SitesBLAST
Comparing PfGW456L13_1974 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1974 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)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
80% 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)
60% 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)
60% 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% 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)
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)
36% identity, 94% coverage: 6:462/488 of query aligns to 15:472/482 of P25526
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 (≠ H228), L264 (≠ M245), C297 (= C278), Q344 (≠ A327), R347 (≠ A330), E394 (= E376), F396 (= F378)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
33% 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)
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)
31% identity, 94% coverage: 5:462/488 of query aligns to 13:476/487 of Q9H2A2
- R109 (≠ S101) 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.
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
32% identity, 93% coverage: 1:453/488 of query aligns to 5:461/489 of 6wsbA
- active site: N152 (= N146), E250 (= E244), C284 (= C278)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F142), G149 (= G143), A150 (≠ P144), W151 (≠ Y145), N152 (= N146), K175 (= K169), E178 (= E172), G208 (≠ R202), G211 (= G205), A212 (≠ I206), F225 (= F219), T226 (= T220), G227 (= G221), G228 (≠ S222), T231 (= T225), V235 (≠ L229), E250 (= E244), L251 (≠ M245), G252 (= G246), C284 (= C278), E385 (= E376), F387 (= F378)
Sites not aligning to the query:
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 94% coverage: 2:461/488 of query aligns to 10:479/505 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.
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
34% 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 (≠ H228), G256 (= G246)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
33% 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 (≠ S101), F185 (= F147), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2j5nA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding glycine: S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ F142), A181 (≠ G143), P182 (= P144), W183 (≠ Y145), N184 (= N146), I189 (≠ L151), K207 (= K169), E210 (= E172), G240 (vs. gap), F258 (= F219), T259 (= T220), G260 (= G221), S261 (= S222), V264 (≠ T225), E288 (= E244), T289 (≠ M245), C322 (= C278), E417 (= E376), F419 (= F378)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2ej6A
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding d-proline: E137 (≠ S101), F185 (= F147), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2eitA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding alanine: S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ F142), A181 (≠ G143), W183 (≠ Y145), N184 (= N146), I189 (≠ L151), K207 (= K169), E210 (= E172), G240 (vs. gap), E241 (≠ R202), G244 (= G205), F258 (= F219), T259 (= T220), G260 (= G221), S261 (= S222), V264 (≠ T225), E288 (= E244), G290 (= G246), C322 (= C278), E417 (= E376), F419 (= F378)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2eiiA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ F142), A181 (≠ G143), P182 (= P144), W183 (≠ Y145), N184 (= N146), I189 (≠ L151), K207 (= K169), E210 (= E172), G240 (vs. gap), E241 (≠ R202), G244 (= G205), F258 (= F219), T259 (= T220), G260 (= G221), S261 (= S222), V264 (≠ T225), E288 (= E244), T289 (≠ M245), C322 (= C278), E417 (= E376), F419 (= F378)
- binding valine: E137 (≠ S101), F185 (= F147), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2ehuA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ F142), A181 (≠ G143), P182 (= P144), W183 (≠ Y145), N184 (= N146), I189 (≠ L151), K207 (= K169), E210 (= E172), G240 (vs. gap), F258 (= F219), T259 (= T220), G260 (= G221), S261 (= S222), V264 (≠ T225), E288 (= E244), T289 (≠ M245), C322 (= C278), E417 (= E376), F419 (= F378)
- binding serine: F185 (= F147), C322 (= C278), S323 (≠ T279), G477 (= G436), A478 (= A437), F485 (= F443)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
32% identity, 94% coverage: 4:463/488 of query aligns to 40:503/516 of 2ehqA
- active site: N184 (= N146), K207 (= K169), E288 (= E244), C322 (= C278), E417 (= E376), T497 (≠ S455)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (≠ F142), A181 (≠ G143), P182 (= P144), W183 (≠ Y145), N184 (= N146), I189 (≠ L151), K207 (= K169), A209 (≠ S171), E210 (= E172), V239 (≠ A201), G240 (vs. gap), E241 (≠ R202), F258 (= F219), T259 (= T220), G260 (= G221), S261 (= S222), V264 (≠ T225), E288 (= E244), T289 (≠ M245), C322 (= C278), E417 (= E376), F419 (= F378)
Query Sequence
>PfGW456L13_1974 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1974
MKSLYIAGEWLAGGGEAFESLNPVTQQVLWSGVGATAGQVESAVQAARQAFPDWARRTLE
ERISVLEAFAAALKNHADELAHTIGEETGKPLWEAATEVTSMVNKIAISVQSYRERTGEK
SGPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVLFKPSELTPKVAEL
TVKCWIEAGLPAGVLNLLQGARETGIALAANPGIDGLFFTGSSRTGNHLHQQFAGRPDKI
LALEMGGNNPLVVDQVADLDAAVYTIIQSAFISAGQRCTCARRLLVPQGAWGDSLLARLV
AVSSTLSVGAFDQQPAPFMGSVVSLGAAKALMDAQEHLLANGAVALLEMTQPQAQSALLT
PGILDVSAVADRPDEELFGPLLQVIRYADFEAAIAEANDTAYGLAAGLLSDSEARYQQFW
LESRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETPSLVLPSA
LTPGVKMA
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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