SitesBLAST
Comparing PfGW456L13_1417 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1417 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)
A0QV10 Aldo-keto reductase MSMEG_2408/MSMEI_2347; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
38% identity, 94% coverage: 9:267/277 of query aligns to 10:267/275 of A0QV10
- K262 (≠ E261) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
35% identity, 94% coverage: 7:267/277 of query aligns to 10:268/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
35% identity, 94% coverage: 7:267/277 of query aligns to 15:273/281 of 1vbjA
- active site: D52 (= D43), Y57 (= Y48), K82 (= K73), H115 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G18), M27 (≠ T19), W28 (= W20), D52 (= D43), Y57 (= Y48), H115 (= H106), N145 (= N137), Q166 (= Q158), W192 (≠ Y184), S193 (≠ T185), P194 (= P186), L195 (= L187), Q197 (≠ R189), G198 (≠ N190), V201 (≠ S193), A218 (≠ T210), I233 (= I226), K235 (= K228), S236 (≠ A229), G237 (≠ S230), R241 (≠ N234), E244 (≠ A237), N245 (= N238)
6kiyA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor epalrestat (see paper)
34% identity, 92% coverage: 5:258/277 of query aligns to 7:275/275 of 6kiyA
- binding {5-[(2E)-2-methyl-3-phenylprop-2-en-1-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl}acetic acid: W22 (= W20), Y59 (= Y48), W87 (= W75), H118 (= H106), R204 (= R189)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (= W20), Y59 (= Y48), H118 (= H106), N149 (= N137), Q170 (= Q158), Y199 (= Y184), S200 (≠ T185), P201 (= P186), L202 (= L187), R204 (= R189), T205 (≠ N190), Y227 (≠ T210), I243 (= I226), P244 (= P227), K245 (= K228), G247 (≠ S230), R248 (≠ S231), H251 (≠ N234), E254 (≠ A237), N255 (= N238)
6kikA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor tolrestat (see paper)
34% identity, 92% coverage: 5:258/277 of query aligns to 7:275/275 of 6kikA
5danA Crystal structure of a novel aldo keto reductase tm1743 from thermotoga maritima in complex with NADP+
34% identity, 92% coverage: 5:258/277 of query aligns to 6:274/274 of 5danA
- active site: D53 (= D43), Y58 (= Y48), K84 (= K73), H117 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), T20 (= T19), W21 (= W20), D53 (= D43), Y58 (= Y48), H117 (= H106), Q169 (= Q158), Y198 (= Y184), S199 (≠ T185), P200 (= P186), L201 (= L187), R203 (= R189), Y226 (≠ T210), I242 (= I226), P243 (= P227), K244 (= K228), G246 (≠ S230), R247 (≠ S231), H250 (≠ N234), E253 (≠ A237), N254 (= N238)
P14065 Glycerol 2-dehydrogenase (NADP(+)); Galactose-inducible crystallin-like protein 1; EC 1.1.1.156 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
34% identity, 95% coverage: 9:270/277 of query aligns to 17:307/312 of P14065
- Q29 (≠ P21) mutation to K: Decreases catalytic activity.
- Y56 (= Y48) mutation to L: Loss of catalytic activity.
- K264 (= K228) mutation to R: Decreases catalytic activity.
- N267 (≠ E232) mutation to Q: Decreases catalytic activity.
- R270 (≠ Q235) mutation R->H,Y,K: Decreases catalytic activity.
