDS 375:378 (≠ GGDT 352:355) binding ATP
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
45% identity, 98% coverage: 6:396/399 of query aligns to 16:424/424 of 1ltkC
- active site: R47 (= R38), K223 (= K200), G381 (= G353), G404 (= G376)
- binding adenosine monophosphate: G221 (= G198), A222 (= A199), K223 (= K200), G245 (= G222), G246 (= G223), G348 (= G323), V349 (= V324), E351 (= E326), D382 (= D354)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
47% identity, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R38), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (= A199), K204 (= K200), K208 (= K204), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding tetrafluoroaluminate ion: R37 (= R38), K204 (= K200), K208 (= K204), G361 (= G352), G362 (= G353), G384 (= G375)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
47% identity, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R38), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (= A199), K204 (= K200), K208 (= K204), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding trifluoromagnesate: K204 (= K200), K208 (= K204), G361 (= G352), G384 (= G375), G385 (= G376)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
46% identity, 97% coverage: 6:393/399 of query aligns to 7:404/407 of 4axxA
- active site: R37 (= R38), K206 (= K200), G364 (= G353), G387 (= G376)
- binding adenosine-5'-diphosphate: G204 (= G198), A205 (= A199), K210 (= K204), G228 (= G222), G229 (= G223), N327 (= N319), P329 (= P321), G331 (= G323), V332 (= V324), E334 (= E326), G363 (= G352), G364 (= G353), D365 (= D354), T366 (= T355)
- binding beryllium trifluoride ion: K206 (= K200), K210 (= K204), G363 (= G352)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
46% identity, 97% coverage: 6:393/399 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R38), K207 (= K200), G365 (= G353), G388 (= G376)
- binding adenosine-5'-diphosphate: G205 (= G198), A206 (= A199), K207 (= K200), K211 (= K204), G229 (= G222), G230 (= G223), N328 (= N319), P330 (= P321), G332 (= G323), V333 (= V324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355)
- binding adenosine-5'-triphosphate: G205 (= G198), A206 (= A199), K207 (= K200), K211 (= K204), G229 (= G222), G230 (= G223), N328 (= N319), G332 (= G323), V333 (= V324), E335 (= E326), G364 (= G352), G365 (= G353), D366 (= D354), T367 (= T355), G387 (= G375), G388 (= G376)
- binding 1,3-bisphosphoglyceric acid: D22 (= D22), N24 (= N24), R37 (= R38), H61 (= H61), R64 (= R64), R121 (= R120), R162 (= R153), K207 (= K200), K211 (= K204), G364 (= G352), G387 (= G375), G388 (= G376)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
46% identity, 97% coverage: 6:393/399 of query aligns to 7:402/405 of 2wzdA
- active site: R37 (= R38), K204 (= K200), G362 (= G353), G385 (= G376)
- binding adenosine-5'-diphosphate: G202 (= G198), A203 (= A199), K204 (= K200), G226 (= G222), G227 (= G223), N325 (= N319), P327 (= P321), G329 (= G323), V330 (= V324), E332 (= E326), G361 (= G352), D363 (= D354), T364 (= T355)
- binding aluminum fluoride: R37 (= R38), K204 (= K200), G361 (= G352), G362 (= G353), G384 (= G375)
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
49% identity, 96% coverage: 11:393/399 of query aligns to 10:395/398 of 3zlbA
- active site: R36 (= R38), K204 (= K200), G355 (= G353), G378 (= G376)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G198), S203 (≠ A199), G226 (= G222), G227 (= G223), N320 (= N319), P322 (= P321), G324 (= G323), V325 (= V324), E327 (= E326), G354 (= G352), G355 (= G353), D356 (= D354), S357 (≠ T355)
Sites not aligning to the query:
Query Sequence
>WP_011735584.1 NCBI__GCF_000015045.1:WP_011735584.1
MPIRYIDQLADLKDKKVFIRVDFNVPQDSKGNITEDTRITGALPTIRYAIEQGARVILAS
HLGRPKGEKNEKYSMVPAAKRLSELLGRKVKQASDCFGEEVTREIDAMKSGEVLMLENVR
FYPGEEKNDPKFAQQLANGCQVYVNDAFAVSHRAHASVEAITRVIPTVVAGFLMRNEMTF
FDKAMQNPVRPLVAILGGAKVSGKLEVLEKLMNKVDKVVIGGGMAFTFLKSMGYSVGASK
VEDELLPTAKKIMDKARKKGIMFYLPVDCVVANAFEASATNFITTVQEIPEGWLALDIGP
ASATLFTETLRDAKTVIWNGPMGVFEMDAFARGTFAVAEAVASAFATTIIGGGDTDSAVR
KAGVESKVSYISTGGGAFLELLEGKVLPGVKALDIKVKK
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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