SitesBLAST
Comparing Pf6N2E2_5668 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5668 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
82% identity, 99% coverage: 1:485/488 of query aligns to 2:486/486 of 3ju8A
- active site: N147 (= N146), K170 (= K169), E245 (= E244), C279 (= C278), E377 (= E376), P455 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: G144 (= G143), Y146 (= Y145), N147 (= N146), L152 (= L151), K170 (= K169), S172 (= S171), F220 (= F219), T221 (= T220), G222 (= G221), S223 (= S222), T226 (= T225), E245 (= E244), M246 (= M245), G247 (= G246), C279 (= C278), E377 (= E376), F379 (= F378), F444 (= F443)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
61% identity, 99% coverage: 3:487/488 of query aligns to 5:488/488 of 5u0mA
- active site: N148 (= N146), K171 (= K169), E246 (= E244), C280 (= C278), E377 (= E376), P455 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: F144 (= F142), Y147 (= Y145), N148 (= N146), K171 (= K169), S173 (= S171), E174 (= E172), G207 (= G205), T222 (= T220), G223 (= G221), S224 (= S222), V227 (≠ T225), E246 (= E244), M247 (= M245), G248 (= G246), C280 (= C278), E377 (= E376), F379 (= F378)
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
61% identity, 99% coverage: 3:487/488 of query aligns to 5:488/488 of 5u0lA
- active site: N148 (= N146), K171 (= K169), E246 (= E244), C280 (= C278), E377 (= E376), P455 (≠ A454)
- binding decanal: K107 (= K105), H152 (= H150), L153 (= L151), G156 (= G154), H157 (= H155), S456 (= S455), A457 (= A456)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 94% coverage: 6:462/488 of query aligns to 15:472/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 94% coverage: 6:462/488 of query aligns to 14:471/481 of 3jz4A
- active site: N156 (= N146), K179 (= K169), E254 (= E244), C288 (= C278), E385 (= E376), E462 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P144), W155 (≠ Y145), K179 (= K169), A181 (≠ S171), S182 (≠ E172), A212 (= A201), G216 (= G205), G232 (= G221), S233 (= S222), I236 (≠ T225), C288 (= C278), K338 (≠ D333), E385 (= E376), F387 (= F378)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
32% identity, 84% coverage: 3:410/488 of query aligns to 4:415/494 of 5izdA
- active site: N149 (= N146), K172 (= K169), E247 (= E244), C281 (= C278), E381 (= E376)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ F142), T146 (≠ G143), W148 (≠ Y145), K172 (= K169), P173 (= P170), S174 (= S171), S175 (≠ E172), R204 (vs. gap), G205 (≠ A201), G209 (= G205), D210 (≠ I206), G225 (= G221), S226 (= S222), T229 (= T225)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 94% coverage: 3:461/488 of query aligns to 18:478/491 of 5gtlA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E376), E471 (≠ A454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ F142), P163 (= P144), K188 (= K169), A190 (≠ S171), E191 (= E172), Q192 (≠ L173), G221 (≠ A201), G225 (= G205), G241 (= G221), S242 (= S222), T245 (= T225), L264 (≠ M245), C297 (= C278), E394 (= E376), F396 (= F378)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 94% coverage: 3:461/488 of query aligns to 18:478/491 of 5gtkA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E376), E471 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ F142), I162 (≠ G143), P163 (= P144), W164 (≠ Y145), K188 (= K169), E191 (= E172), G221 (≠ A201), G225 (= G205), A226 (≠ I206), F239 (= F219), G241 (= G221), S242 (= S222), T245 (= T225), Y248 (≠ L228), L264 (≠ M245), C297 (= C278), Q344 (≠ A327), R347 (≠ A330), E394 (= E376), F396 (= F378)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
30% identity, 94% coverage: 2:462/488 of query aligns to 5:476/487 of Q9H2A2
- R109 (≠ T101) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N146) mutation to A: Complete loss of activity.
- R451 (≠ A437) mutation to A: Complete loss of activity.
