SitesBLAST
Comparing GFF3251 FitnessBrowser__Phaeo:GFF3251 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
47% identity, 99% coverage: 5:477/479 of query aligns to 12:481/485 of 6x9lA
- active site: N154 (= N151), E252 (= E249), A286 (≠ C282), E462 (= E458)
- binding nicotinamide-adenine-dinucleotide: I150 (= I147), T151 (= T148), W153 (= W150), N154 (= N151), Q159 (= Q156), K177 (= K174), E180 (= E177), G210 (= G207), P211 (≠ T208), G214 (= G211), T229 (= T226), G230 (= G227), S231 (= S228), E252 (= E249), L253 (= L250), A286 (≠ C282), E386 (= E382), F388 (= F384), F451 (= F447)
- binding octanal: W155 (= W152), S285 (= S281)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
43% identity, 99% coverage: 5:476/479 of query aligns to 3:452/454 of 3ty7B
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 98% coverage: 3:473/479 of query aligns to 15:486/491 of 5gtlA
- active site: N165 (= N151), K188 (= K174), E263 (= E249), C297 (= C282), E394 (= E382), E471 (= E458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I147), P163 (= P149), K188 (= K174), A190 (≠ S176), E191 (= E177), Q192 (= Q178), G221 (= G207), G225 (= G211), G241 (= G227), S242 (= S228), T245 (≠ A231), L264 (= L250), C297 (= C282), E394 (= E382), F396 (= F384)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 98% coverage: 3:473/479 of query aligns to 15:486/491 of 5gtkA
- active site: N165 (= N151), K188 (= K174), E263 (= E249), C297 (= C282), E394 (= E382), E471 (= E458)
- binding nicotinamide-adenine-dinucleotide: I161 (= I147), I162 (≠ T148), P163 (= P149), W164 (= W150), K188 (= K174), E191 (= E177), G221 (= G207), G225 (= G211), A226 (≠ T212), F239 (= F225), G241 (= G227), S242 (= S228), T245 (≠ A231), Y248 (≠ A234), L264 (= L250), C297 (= C282), Q344 (= Q329), R347 (≠ K332), E394 (= E382), F396 (= F384)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
40% identity, 98% coverage: 3:473/479 of query aligns to 4:475/483 of 3b4wA
- active site: N154 (= N151), K177 (= K174), E251 (= E249), C285 (= C282), E384 (= E382), E460 (= E458)
- binding nicotinamide-adenine-dinucleotide: I150 (= I147), V151 (≠ T148), W153 (= W150), N154 (= N151), K177 (= K174), I210 (≠ T208), G213 (= G211), T228 (= T226), G229 (= G227), S230 (= S228), V233 (≠ A231), E236 (≠ A234), E251 (= E249), L252 (= L250), C285 (= C282), E384 (= E382), F386 (= F384)
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)
38% identity, 97% coverage: 9:471/479 of query aligns to 15:476/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
38% identity, 97% coverage: 9:471/479 of query aligns to 14:475/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E249), C288 (= C282), E385 (= E382), E462 (= E458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (≠ S176), S182 (≠ E177), A212 (≠ G207), G216 (= G211), G232 (= G227), S233 (= S228), I236 (≠ A231), C288 (= C282), K338 (= K332), E385 (= E382), F387 (= F384)
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)
40% identity, 99% coverage: 2:473/479 of query aligns to 17:491/501 of Q56YU0
- G152 (≠ D134) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A399) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 100% coverage: 2:479/479 of query aligns to 5:491/503 of Q84LK3
- N162 (= N151) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ L159) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
36% identity, 99% coverage: 2:473/479 of query aligns to 5:482/497 of P17202
- I28 (= I25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ TPW 148:150) binding
- Y160 (≠ W152) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ L159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 174:177) binding
- L186 (≠ Q178) binding
- SSAT 236:239 (≠ STRA 228:231) binding
- V251 (≠ L243) binding in other chain
- L258 (= L250) binding
- W285 (≠ N276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E382) binding
- A441 (≠ M433) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S442) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F447) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K451) binding
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
36% identity, 100% coverage: 2:479/479 of query aligns to 5:491/503 of Q93YB2
- I28 (= I25) binding
- D99 (≠ E91) binding
- W161 (= W150) binding
- K185 (= K174) binding
- L189 (≠ Q178) binding
- S239 (= S228) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
