SitesBLAST
Comparing Pf1N1B4_128 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_128 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)
39% identity, 96% coverage: 2:256/267 of query aligns to 12:264/275 of A0QV10
- K262 (≠ Q254) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vdgA Barley aldose reductase 1 complex with butanol (see paper)
36% identity, 96% coverage: 2:256/267 of query aligns to 11:282/308 of 2vdgA
- active site: D43 (= D34), Y48 (= Y39), K76 (= K64), H109 (= H97)
- binding 1-butanol: E47 (≠ I38), E123 (≠ D103), A124 (≠ Q104)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G18 (= G9), T19 (= T10), W20 (≠ F11), D43 (= D34), Y48 (= Y39), K76 (= K64), H109 (= H97), C154 (≠ S129), N155 (= N130), Q176 (= Q152), Y202 (= Y178), S203 (≠ M179), P204 (≠ T180), L205 (= L181), S207 (≠ Y183), S208 (≠ G184), N211 (vs. gap), I245 (= I219), P246 (= P220), K247 (≠ S221), S248 (= S222), S249 (≠ T223), K250 (= K224), R253 (≠ N227), E256 (≠ G230), N257 (= N231)
Sites not aligning to the query:
2bgsA Holo aldose reductase from barley (see paper)
36% identity, 96% coverage: 2:256/267 of query aligns to 11:282/308 of 2bgsA
- active site: D43 (= D34), Y48 (= Y39), K76 (= K64), H109 (= H97)
- binding bicarbonate ion: W20 (≠ F11), Y48 (= Y39), H109 (= H97)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G18 (= G9), T19 (= T10), W20 (≠ F11), D43 (= D34), Y48 (= Y39), C154 (≠ S129), N155 (= N130), Q176 (= Q152), Y202 (= Y178), S203 (≠ M179), P204 (≠ T180), L205 (= L181), S207 (≠ Y183), I245 (= I219), P246 (= P220), K247 (≠ S221), S248 (= S222), K250 (= K224), R253 (≠ N227), E256 (≠ G230), N257 (= N231)
Sites not aligning to the query:
7s5fB Crystal structure of mannose-6-phosphate reductase from celery (apium graveolens) leaves with NADP+ and mannonic acid bound (see paper)
33% identity, 97% coverage: 1:259/267 of query aligns to 9:299/309 of 7s5fB
- binding d-mannonic acid: W19 (≠ F11), D46 (≠ I38), Y47 (= Y39), W78 (= W66), H107 (= H97)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G9), V18 (≠ T10), W19 (≠ F11), D42 (= D34), Y47 (= Y39), N161 (= N130), Q182 (= Q152), H208 (≠ Y178), T209 (≠ M179), P210 (≠ T180), L211 (= L181), G213 (vs. gap), A214 (vs. gap), A244 (= A204), I259 (= I219), K261 (≠ S221), S262 (= S222), S263 (≠ T223), R267 (≠ N227), E270 (≠ G230), N271 (= N231)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
34% identity, 99% coverage: 1:264/267 of query aligns to 10:274/277 of 4fziA
Q0PGJ6 NADPH-dependent aldo-keto reductase, chloroplastic; AtChlAKR; Aldo-keto reductase family 4 member C9; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 96% coverage: 3:257/267 of query aligns to 16:292/315 of Q0PGJ6
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
34% identity, 99% coverage: 1:264/267 of query aligns to 21:285/288 of 4gieA
- active site: D55 (= D34), Y60 (= Y39), K85 (= K64), H118 (= H97)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G9), W31 (≠ F11), D55 (= D34), Y60 (= Y39), H118 (= H97), W119 (= W98), N148 (= N130), Q169 (= Q152), W195 (≠ Y178), S196 (≠ M179), P197 (≠ T180), L198 (= L181), S200 (≠ Y183), L207 (= L187), A224 (= A204), I239 (= I219), P240 (= P220), K241 (≠ S221), S242 (= S222), R247 (≠ N227), E250 (≠ G230), N251 (= N231)
3h7uA Crystal structure of the plant stress-response enzyme akr4c9 (see paper)
33% identity, 96% coverage: 3:257/267 of query aligns to 13:289/312 of 3h7uA
- active site: S24 (≠ Q14), D44 (= D34), Y49 (= Y39), K78 (= K64), H111 (= H97)
- binding acetate ion: W21 (≠ F11), Y49 (= Y39), H111 (= H97)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G9), T20 (= T10), W21 (≠ F11), D44 (= D34), Y49 (= Y39), H111 (= H97), W112 (= W98), N156 (= N130), Q177 (= Q152), Y203 (= Y178), S204 (≠ M179), P205 (≠ T180), L206 (= L181), S208 (vs. gap), P209 (vs. gap), G210 (vs. gap), A236 (= A204), L251 (≠ I219), P252 (= P220), K253 (≠ S221), S254 (= S222), R259 (≠ N227), E262 (≠ G230), N263 (= N231)