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
35% identity, 94% coverage: 10:270/277 of query aligns to 21:285/288 of 4gieA
- active site: D55 (= D43), Y60 (= Y48), K85 (= K73), H118 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G18), W31 (= W20), D55 (= D43), Y60 (= Y48), H118 (= H106), W119 (= W107), N148 (= N137), Q169 (= Q158), W195 (≠ Y184), S196 (≠ T185), P197 (= P186), L198 (= L187), S200 (≠ R189), L207 (vs. gap), A224 (≠ T210), I239 (= I226), P240 (= P227), K241 (= K228), S242 (≠ A229), R247 (≠ N234), E250 (≠ A237), N251 (= N238)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
35% identity, 94% coverage: 10:270/277 of query aligns to 10:274/277 of 4fziA
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
36% identity, 94% coverage: 9:267/277 of query aligns to 13:269/275 of 3d3fA
- active site: D48 (= D43), Y53 (= Y48), K78 (= K73), H111 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G18), F24 (≠ W20), D48 (= D43), Y53 (= Y48), H111 (= H106), S140 (≠ A136), N141 (= N137), Q162 (= Q158), W188 (≠ Y184), S189 (≠ T185), P190 (= P186), L191 (= L187), Q193 (≠ R189), L197 (≠ S193), I229 (= I226), K231 (= K228), S232 (≠ A229), K234 (≠ S231), R237 (≠ N234), E240 (≠ A237), N241 (= N238)
3wbwA Crystal structure of gox0644 in complex with NADPH
32% identity, 94% coverage: 9:267/277 of query aligns to 11:265/271 of 3wbwA
- active site: D45 (= D43), Y50 (= Y48), K71 (= K73), H104 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), H104 (= H106), N136 (= N137), W183 (≠ Y184), R184 (≠ T185), P185 (= P186), L186 (= L187), L192 (≠ S193), A209 (≠ T210), K226 (= K228), S227 (= S230), V228 (≠ S231), R232 (≠ Q235), E235 (vs. gap), N236 (= N238)
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Rattus norvegicus (Rat) (see paper)
30% identity, 93% coverage: 9:266/277 of query aligns to 11:301/325 of P51635
- K13 (≠ N11) Not glycated
- K23 (≠ P21) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ T28) Not glycated
- K34 (≠ E32) Not glycated
- K61 (vs. gap) Not glycated
- K68 (≠ S61) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K73) Not glycated
- K85 (≠ Q78) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ R90) Not glycated
- K127 (vs. gap) Not glycated
- K134 (≠ D111) Not glycated
- K141 (≠ I118) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (vs. gap) Not glycated
- K153 (≠ Q127) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R131) Not glycated
- K240 (= K204) Not glycated
- K257 (≠ N222) Not glycated
- K263 (= K228) Not glycated
- K287 (≠ A252) Not glycated
- K294 (= K259) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 308 Not glycated
Q9JII6 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Mus musculus (Mouse)
30% identity, 93% coverage: 9:266/277 of query aligns to 11:301/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
34% identity, 94% coverage: 7:267/277 of query aligns to 11:277/283 of 4g5dA
- active site: D48 (= D43), Y53 (= Y48), K78 (= K73), H111 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G18), V23 (≠ T19), W24 (= W20), D48 (= D43), Y53 (= Y48), H111 (= H106), S148 (≠ A136), N149 (= N137), Q170 (= Q158), W196 (≠ Y184), S197 (≠ T185), P198 (= P186), L199 (= L187), Q201 (≠ R189), G202 (≠ N190), L205 (≠ S193), I237 (= I226), P238 (= P227), K239 (= K228), S240 (≠ A229), V241 (≠ S230), H242 (≠ S231), R245 (≠ N234), E248 (≠ A237), N249 (= N238)
5z6tA Crystal structure of d-xylose reductase from scheffersomyces stipitis in complex with NADPH (see paper)
31% identity, 93% coverage: 9:266/277 of query aligns to 8:307/317 of 5z6tA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G18), C18 (≠ T19), W19 (= W20), D42 (= D43), Y47 (= Y48), H109 (= H106), S164 (≠ A136), Q186 (= Q158), Y212 (= Y184), S213 (≠ T185), F215 (≠ L187), Q218 (≠ N190), S219 (≠ K191), E222 (≠ D194), F235 (vs. gap), A252 (≠ T210), I267 (= I226), P268 (= P227), K269 (= K228), N271 (≠ S230), R275 (≠ N234), E278 (≠ A237), N279 (= N238), N305 (≠ V264)
7s5fB Crystal structure of mannose-6-phosphate reductase from celery (apium graveolens) leaves with NADP+ and mannonic acid bound (see paper)
30% identity, 96% coverage: 8:272/277 of query aligns to 7:303/309 of 7s5fB
- binding d-mannonic acid: W19 (= W20), D46 (≠ A47), Y47 (= Y48), W78 (= W75), H107 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G18), V18 (≠ T19), W19 (= W20), D42 (= D43), Y47 (= Y48), N161 (= N137), Q182 (= Q158), H208 (≠ Y184), T209 (= T185), P210 (= P186), L211 (= L187), G213 (≠ R189), A214 (vs. gap), A244 (≠ T210), I259 (= I226), K261 (= K228), S262 (≠ A229), S263 (= S230), R267 (≠ N234), E270 (≠ A237), N271 (= N238)
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Homo sapiens (Human) (see 3 papers)
29% identity, 93% coverage: 9:266/277 of query aligns to 11:301/325 of P14550
- Y50 (= Y48) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N50) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ A53) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K73) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H106) binding ; mutation to Q: Strong decrease in enzymatic activity.