36% identity, 100% coverage: 2:479/479 of query aligns to 2:488/500 of 3iwjA
- active site: N159 (= N151), K182 (= K174), E257 (= E249), C291 (= C282), E390 (= E382), E467 (= E458)
- binding glycerol: D110 (≠ N113), Y160 (≠ W152), W167 (≠ L159), I290 (≠ S281), C291 (= C282), C450 (≠ S442), W456 (≠ F447)
- binding nicotinamide-adenine-dinucleotide: I155 (= I147), T156 (= T148), W158 (= W150), K182 (= K174), S184 (= S176), E185 (= E177), G215 (= G207), A220 (≠ T212), F233 (= F225), G235 (= G227), S236 (= S228), T239 (≠ A231), I243 (= I235)
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
39% identity, 99% coverage: 2:473/479 of query aligns to 18:492/501 of Q28399
1o9jA The x-ray crystal structure of eta-crystallin (see paper)
39% identity, 99% coverage: 2:473/479 of query aligns to 11:485/494 of 1o9jA
- active site: N163 (= N151), K186 (= K174), E262 (= E249), C296 (= C282), E393 (= E382), E470 (= E458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I147), F160 (≠ T148), P161 (= P149), W162 (= W150), N163 (= N151), K186 (= K174), E189 (= E177), G219 (= G207), G223 (= G211), F237 (= F225), T238 (= T226), G239 (= G227), S240 (= S228), V243 (≠ A231), E262 (= E249), L263 (= L250), C296 (= C282), E393 (= E382), F395 (= F384), L421 (= L410)
P15437 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Equus caballus (Horse) (see paper)
40% identity, 97% coverage: 8:473/479 of query aligns to 24:492/501 of P15437
Sites not aligning to the query:
- 2 modified: N-acetylserine
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
35% identity, 100% coverage: 2:479/479 of query aligns to 7:493/505 of O24174
- N164 (= N151) 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 (≠ L159) 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.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 99% coverage: 2:473/479 of query aligns to 3:480/495 of 4v37A
- active site: N157 (= N151), K180 (= K174), E255 (= E249), A289 (≠ C282), E388 (= E382), E465 (= E458)
- binding 3-aminopropan-1-ol: C448 (≠ S442), W454 (≠ F447)
- binding nicotinamide-adenine-dinucleotide: I153 (= I147), S154 (≠ T148), P155 (= P149), W156 (= W150), N157 (= N151), M162 (≠ Q156), K180 (= K174), S182 (= S176), E183 (= E177), G213 (= G207), G217 (= G211), A218 (≠ T212), T232 (= T226), G233 (= G227), S234 (= S228), T237 (≠ A231), E255 (= E249), L256 (= L250), A289 (≠ C282), E388 (= E382), F390 (= F384)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 97% coverage: 7:473/479 of query aligns to 8:476/486 of 4pxlA
- active site: N154 (= N151), K177 (= K174), E253 (= E249), C287 (= C282), E384 (= E382), D461 (≠ E458)
- binding nicotinamide-adenine-dinucleotide: I150 (= I147), V151 (≠ T148), P152 (= P149), W153 (= W150), K177 (= K174), E180 (= E177), G210 (= G207), G214 (= G211), A215 (≠ T212), F228 (= F225), G230 (= G227), S231 (= S228), V234 (≠ A231), E253 (= E249), G255 (= G251), C287 (= C282), Q334 (= Q329), K337 (= K332), E384 (= E382), F386 (= F384)
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)
36% identity, 99% coverage: 2:473/479 of query aligns to 5:485/503 of Q8VWZ1
- N27 (≠ V24) binding
- I28 (= I25) binding
- D99 (≠ E91) binding
- L189 (≠ Q178) binding
- 238:245 (vs. 227:234, 38% identical) binding
- C294 (= C282) binding
- E393 (= E382) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
36% identity, 98% coverage: 5:473/479 of query aligns to 3:480/497 of 3iwkH
- active site: N157 (= N151), K180 (= K174), E255 (= E249), C289 (= C282), E388 (= E382), E465 (= E458)
- binding nicotinamide-adenine-dinucleotide: W156 (= W150), G213 (= G207), G217 (= G211), A218 (≠ T212), G233 (= G227), S234 (= S228), T237 (≠ A231), K240 (≠ A234), C289 (= C282), Q336 (= Q329), E388 (= E382), F390 (= F384)
Query Sequence
>GFF3251 FitnessBrowser__Phaeo:GFF3251
MIEKRDFYINGQWVAPAAPNDFEVIDPSTEAPCAVISLGDAADTNAAVAAAKTALPGWMT
TPVEERIALVEKLIEVYESRTEDLAQAMSVEMGAPIDMARTQQAGAGSWHLRNFIKAAKA
FSFDAPLGDHAPNDRIIHEAVGVAALITPWNWPMNQVTLKVGAAAIAGCTMVLKPSEQSP
LNAMIFAEMMDEAGFPAGVFNLVNGDGTGVGTQLSSHPDVDMVSFTGSTRAGTAISKAAA
DTLKKVHLELGGKGANVIFDDADEKAVKRGVLHMMNNTGQSCNAPSRMLVQKGIYDKAVE
EAAAVANKVEVGPASSEGRHIGPVVNELQWGKIQDLIQKGIDEGARLVAGGTGRPDGLNQ
GFYVKPTVFADVNNQMTIAREEIFGPVLSIIPFESEEDAIEIANDTPYGLTNYVQTQDLA
RANRMARKLRAGMIEMNGKSRSAGSPFGGMKQSGNGREGGSWGIEDFLEVKAVGGWADE
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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