SitesBLAST
Comparing WP_010964029.1 NCBI__GCF_000008765.1:WP_010964029.1 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)
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)
61% identity, 99% coverage: 3:397/397 of query aligns to 1:397/654 of P36204
- R36 (= R38) binding substrate
- R118 (= R121) binding substrate
- R151 (= R154) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
61% identity, 99% coverage: 4:397/397 of query aligns to 1:396/398 of 1vpeA
- active site: R35 (= R38), K196 (= K201), G353 (= G354), G376 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G199), A195 (= A200), K196 (= K201), K200 (= K205), G218 (= G223), A219 (≠ G224), N316 (= N320), P318 (= P322), G320 (= G324), V321 (= V325), E323 (= E327), G352 (= G353), G353 (= G354), D354 (= D355), S355 (= S356)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
58% identity, 99% coverage: 3:397/397 of query aligns to 1:394/394 of P40924
- S183 (≠ E187) modified: Phosphoserine
- T299 (= T303) modified: Phosphothreonine
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
58% identity, 99% coverage: 3:397/397 of query aligns to 1:394/394 of 1phpA
- active site: R36 (= R38), K197 (= K201), G351 (= G354), G374 (= G377)
- binding adenosine-5'-diphosphate: G195 (= G199), K201 (= K205), G219 (= G223), G220 (= G224), L237 (= L241), N316 (= N320), P318 (= P322), G320 (= G324), V321 (= V325), E323 (= E327), G350 (= G353), D352 (= D355), S353 (= S356)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
58% identity, 99% coverage: 3:397/397 of query aligns to 1:394/394 of P18912
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
49% identity, 99% coverage: 5:397/397 of query aligns to 2:415/415 of 16pkA
- active site: R35 (= R38), K215 (= K201), G372 (= G354), G395 (= G377)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G199), A214 (= A200), K219 (= K205), A238 (≠ G224), Y241 (= Y227), L311 (= L297), P336 (= P322), G338 (= G324), V339 (= V325), E341 (= E327), G393 (= G375), G394 (= G376), G395 (= G377)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
49% identity, 99% coverage: 5:397/397 of query aligns to 2:415/415 of 13pkA
- active site: R35 (= R38), K215 (= K201), G372 (= G354), G395 (= G377)
- binding adenosine-5'-diphosphate: G213 (= G199), A214 (= A200), K219 (= K205), L311 (= L297), P336 (= P322), G338 (= G324), V339 (= V325), E341 (= E327), G371 (= G353), D373 (= D355), S374 (= S356)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
49% identity, 100% coverage: 1:397/397 of query aligns to 1:419/440 of P07378
- DFN 24:26 (= DFN 23:25) binding substrate
- R39 (= R38) binding substrate
- HLGR 62:65 (≠ HLGK 61:64) binding substrate
- R135 (= R121) binding substrate
- R172 (= R154) binding substrate
- K223 (= K205) binding ATP
- N338 (= N320) binding ATP
- E345 (= E327) binding ATP
- GGDS 375:378 (= GGDS 353:356) binding ATP
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
54% identity, 99% coverage: 5:397/397 of query aligns to 3:398/398 of 3zlbA
- active site: R36 (= R38), K204 (= K201), G355 (= G354), G378 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G199), S203 (≠ A200), G226 (= G223), G227 (= G224), N320 (= N320), P322 (= P322), G324 (= G324), V325 (= V325), E327 (= E327), G354 (= G353), G355 (= G354), D356 (= D355), S357 (= S356)
- binding magnesium ion: D8 (= D10), K398 (= K397)
Sites not aligning to the query:
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
50% identity, 99% coverage: 4:397/397 of query aligns to 5:415/416 of P00560
- R22 (= R21) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R38) binding substrate
- R122 (= R121) binding substrate
- R169 (= R154) binding substrate
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
50% identity, 99% coverage: 4:397/397 of query aligns to 4:414/415 of 1qpgA
- active site: R38 (= R38), K213 (= K201), G371 (= G354), G394 (= G377)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G223), G236 (= G224), N334 (= N320), P336 (= P322), G338 (= G324), V339 (= V325), F340 (= F326), E341 (= E327), G370 (= G353), G371 (= G354), D372 (= D355), T373 (≠ S356)
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
49% identity, 98% coverage: 7:397/397 of query aligns to 5:389/392 of 4feyA
- active site: R36 (= R38), K193 (= K201), G346 (= G354), G369 (= G377)
- binding adenosine-5'-diphosphate: G191 (= G199), S192 (≠ A200), K197 (= K205), G215 (= G223), G316 (= G324), V317 (= V325), E319 (= E327), D347 (= D355)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
50% identity, 99% coverage: 4:396/397 of query aligns to 3:404/405 of 2wzcA
- active site: R37 (= R38), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (= A200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (≠ S356)
