SitesBLAST
Comparing WP_012975072.1 NCBI__GCF_000010725.1:WP_012975072.1 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)
48% identity, 98% coverage: 6:396/397 of query aligns to 5:395/654 of P36204
- R36 (= R37) binding substrate
- R118 (= R119) binding substrate
- R151 (= R152) binding substrate
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
48% identity, 98% coverage: 6:395/397 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R37), K196 (= K198), G353 (= G355), G376 (= G378)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G196), A195 (= A197), K196 (= K198), K200 (= K202), G218 (= G220), A219 (≠ G221), N316 (= N317), P318 (= P319), G320 (= G321), V321 (≠ A322), E323 (= E324), G352 (= G354), G353 (= G355), D354 (= D356), S355 (≠ T357)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
47% identity, 98% coverage: 6:395/397 of query aligns to 5:391/394 of 1phpA
- active site: R36 (= R37), K197 (= K198), G351 (= G355), G374 (= G378)
- binding adenosine-5'-diphosphate: G195 (= G196), K201 (= K202), G219 (= G220), G220 (= G221), L237 (= L238), N316 (= N317), P318 (= P319), G320 (= G321), V321 (≠ A322), E323 (= E324), G350 (= G354), D352 (= D356), S353 (≠ T357)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
47% identity, 98% coverage: 6:395/397 of query aligns to 5:391/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
46% identity, 98% coverage: 6:395/397 of query aligns to 5:391/394 of P40924
- S183 (≠ E184) modified: Phosphoserine
- T299 (= T300) modified: Phosphothreonine
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
45% identity, 99% coverage: 4:395/397 of query aligns to 3:386/392 of 4feyA
- active site: R36 (= R37), K193 (= K198), G346 (= G355), G369 (= G378)
- binding adenosine-5'-diphosphate: G191 (= G196), S192 (≠ A197), K197 (= K202), G215 (= G220), G316 (= G321), V317 (≠ A322), E319 (= E324), D347 (= D356)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
40% identity, 99% coverage: 1:395/397 of query aligns to 3:416/440 of P07378
- DFN 24:26 (≠ DLN 22:24) binding substrate
- R39 (= R37) binding substrate
- HLGR 62:65 (≠ HFGR 60:63) binding substrate
- R135 (= R119) binding substrate
- R172 (= R152) binding substrate
- K223 (= K202) binding ATP
- N338 (= N317) binding ATP
- E345 (= E324) binding ATP
- GGDS 375:378 (≠ GGDT 354:357) binding ATP
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
40% identity, 98% coverage: 5:395/397 of query aligns to 3:412/415 of 16pkA
- active site: R35 (= R37), K215 (= K198), G372 (= G355), G395 (= G378)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G196), A214 (= A197), K219 (= K202), A238 (≠ G221), Y241 (≠ N224), L311 (= L294), P336 (= P319), G338 (= G321), V339 (≠ A322), E341 (= E324), G393 (≠ A376), G394 (= G377), G395 (= G378)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
40% identity, 98% coverage: 5:395/397 of query aligns to 3:412/415 of 13pkA
- active site: R35 (= R37), K215 (= K198), G372 (= G355), G395 (= G378)
- binding adenosine-5'-diphosphate: G213 (= G196), A214 (= A197), K219 (= K202), L311 (= L294), P336 (= P319), G338 (= G321), V339 (≠ A322), E341 (= E324), G371 (= G354), D373 (= D356), S374 (≠ T357)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
45% identity, 99% coverage: 4:397/397 of query aligns to 2:386/389 of 4ng4B
- active site: R35 (= R37), K191 (= K198), G344 (= G355), G367 (= G378)
- binding adenosine-5'-diphosphate: G189 (= G196), K195 (= K202), G213 (= G220), I286 (≠ A293), N310 (= N317), G311 (= G318), P312 (= P319), V315 (≠ A322), E317 (= E324), G343 (= G354), D345 (= D356), T346 (= T357)
- binding magnesium ion: D288 (= D295), G314 (= G321), F321 (= F328), S322 (≠ D329), T325 (= T332)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
43% identity, 98% coverage: 6:396/397 of query aligns to 8:415/417 of P09041
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
45% identity, 97% coverage: 9:395/397 of query aligns to 7:380/386 of 1zmrA
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 97% coverage: 9:395/397 of query aligns to 8:381/387 of P0A799
- K84 (≠ A84) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