5jh2A Crystal structure of the holo form of akr4c7 from maize (see paper)
38% identity, 90% coverage: 3:241/267 of query aligns to 12:245/257 of 5jh2A
- active site: D43 (= D34), Y48 (= Y39), K77 (= K64), H110 (= H97)
- binding adenosine-2'-5'-diphosphate: S185 (≠ M179), P186 (≠ T180), L187 (= L181), G188 (= G184), A208 (= A204), K225 (≠ S221), S226 (= S222), T227 (= T223), R231 (≠ N227), N235 (= N231)
3wbwA Crystal structure of gox0644 in complex with NADPH
37% identity, 94% coverage: 2:252/267 of query aligns to 13:257/271 of 3wbwA
- active site: D45 (= D34), Y50 (= Y39), K71 (= K64), H104 (= H97)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), H104 (= H97), N136 (= N130), W183 (≠ Y178), R184 (≠ M179), P185 (≠ T180), L186 (= L181), L192 (= L187), A209 (= A204), K226 (≠ S221), S227 (= S222), V228 (≠ T223), R232 (≠ N227), E235 (≠ G230), N236 (= N231)
P06632 2,5-diketo-D-gluconic acid reductase A; 2,5-DKG reductase A; 2,5-DKGR A; 25DKGR-A; AKR5C; EC 1.1.1.346 from Corynebacterium sp. (strain ATCC 31090) (see 3 papers)
41% identity, 94% coverage: 2:253/267 of query aligns to 13:264/278 of P06632
- Y50 (= Y39) active site, Proton donor
- H108 (= H97) binding
- 188:242 (vs. 179:231, 31% identical) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1a80A Native 2,5-diketo-d-gluconic acid reductase a from corynbacterium sp. Complexed with NADPH (see paper)
41% identity, 94% coverage: 2:253/267 of query aligns to 12:263/277 of 1a80A
- active site: D44 (= D34), Y49 (= Y39), K74 (= K64), H107 (= H97)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G9), F21 (= F11), D44 (= D34), Y49 (= Y39), H107 (= H97), S138 (= S129), Q160 (= Q152), W186 (≠ Y178), G187 (≠ M179), P188 (≠ T180), L189 (= L181), Q191 (≠ Y183), A214 (= A204), F229 (≠ I219), K231 (≠ S221), S232 (= S222), V233 (≠ T223), R234 (≠ K224), R237 (≠ N227), E240 (≠ G230), N241 (= N231)
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)
38% identity, 96% coverage: 2:256/267 of query aligns to 21:273/283 of A0QV09
- G196 (≠ M179) binding
- L198 (= L181) binding
- V200 (≠ Y183) binding
- I236 (= I219) binding
- R238 (≠ S221) binding
- S239 (= S222) binding
- A240 (≠ T223) binding
- R244 (≠ N227) binding
- S247 (≠ G230) binding
- N248 (= N231) binding
Sites not aligning to the query:
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
38% identity, 96% coverage: 2:256/267 of query aligns to 12:264/274 of 2wzmA
- active site: D44 (= D34), Y49 (= Y39), K74 (= K64), H107 (= H97)
- 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 (= Y178), G187 (≠ M179), P188 (≠ T180), L189 (= L181), G190 (≠ A182), V191 (≠ Y183), G192 (= G184), L195 (= L187), A212 (= A204), I227 (= I219), R229 (≠ S221), S230 (= S222), R235 (≠ N227), N239 (= N231)
Sites not aligning to the query:
1m9hA Corynebacterium 2,5-dkgr a and phe 22 replaced with tyr (f22y), lys 232 replaced with gly (k232g), arg 238 replaced with his (r238h)and ala 272 replaced with gly (a272g)in presence of nadh cofactor (see paper)
40% identity, 94% coverage: 2:253/267 of query aligns to 12:263/277 of 1m9hA
- active site: D44 (= D34), Y49 (= Y39), K74 (= K64), H107 (= H97)
- binding nicotinamide-adenine-dinucleotide: G19 (= G9), Y21 (≠ F11), Y49 (= Y39), H107 (= H97), Q160 (= Q152), W186 (≠ Y178), G187 (≠ M179), P188 (≠ T180), L189 (= L181), Q191 (≠ Y183), A214 (= A204), F229 (≠ I219), P230 (= P220), G231 (≠ S221), H237 (≠ N227), N241 (= N231)
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)
31% identity, 99% coverage: 3:266/267 of query aligns to 20:305/312 of P14065
- Q29 (≠ R12) mutation to K: Decreases catalytic activity.