- binding tetrafluoroaluminate ion: R37 (= R38), K204 (= K201), K208 (= K205), G361 (= G353), G362 (= G354), G384 (= G376)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
50% identity, 99% coverage: 4:396/397 of query aligns to 3:404/405 of 2wzbA
- active site: R37 (= R38), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (= A200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (≠ S356)
- binding trifluoromagnesate: K204 (= K201), K208 (= K205), G361 (= G353), G384 (= G376), G385 (= G377)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
51% identity, 99% coverage: 5:397/397 of query aligns to 6:414/414 of O60101
- Y75 (vs. gap) modified: Phosphotyrosine
- S76 (≠ T73) modified: Phosphoserine
- S143 (vs. gap) modified: Phosphoserine
- S172 (≠ C157) modified: Phosphoserine
- S173 (= S158) modified: Phosphoserine
- S183 (≠ C171) modified: Phosphoserine
- S253 (= S240) modified: Phosphoserine
- S260 (≠ V247) modified: Phosphoserine
- T299 (= T285) modified: Phosphothreonine
- S328 (≠ A314) modified: Phosphoserine
- S351 (≠ D337) modified: Phosphoserine
- T373 (≠ S356) modified: Phosphothreonine
- S387 (≠ T370) modified: Phosphoserine
- S390 (= S373) modified: Phosphoserine
- S412 (≠ N395) modified: Phosphoserine
- S413 (≠ D396) modified: Phosphoserine
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
49% identity, 99% coverage: 4:397/397 of query aligns to 4:414/415 of 3pgkA
- active site: R38 (= R38), K213 (= K201), G371 (= G354), G394 (= G377)
- binding adenosine-5'-triphosphate: G211 (= G199), A212 (= A200), K213 (= K201), F289 (= F276), L311 (= L297), N334 (= N320), G335 (= G321), P336 (= P322), G338 (= G324), V339 (= V325), D372 (= D355)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
50% identity, 99% coverage: 4:396/397 of query aligns to 3:404/405 of 2wzdA
- active site: R37 (= R38), K204 (= K201), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (= A200), K204 (= K201), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G353), D363 (= D355), T364 (≠ S356)
- binding aluminum fluoride: R37 (= R38), K204 (= K201), G361 (= G353), G362 (= G354), G384 (= G376)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
50% identity, 99% coverage: 4:396/397 of query aligns to 3:406/407 of 4axxA
- active site: R37 (= R38), K206 (= K201), G364 (= G354), G387 (= G377)
- binding adenosine-5'-diphosphate: G204 (= G199), A205 (= A200), K210 (= K205), G228 (= G223), G229 (= G224), N327 (= N320), P329 (= P322), G331 (= G324), V332 (= V325), E334 (= E327), G363 (= G353), G364 (= G354), D365 (= D355), T366 (≠ S356)
- binding beryllium trifluoride ion: K206 (= K201), K210 (= K205), G363 (= G353)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
50% identity, 99% coverage: 4:396/397 of query aligns to 3:407/408 of 2x15A
- active site: R37 (= R38), K207 (= K201), G365 (= G354), G388 (= G377)
- binding adenosine-5'-diphosphate: G205 (= G199), A206 (= A200), K207 (= K201), K211 (= K205), G229 (= G223), G230 (= G224), N328 (= N320), P330 (= P322), G332 (= G324), V333 (= V325), E335 (= E327), G364 (= G353), G365 (= G354), D366 (= D355), T367 (≠ S356)
- binding adenosine-5'-triphosphate: G205 (= G199), A206 (= A200), K207 (= K201), K211 (= K205), G229 (= G223), G230 (= G224), N328 (= N320), G332 (= G324), V333 (= V325), E335 (= E327), G364 (= G353), G365 (= G354), D366 (= D355), T367 (≠ S356), G387 (= G376), G388 (= G377)
- binding 1,3-bisphosphoglyceric acid: D22 (= D23), N24 (= N25), R37 (= R38), H61 (= H61), R64 (≠ K64), R121 (= R121), R162 (= R154), K207 (= K201), K211 (= K205), G364 (= G353), G387 (= G376), G388 (= G377)
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
49% identity, 99% coverage: 4:396/397 of query aligns to 3:414/414 of 2y3iA
- active site: R37 (= R38), K214 (= K201), G372 (= G354), G395 (= G377)
- binding tetrafluoroaluminate ion: K214 (= K201), G371 (= G353), G372 (= G354), G394 (= G376)
- binding l-adenosine-5'-diphosphate: G212 (= G199), A213 (= A200), F290 (= F276), N335 (= N320), G339 (= G324), V340 (= V325), E342 (= E327), G371 (= G353), G372 (= G354), D373 (= D355), T374 (≠ S356)
Query Sequence
>WP_010964029.1 NCBI__GCF_000008765.1:WP_010964029.1
MKFNKKTIEDVDVKGKRVLVRCDFNVPLKDGVITDENRLNGALPTIKYLSEHGGKVILCS
HLGKAKGPDPSKTLAPVAKRLSELLGREVKFAADDTVVGENAKKAVAELKEGEIVLLENT
RFRPEEGKNDDAFSKDLASLADVYVNDAFGTAHRAHCSTVGVTKFVDTAVCGYLIQKELK
FLGSAVENPVRPFVAILGGAKVSDKINVINNLLEKVDTLIIGGGMAYTFLKAQGYTIGTS
LLEADKVDYAKEMIEKAEAKGVKLLLPIDNIVGAEFKADTKAVTTEDANIPEGYMGLDIG
PKTQKLYADAVKEAKTVVWNGPMGVFEFENFAKGTKDVAKAMAESDATTVIGGGDSAAAV
NQLGFGDKMTHISTGGGASLEFLEGKELPGIVALNDK
Or try a new SitesBLAST search
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