- I299 (≠ V264) mutation to A: No change in enzymatic activity.; mutation to C: No change in enzymatic activity.
- V300 (≠ S265) mutation to C: No change in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
A0QV09 Aldo-keto reductase MSMEG_2407/MSMEI_2346; AKR; AKR5H1; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
35% identity, 91% coverage: 12:262/277 of query aligns to 22:272/283 of A0QV09
- G196 (≠ T185) binding
- L198 (= L187) binding
- V200 (≠ R189) binding
- I236 (≠ P227) binding
- R238 (≠ A229) binding
- S239 (= S230) binding
- A240 (≠ S231) binding
- R244 (≠ Q235) binding
- S247 (vs. gap) binding
- N248 (= N238) binding
Sites not aligning to the query:
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
35% identity, 91% coverage: 12:262/277 of query aligns to 13:263/274 of 2wzmA
- active site: D44 (= D43), Y49 (= Y48), K74 (= K73), H107 (= H106)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: Y186 (= Y184), G187 (≠ T185), P188 (= P186), L189 (= L187), G190 (≠ A188), V191 (≠ R189), G192 (≠ N190), L195 (≠ S193), A212 (≠ T210), I227 (≠ P227), R229 (≠ A229), S230 (= S230), R235 (≠ Q235), N239 (= N238)
Sites not aligning to the query:
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
30% identity, 93% coverage: 9:266/277 of query aligns to 11:301/320 of 3h4gA
- active site: D45 (= D43), Y50 (= Y48), K80 (= K73), H113 (= H106)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (= W20), Y50 (= Y48), H113 (= H106), W114 (= W107), W220 (vs. gap), I299 (≠ V264), V300 (≠ S265), P301 (= P266)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (= W20), D45 (= D43), Y50 (= Y48), H113 (= H106), S162 (≠ A136), N163 (= N137), Q184 (= Q158), Y210 (= Y184), S211 (≠ T185), P212 (= P186), L213 (= L187), S215 (≠ R189), D217 (≠ K191), A246 (≠ T210), I261 (= I226), P262 (= P227), K263 (= K228), S264 (≠ A229), V265 (≠ S230), T266 (≠ S231), R269 (≠ N234), Q272 (≠ A237), N273 (= N238)
Query Sequence
>PfGW456L13_1417 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1417
MQHIINAQGLNMPKLGLGTWPMLGEECTRAVEQALALGYRHIDTAAAYNNEDAVGQALAN
SPTPREQIHVTTKVWWDQLQPDAMRHSMDRSLKALRSEYVDLFMLHWPTTDWDLPRTIET
LVSFREQGLARNIGVANFPLHLLRKVVEELGAPLSAIQVEYHVLLGQNALLDYARQQDLA
LTAYTPLARNKVSDIPAIRRIAAKHGVLPTQVALKWLLDQPNVAAIPKASSEPNQLANLA
ALDVRLDDEDRALIASLSKRERQVSPDFAPVWDAFDE
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