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 99% coverage: 1:483/488 of query aligns to 19:499/501 of Q56YU0
- G152 (vs. gap) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A393) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
31% identity, 94% coverage: 5:462/488 of query aligns to 30:494/515 of 2d4eC
- active site: N173 (= N146), K196 (= K169), E271 (= E244), C305 (= C278), E409 (= E376), E486 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F142), T170 (≠ G143), P171 (= P144), W172 (≠ Y145), K196 (= K169), A198 (≠ S171), G229 (≠ A201), G233 (= G205), A234 (≠ I206), T248 (= T220), G249 (= G221), E250 (≠ S222), T253 (= T225), E271 (= E244), L272 (≠ M245), C305 (= C278), E409 (= E376), F411 (= F378), F475 (= F443)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 94% coverage: 4:461/488 of query aligns to 12:479/505 of O24174
- N164 (= N146) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ G154) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
30% identity, 98% coverage: 1:478/488 of query aligns to 10:492/494 of 4pz2B
- active site: N159 (= N146), K182 (= K169), E258 (= E244), C292 (= C278), E392 (= E376), D469 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ F142), I156 (≠ G143), P157 (= P144), W158 (≠ Y145), N159 (= N146), M164 (≠ L151), K182 (= K169), A184 (≠ S171), E185 (= E172), G215 (≠ R202), G219 (= G205), F233 (= F219), T234 (= T220), G235 (= G221), S236 (= S222), V239 (≠ T225), E258 (= E244), L259 (≠ M245), C292 (= C278), E392 (= E376), F394 (= F378)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
31% identity, 92% coverage: 4:453/488 of query aligns to 10:469/503 of Q8VWZ1
- N27 (≠ S20) binding
- I28 (≠ L21) binding
- D99 (≠ E87) binding
- L189 (= L173) binding
- 238:245 (vs. 221:228, 63% identical) binding
- C294 (= C278) binding
- E393 (= E376) binding
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
31% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2eiwA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding proline: E137 (≠ T101), F185 (= F147), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
31% identity, 92% coverage: 4:453/488 of query aligns to 5:464/497 of 3iwkH
- active site: N157 (= N146), K180 (= K169), E255 (= E244), C289 (= C278), E388 (= E376)
- binding nicotinamide-adenine-dinucleotide: W156 (≠ Y145), G213 (≠ A201), G217 (= G205), A218 (≠ I206), G233 (= G221), S234 (= S222), T237 (= T225), K240 (≠ L228), C289 (= C278), Q336 (≠ A327), E388 (= E376), F390 (= F378)
Sites not aligning to the query:
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
32% identity, 83% coverage: 54:458/488 of query aligns to 63:466/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F142), T153 (≠ G143), P154 (= P144), K179 (= K169), A212 (= A201), K213 (≠ R202), F230 (= F219), T231 (= T220), G232 (= G221), S233 (= S222), V236 (≠ T225), W239 (≠ L228), G256 (= G246)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
31% identity, 92% coverage: 15:461/488 of query aligns to 32:483/495 of 5iuwA
- active site: N166 (= N146), K189 (= K169), E265 (= E244), C300 (= C278), E399 (= E376), D476 (≠ A454)
- binding 1h-indol-3-ylacetic acid: F167 (= F147), M170 (≠ H150), C300 (= C278), D457 (≠ T435), F465 (= F443)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F142), V163 (≠ G143), P164 (= P144), W165 (≠ Y145), N166 (= N146), K189 (= K169), G222 (≠ R202), G226 (= G205), K227 (≠ I206), F240 (= F219), T241 (= T220), G242 (= G221), S243 (= S222), I246 (≠ T225), Y253 (≠ Q232), E265 (= E244), A266 (≠ M245), C300 (= C278), E399 (= E376), F401 (= F378)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
31% identity, 92% coverage: 15:461/488 of query aligns to 32:483/495 of 5iuvA
- active site: N166 (= N146), K189 (= K169), E265 (= E244), C300 (= C278), E399 (= E376), D476 (≠ A454)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ F142), V163 (≠ G143), P164 (= P144), W165 (≠ Y145), N166 (= N146), K189 (= K169), S191 (= S171), G222 (≠ R202), G226 (= G205), K227 (≠ I206), F240 (= F219), T241 (= T220), G242 (= G221), S243 (= S222), I246 (≠ T225), Y253 (≠ Q232), E265 (= E244), A266 (≠ M245), C300 (= C278), E399 (= E376), F401 (= F378)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
32% identity, 93% coverage: 5:459/488 of query aligns to 4:461/476 of 4yweA
Query Sequence
>Pf6N2E2_5668 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5668
MNSLYIAGSWLEGQGDVFESLNPVTQQVLWSGKGATAAQVESAVQAARQAFPGWARRTLD
ERIQVLEAFAATLKSHADELAQCIGEETGKPLWEAATEVTTMVNKIAISVQSYRERTGEK
SGPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVLFKPSELTPKVAEL
TVKCWVEAGLPAGVLNLLQGARETGIALAANSGIDGLFFTGSSRTGNLLHQQFSGRPDKI
LALEMGGNNPLVVDEVADVDAAVYTIIQSAFISAGQRCTCARRLLVPEGAWGDALLARLV
AVSSTLEVGAFDQQPAPFMGAVISLGAAKALMDAQNHLLGKGAVPLLSMTQPQPQAALLT
PGILDVTTVAERPDEELFGPLLQVIRYKDFAAAITEANNTQYGLAAGLLSDSQERYQQFW
LESRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETPSLVMPAA
LTPGVRMA
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