- Y56 (= Y39) mutation to L: Loss of catalytic activity.
- K264 (≠ S221) mutation to R: Decreases catalytic activity.
- N267 (≠ K224) mutation to Q: Decreases catalytic activity.
- R270 (≠ N227) mutation R->H,Y,K: Decreases catalytic activity.
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
33% identity, 95% coverage: 3:255/267 of query aligns to 15:264/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
33% identity, 95% coverage: 3:255/267 of query aligns to 20:269/281 of 1vbjA
- active site: D52 (= D34), Y57 (= Y39), K82 (= K64), H115 (= H97)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G9), M27 (≠ T10), W28 (≠ F11), D52 (= D34), Y57 (= Y39), H115 (= H97), N145 (= N130), Q166 (= Q152), W192 (≠ Y178), S193 (≠ M179), P194 (≠ T180), L195 (= L181), Q197 (≠ Y183), G198 (= G184), V201 (≠ L187), A218 (= A204), I233 (= I219), K235 (≠ S221), S236 (= S222), G237 (≠ T223), R241 (≠ N227), E244 (≠ G230), N245 (= N231)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
37% identity, 96% coverage: 1:256/267 of query aligns to 14:266/275 of 3d3fA
- active site: D48 (= D34), Y53 (= Y39), K78 (= K64), H111 (= H97)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G9), F24 (= F11), D48 (= D34), Y53 (= Y39), H111 (= H97), S140 (= S129), N141 (= N130), Q162 (= Q152), W188 (≠ Y178), S189 (≠ M179), P190 (≠ T180), L191 (= L181), Q193 (≠ Y183), L197 (= L187), I229 (= I219), K231 (≠ S221), S232 (= S222), K234 (= K224), R237 (≠ N227), E240 (≠ G230), N241 (= N231)
7f7mA Akr4c17 in complex with NADP+ and glyphosate
37% identity, 97% coverage: 3:262/267 of query aligns to 12:297/309 of 7f7mA
- binding glyphosate: Y48 (= Y39), W79 (= W66), H110 (= H97), W111 (= W98)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G9), T19 (= T10), W20 (≠ F11), D43 (= D34), Y48 (= Y39), H110 (= H97), Q175 (= Q152), Y201 (= Y178), S202 (≠ M179), P203 (≠ T180), L204 (= L181), S206 (≠ Y183), P207 (vs. gap), A234 (= A204), L249 (≠ I219), P250 (= P220), K251 (≠ S221), S252 (= S222), T253 (= T223), R257 (≠ N227), N261 (= N231)
Query Sequence
>Pf1N1B4_128 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_128
MSIPAFGLGTFRLQGQVVIDSVSTGLELGYRVIDTAQIYKNEAEVGQAIAASGIARDELF
ITSKIWVANFAKDRLIDSLKESLNKLQTDYLDLTLIHWPSPEDQVPVEEFMGALLQAKQL
GLTRKIGVSNFTVDLMQQAITAIGAENIATNQIELHPYLQNRKVVEFAQSQGIRITSYMT
LAYGEVLKDPLIQQIADRLQATPAQVTLAWAMQLGYAVIPSSTKRANLQGNLQACALTLS
DADMALIAALDRGQRLTSPKGIAPQWD
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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