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Comparing WP_018232695.1 NCBI__GCF_000378965.1:WP_018232695.1 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)
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
74% identity, 100% coverage: 1:391/392 of query aligns to 1:386/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L84) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
74% identity, 99% coverage: 2:391/392 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
60% identity, 99% coverage: 1:390/392 of query aligns to 1:390/392 of 4feyA
- active site: R36 (= R36), K193 (= K193), G346 (= G346), G369 (= G369)
- binding adenosine-5'-diphosphate: G191 (= G191), S192 (= S192), K197 (= K197), G215 (= G215), G316 (= G316), V317 (= V317), E319 (= E319), D347 (= D347)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
58% identity, 99% coverage: 4:391/392 of query aligns to 3:389/389 of 4ng4B
- active site: R35 (= R36), K191 (= K193), G344 (= G346), G367 (= G369)
- binding adenosine-5'-diphosphate: G189 (= G191), K195 (= K197), G213 (= G215), I286 (= I288), N310 (= N312), G311 (= G313), P312 (= P314), V315 (= V317), E317 (= E319), G343 (= G345), D345 (= D347), T346 (= T348)
- binding magnesium ion: D288 (= D290), G314 (= G316), F321 (= F323), S322 (≠ A324), T325 (= T327)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
50% identity, 99% coverage: 1:389/392 of query aligns to 1:394/394 of P40924
- S183 (≠ G179) modified: Phosphoserine
- T299 (= T295) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
48% identity, 99% coverage: 1:387/392 of query aligns to 1:392/394 of 1phpA
- active site: R36 (= R36), K197 (= K193), G351 (= G346), G374 (= G369)
- binding adenosine-5'-diphosphate: G195 (= G191), K201 (= K197), G219 (= G215), G220 (= G216), L237 (= L233), N316 (= N312), P318 (= P314), G320 (= G316), V321 (= V317), E323 (= E319), G350 (= G345), D352 (= D347), S353 (≠ T348)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
48% identity, 99% coverage: 1:387/392 of query aligns to 1:392/394 of P18912
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, 100% coverage: 1:391/392 of query aligns to 1:399/654 of P36204
- R36 (= R36) binding substrate
- R118 (= R113) binding substrate
- R151 (= R146) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
47% identity, 98% coverage: 5:389/392 of query aligns to 2:396/398 of 1vpeA
- active site: R35 (= R36), K196 (= K193), G353 (= G346), G376 (= G369)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G191), A195 (≠ S192), K196 (= K193), K200 (= K197), G218 (= G215), A219 (≠ G216), N316 (= N312), P318 (= P314), G320 (= G316), V321 (= V317), E323 (= E319), G352 (= G345), G353 (= G346), D354 (= D347), S355 (≠ T348)
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
41% identity, 97% coverage: 6:387/392 of query aligns to 5:413/415 of 16pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G346), G395 (= G369)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G191), A214 (≠ S192), K219 (= K197), A238 (≠ G216), Y241 (≠ N219), L311 (≠ F289), P336 (= P314), G338 (= G316), V339 (= V317), E341 (= E319), G393 (= G367), G394 (= G368), G395 (= G369)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
41% identity, 97% coverage: 6:387/392 of query aligns to 5:413/415 of 13pkA
- active site: R35 (= R36), K215 (= K193), G372 (= G346), G395 (= G369)
- binding adenosine-5'-diphosphate: G213 (= G191), A214 (≠ S192), K219 (= K197), L311 (≠ F289), P336 (= P314), G338 (= G316), V339 (= V317), E341 (= E319), G371 (= G345), D373 (= D347), S374 (≠ T348)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
41% identity, 98% coverage: 6:390/392 of query aligns to 9:420/440 of P07378
- DFN 24:26 (≠ DLN 21:23) binding substrate
- R39 (= R36) binding substrate
- HLGR 62:65 (= HLGR 59:62) binding substrate
- R135 (= R113) binding substrate
- R172 (= R146) binding substrate
