SitesBLAST
Comparing WP_012412172.1 NCBI__GCF_000020025.1:WP_012412172.1 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)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
63% identity, 100% coverage: 1:399/400 of query aligns to 1:393/394 of 1phpA
- active site: R36 (= R40), K197 (= K201), G351 (= G357), G374 (= G380)
- 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 (= G356), D352 (= D358), S353 (= S359)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
63% identity, 100% coverage: 1:399/400 of query aligns to 1:393/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
61% identity, 100% coverage: 1:399/400 of query aligns to 1:393/394 of P40924
- S183 (≠ E187) modified: Phosphoserine
- T299 (≠ S303) 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)
57% identity, 98% coverage: 8:399/400 of query aligns to 5:396/654 of P36204
- R36 (= R40) binding
- R118 (= R121) binding
- R151 (= R154) binding
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
57% identity, 98% coverage: 8:397/400 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R40), K196 (= K201), G353 (= G357), G376 (= G380)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G199), A195 (≠ S200), K196 (= K201), K200 (= K205), G218 (= G223), A219 (≠ G224), N316 (= N320), P318 (= P322), G320 (= G324), V321 (= V325), E323 (= E327), G352 (= G356), G353 (= G357), D354 (= D358), S355 (= S359)
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
53% identity, 98% coverage: 8:397/400 of query aligns to 5:395/398 of 3zlbA
- active site: R36 (= R40), K204 (= K201), G355 (= G357), G378 (= G380)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G199), S203 (= S200), G226 (= G223), G227 (= G224), N320 (= N320), P322 (= P322), G324 (= G324), V325 (= V325), E327 (= E327), G354 (= G356), G355 (= G357), D356 (= D358), S357 (= S359)
- binding magnesium ion: D8 (≠ S11)
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)
49% identity, 100% coverage: 1:399/400 of query aligns to 1:414/416 of P00560
- R22 (= R22) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R40) binding
- R122 (= R121) binding
- R169 (= R154) binding
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
49% identity, 98% coverage: 8:399/400 of query aligns to 7:413/415 of 1qpgA
- active site: R38 (= R40), K213 (= K201), G371 (= G357), G394 (= G380)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G223), G236 (= G224), N334 (= N320), P336 (= P322), G338 (= G324), V339 (= V325), F340 (= F326), E341 (= E327), G370 (= G356), G371 (= G357), D372 (= D358), T373 (≠ S359)
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
48% identity, 98% coverage: 8:399/400 of query aligns to 4:414/415 of 16pkA
- active site: R35 (= R40), K215 (= K201), G372 (= G357), G395 (= G380)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G199), A214 (≠ S200), K219 (= K205), A238 (≠ G224), Y241 (≠ F227), L311 (= L297), P336 (= P322), G338 (= G324), V339 (= V325), E341 (= E327), G393 (= G378), G394 (= G379), G395 (= G380)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
48% identity, 98% coverage: 8:399/400 of query aligns to 4:414/415 of 13pkA
- active site: R35 (= R40), K215 (= K201), G372 (= G357), G395 (= G380)
- binding adenosine-5'-diphosphate: G213 (= G199), A214 (≠ S200), K219 (= K205), L311 (= L297), P336 (= P322), G338 (= G324), V339 (= V325), E341 (= E327), G371 (= G356), D373 (= D358), S374 (= S359)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
49% identity, 97% coverage: 13:399/400 of query aligns to 21:423/424 of 1ltkC
- active site: R47 (= R40), K223 (= K201), G381 (= G357), G404 (= G380)
- binding adenosine monophosphate: G221 (= G199), A222 (≠ S200), K223 (= K201), G245 (= G223), G246 (= G224), G348 (= G324), V349 (= V325), E351 (= E327), D382 (= D358)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
47% identity, 98% coverage: 8:399/400 of query aligns to 8:418/440 of P07378
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
48% identity, 99% coverage: 1:397/400 of query aligns to 1:411/414 of O60101
- Y75 (≠ L74) modified: Phosphotyrosine
- S76 (≠ R75) modified: Phosphoserine