41% identity, 98% coverage: 6:396/397 of query aligns to 7:414/416 of 6yjeA
- active site: R39 (= R37), K215 (= K198), G373 (= G355), G396 (= G378)
- 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 (= G220), G238 (= G221), Y241 (≠ N224), L256 (= L238), F291 (= F273), M311 (= M292), G312 (≠ A293), L313 (= L294), G340 (= G321), V341 (≠ A322)
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
42% identity, 98% coverage: 6:396/397 of query aligns to 4:411/413 of 2paaA
- active site: R35 (= R37), K212 (= K198), G370 (= G355), G393 (= G378)
- binding adenosine-5'-triphosphate: G210 (= G196), A211 (= A197), K216 (= K202), G235 (= G221), L253 (= L238), G309 (≠ A293), L310 (= L294), G334 (= G318), G337 (= G321), V338 (≠ A322), E340 (= E324), D371 (= D356)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
43% identity, 98% coverage: 6:396/397 of query aligns to 6:403/405 of 2wzcA
- active site: R37 (= R37), K204 (= K198), G362 (= G355), G385 (= G378)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (= A197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (≠ A322), E332 (= E324), G361 (= G354), D363 (= D356), T364 (= T357)
- binding tetrafluoroaluminate ion: R37 (= R37), K204 (= K198), K208 (= K202), G361 (= G354), G362 (= G355), G384 (= G377)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
43% identity, 98% coverage: 6:396/397 of query aligns to 6:403/405 of 2wzbA
- active site: R37 (= R37), K204 (= K198), G362 (= G355), G385 (= G378)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (= A197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (≠ A322), E332 (= E324), G361 (= G354), D363 (= D356), T364 (= T357)
- binding trifluoromagnesate: K204 (= K198), K208 (= K202), G361 (= G354), G384 (= G377), G385 (= G378)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 98% coverage: 6:396/397 of query aligns to 6:405/407 of 4axxA
- active site: R37 (= R37), K206 (= K198), G364 (= G355), G387 (= G378)
- binding adenosine-5'-diphosphate: G204 (= G196), A205 (= A197), K210 (= K202), G228 (= G220), G229 (= G221), N327 (= N317), P329 (= P319), G331 (= G321), V332 (≠ A322), E334 (= E324), G363 (= G354), G364 (= G355), D365 (= D356), T366 (= T357)
- binding beryllium trifluoride ion: K206 (= K198), K210 (= K202), G363 (= G354)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
40% identity, 98% coverage: 6:396/397 of query aligns to 15:422/424 of 1ltkC
- active site: R47 (= R37), K223 (= K198), G381 (= G355), G404 (= G378)
- binding adenosine monophosphate: G221 (= G196), A222 (= A197), K223 (= K198), G245 (= G220), G246 (= G221), G348 (= G321), V349 (≠ A322), E351 (= E324), D382 (= D356)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 98% coverage: 6:396/397 of query aligns to 6:406/408 of 2x15A
- active site: R37 (= R37), K207 (= K198), G365 (= G355), G388 (= G378)
- binding adenosine-5'-diphosphate: G205 (= G196), A206 (= A197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), P330 (= P319), G332 (= G321), V333 (≠ A322), E335 (= E324), G364 (= G354), G365 (= G355), D366 (= D356), T367 (= T357)
- binding adenosine-5'-triphosphate: G205 (= G196), A206 (= A197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), G332 (= G321), V333 (≠ A322), E335 (= E324), G364 (= G354), G365 (= G355), D366 (= D356), T367 (= T357), G387 (= G377), G388 (= G378)
- binding 1,3-bisphosphoglyceric acid: D22 (= D22), N24 (= N24), R37 (= R37), H61 (= H60), R64 (= R63), R121 (= R119), R162 (= R152), K207 (= K198), K211 (= K202), G364 (= G354), G387 (= G377), G388 (= G378)
Query Sequence
>WP_012975072.1 NCBI__GCF_000010725.1:WP_012975072.1
MTDFNTIDDLEVSGKTVLVRADLNVPMQDGKVSDTTRIDRLAPTLKELSAKGAKVVVLSH
FGRPKNGPDAKNSLRNVLDALSAAVGQKVAFAEDCVGEKAREAIAKVHEGAIVLLENTRF
HAEEEKNDPAFAKEMAALGDLYVNDAFSAAHRAHASTEGVARLLPNAAGRLMEAELKALT
LALEKPERPVAAVVGGAKISTKLELLGNMVRKVDLLVLGGGMANTFLFAQGIDVGASLCE
KDMADQARAIMATAKEANCEILLPKDFVVAKEFKAGAANRVVAFDAIGSDEMALDVGPAT
VEFLGVKLQGAKTIVWNGPLGAFEIQPFDAGTNAVAGLVAARTEAGGLLSVAGGGDTVAA
LAHAGAEDKFTYVSAAGGAFLEWLEGKELPGVAALAK
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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