- K223 (= K197) binding ATP
- N338 (= N312) binding ATP
- E345 (= E319) binding ATP
- GGDS 375:378 (≠ GGDT 345:348) binding ATP
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
42% identity, 99% coverage: 2:389/392 of query aligns to 4:414/415 of 3pgkA
- active site: R38 (= R36), K213 (= K193), G371 (= G346), G394 (= G369)
- binding adenosine-5'-triphosphate: G211 (= G191), A212 (≠ S192), K213 (= K193), F289 (= F268), L311 (≠ F289), N334 (= N312), G335 (= G313), P336 (= P314), G338 (= G316), V339 (= V317), D372 (= D347)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
42% identity, 99% coverage: 2:389/392 of query aligns to 5:415/416 of P00560
- R22 (= R19) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R36) binding substrate
- R122 (= R113) binding substrate
- R169 (= R146) binding substrate
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
42% identity, 99% coverage: 1:389/392 of query aligns to 1:398/398 of 3zlbA
- active site: R36 (= R36), K204 (= K193), G355 (= G346), G378 (= G369)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G191), S203 (= S192), G226 (= G215), G227 (= G216), N320 (= N312), P322 (= P314), G324 (= G316), V325 (= V317), E327 (= E319), G354 (= G345), G355 (= G346), D356 (= D347), S357 (≠ T348)
- binding magnesium ion: M1 (= M1), D8 (= D8), K398 (≠ R389)
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
41% identity, 99% coverage: 2:389/392 of query aligns to 4:414/415 of 1qpgA
- active site: R38 (= R36), K213 (= K193), G371 (= G346), G394 (= G369)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G215), G236 (= G216), N334 (= N312), P336 (= P314), G338 (= G316), V339 (= V317), F340 (= F318), E341 (= E319), G370 (= G345), G371 (= G346), D372 (= D347), T373 (= T348)
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: 4:386/392 of query aligns to 5:402/405 of 2wzcA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K193), K208 (= K197), G361 (= G345), G362 (= G346), G384 (= G368)
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: 4:386/392 of query aligns to 5:402/405 of 2wzbA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), K208 (= K197), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding trifluoromagnesate: K204 (= K193), K208 (= K197), G361 (= G345), G384 (= G368), G385 (= G369)
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, 98% coverage: 4:386/392 of query aligns to 5:402/405 of 2wzdA
- active site: R37 (= R36), K204 (= K193), G362 (= G346), G385 (= G369)
- binding adenosine-5'-diphosphate: G202 (= G191), A203 (≠ S192), K204 (= K193), G226 (= G215), G227 (= G216), N325 (= N312), P327 (= P314), G329 (= G316), V330 (= V317), E332 (= E319), G361 (= G345), D363 (= D347), T364 (= T348)
- binding aluminum fluoride: R37 (= R36), K204 (= K193), G361 (= G345), G362 (= G346), G384 (= G368)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
39% identity, 98% coverage: 4:386/392 of query aligns to 5:404/407 of 4axxA
- active site: R37 (= R36), K206 (= K193), G364 (= G346), G387 (= G369)
- binding adenosine-5'-diphosphate: G204 (= G191), A205 (≠ S192), K210 (= K197), G228 (= G215), G229 (= G216), N327 (= N312), P329 (= P314), G331 (= G316), V332 (= V317), E334 (= E319), G363 (= G345), G364 (= G346), D365 (= D347), T366 (= T348)
- binding beryllium trifluoride ion: K206 (= K193), K210 (= K197), G363 (= G345)
Query Sequence
>WP_018232695.1 NCBI__GCF_000378965.1:WP_018232695.1
MSVIKMTDLDLAGKRVLIREDLNVPVKDGKVTSDARIRASLPTIEHAMKAGAMVMLMSHL
GRPEEGVFSEENSLKPVADHLSGLLGSEVRLVRDYLDGVDVAEGEVVMLENVRFNKGEKK
NDEDLSRRYAALCDVYVMDAFGTAHRAQASTHGAGQYATTACAGPLLAAELEALGKALGN
PKRPLVAIVGGSKVSTKLTVLESLSGVVDQLIVGGGIANTFIAAQGHPVGKSLYEADLVD
EAKRLMTAAKEKGGDIPVPTDVVTGKAFSESTPAEIKAVADVSDDDMIFDVGPDTAASYA
DLLKKAGTIVWNGPVGVFEFDQFAAGTRALGEAIADSDAFSIAGGGDTLAAIDKYGLASR
ISYISTGGGAFLEFLEGKQLPAVAMLEARAKG
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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