- S143 (≠ E132) modified: Phosphoserine
- S172 (≠ A157) modified: Phosphoserine
- S173 (= S158) modified: Phosphoserine
- S183 (≠ A171) modified: Phosphoserine
- S253 (= S240) modified: Phosphoserine
- S260 (≠ L247) modified: Phosphoserine
- T299 (≠ S286) modified: Phosphothreonine
- S328 (≠ T314) modified: Phosphoserine
- S351 (≠ A337) modified: Phosphoserine
- T373 (≠ S359) modified: Phosphothreonine
- S387 (= S373) modified: Phosphoserine
- S390 (= S376) modified: Phosphoserine
Sites not aligning to the query:
- 412 modified: Phosphoserine
- 413 modified: Phosphoserine
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
49% identity, 98% coverage: 8:399/400 of query aligns to 7:413/415 of 3pgkA
- active site: R38 (= R40), K213 (= K201), G371 (= G357), G394 (= G380)
- binding adenosine-5'-triphosphate: G211 (= G199), A212 (≠ S200), K213 (= K201), F289 (= F276), L311 (= L297), N334 (= N320), G335 (= G321), P336 (= P322), G338 (= G324), V339 (= V325), D372 (= D358)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
46% identity, 98% coverage: 8:399/400 of query aligns to 8:416/417 of P09041
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
47% identity, 96% coverage: 14:397/400 of query aligns to 14:413/416 of 6yjeA
- active site: R39 (= R40), K215 (= K201), G373 (= G357), G396 (= G380)
- binding (2~{S})-2-(5-nitrofuran-2-yl)-2,3,5,6,7,8-hexahydro-1~{H}-[1]benzothiolo[2,3-d]pyrimidin-4-one: G237 (= G223), G238 (= G224), Y241 (≠ F227), L256 (= L241), F291 (= F276), M311 (= M295), G312 (= G296), L313 (= L297), G340 (= G324), V341 (= V325)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
48% identity, 98% coverage: 8:399/400 of query aligns to 6:406/407 of 4axxA
- active site: R37 (= R40), K206 (= K201), G364 (= G357), G387 (= G380)
- binding adenosine-5'-diphosphate: G204 (= G199), A205 (≠ S200), K210 (= K205), G228 (= G223), G229 (= G224), N327 (= N320), P329 (= P322), G331 (= G324), V332 (= V325), E334 (= E327), G363 (= G356), G364 (= G357), D365 (= D358), T366 (≠ S359)
- binding beryllium trifluoride ion: K206 (= K201), K210 (= K205), G363 (= G356)
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
46% identity, 98% coverage: 8:399/400 of query aligns to 4:412/413 of 2paaA
- active site: R35 (= R40), K212 (= K201), G370 (= G357), G393 (= G380)
- binding adenosine-5'-triphosphate: G210 (= G199), A211 (≠ S200), K216 (= K205), G235 (= G224), L253 (= L241), G309 (= G296), L310 (= L297), G334 (= G321), G337 (= G324), V338 (= V325), E340 (= E327), D371 (= D358)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
47% identity, 98% coverage: 8:399/400 of query aligns to 6:404/405 of 2wzcA
- active site: R37 (= R40), K204 (= K201), G362 (= G357), G385 (= G380)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (≠ S200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G356), D363 (= D358), T364 (≠ S359)
- binding tetrafluoroaluminate ion: R37 (= R40), K204 (= K201), K208 (= K205), G361 (= G356), G362 (= G357), G384 (= G379)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
47% identity, 98% coverage: 8:399/400 of query aligns to 6:404/405 of 2wzbA
- active site: R37 (= R40), K204 (= K201), G362 (= G357), G385 (= G380)
- binding adenosine-5'-diphosphate: G202 (= G199), A203 (≠ S200), K204 (= K201), K208 (= K205), G226 (= G223), G227 (= G224), N325 (= N320), P327 (= P322), G329 (= G324), V330 (= V325), E332 (= E327), G361 (= G356), D363 (= D358), T364 (≠ S359)
- binding trifluoromagnesate: K204 (= K201), K208 (= K205), G361 (= G356), G384 (= G379), G385 (= G380)
Query Sequence
>WP_012412172.1 NCBI__GCF_000020025.1:WP_012412172.1
MSKKSLASLSSADISGKRALVRVDFNVPVDDQGKITDDTRIRAALPTIQDLTQKGAKVIL
ASHFGRPKGVDDKLRLTPVAKRLSELLGQEVIKTDDSIGDEVAAKVAALQNGQVLLLENV
RFYPEEEKNDAEFAKKLAANADFYVNDAFGTAHRAHASTEGVTKFLSPSVAGYLVEKELQ
YLQNAIENPQRPLAAIIGGSKVSSKIGVIETLLEKCDKLIIGGGMIFTFYKARGLSVGKS
LVEEDKLELAKSLEAKAKERGVALLLPTDVVLADNFAPDANSQTVSIENIPDGWMGLDIG
PDSVKFFQEALADTKTVIWNGPMGVFEFDKFAAGTEAIAHTLAEIGKTGTTTIIGGGDSV
AAVEKVGLADQMSHISTGGGASLELLEGKVLPGIAALDDA
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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