SitesBLAST
Comparing WP_017549143.1 NCBI__GCF_000330705.1:WP_017549143.1 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
46% identity, 96% coverage: 5:487/501 of query aligns to 8:486/491 of 5gtlA
- active site: N165 (= N162), K188 (= K185), E263 (= E260), C297 (= C294), E394 (= E395), E471 (= E472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I158), P163 (= P160), K188 (= K185), A190 (= A187), E191 (≠ S188), Q192 (≠ L189), G221 (= G218), G225 (= G222), G241 (= G238), S242 (= S239), T245 (= T242), L264 (= L261), C297 (= C294), E394 (= E395), F396 (= F397)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
46% identity, 96% coverage: 5:487/501 of query aligns to 8:486/491 of 5gtkA
- active site: N165 (= N162), K188 (= K185), E263 (= E260), C297 (= C294), E394 (= E395), E471 (= E472)
- binding nicotinamide-adenine-dinucleotide: I161 (= I158), I162 (≠ V159), P163 (= P160), W164 (= W161), K188 (= K185), E191 (≠ S188), G221 (= G218), G225 (= G222), A226 (≠ D223), F239 (= F236), G241 (= G238), S242 (= S239), T245 (= T242), Y248 (≠ D245), L264 (= L261), C297 (= C294), Q344 (= Q341), R347 (≠ S344), E394 (= E395), F396 (= F397)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
44% identity, 96% coverage: 18:499/501 of query aligns to 21:503/505 of 4neaA
- active site: N166 (= N162), K189 (= K185), E264 (= E260), C298 (= C294), E399 (= E395), E476 (= E472)
- binding nicotinamide-adenine-dinucleotide: P164 (= P160), K189 (= K185), E192 (≠ S188), G222 (= G218), G226 (= G222), G242 (= G238), G243 (≠ S239), T246 (= T242), H249 (≠ D245), I250 (= I246), C298 (= C294), E399 (= E395), F401 (= F397)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
45% identity, 96% coverage: 17:495/501 of query aligns to 12:495/505 of O24174
- N164 (= N162) 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 (= W170) 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.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
43% identity, 95% coverage: 17:492/501 of query aligns to 25:498/503 of O14293
- S248 (= S239) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
44% identity, 96% coverage: 14:495/501 of query aligns to 10:492/494 of 4pz2B
- active site: N159 (= N162), K182 (= K185), E258 (= E260), C292 (= C294), E392 (= E395), D469 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I155 (= I158), I156 (≠ V159), P157 (= P160), W158 (= W161), N159 (= N162), M164 (= M167), K182 (= K185), A184 (= A187), E185 (≠ S188), G215 (= G218), G219 (= G222), F233 (= F236), T234 (= T237), G235 (= G238), S236 (= S239), V239 (≠ T242), E258 (= E260), L259 (= L261), C292 (= C294), E392 (= E395), F394 (= F397)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
44% identity, 97% coverage: 10:495/501 of query aligns to 1:484/486 of 4pxlA
- active site: N154 (= N162), K177 (= K185), E253 (= E260), C287 (= C294), E384 (= E395), D461 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I150 (= I158), V151 (= V159), P152 (= P160), W153 (= W161), K177 (= K185), E180 (≠ S188), G210 (= G218), G214 (= G222), A215 (≠ D223), F228 (= F236), G230 (= G238), S231 (= S239), V234 (≠ T242), E253 (= E260), G255 (= G262), C287 (= C294), Q334 (= Q341), K337 (≠ S344), E384 (= E395), F386 (= F397)
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)
42% identity, 96% coverage: 16:495/501 of query aligns to 9:490/497 of P17202
- I28 (= I35) binding K(+)
- D96 (≠ N103) binding K(+)
- SPW 156:158 (≠ VPW 159:161) binding NAD(+)
- Y160 (= Y163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W170) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAS 185:188) binding NAD(+)
- L186 (= L189) binding K(+)
- SSAT 236:239 (≠ STDT 239:242) binding NAD(+)
- V251 (≠ L254) binding in other chain
- L258 (= L261) binding NAD(+)
- W285 (≠ N288) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E395) binding NAD(+)
- A441 (≠ I446) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A455) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F461) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K465) binding K(+)
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)
43% identity, 96% coverage: 13:495/501 of query aligns to 18:499/501 of Q56YU0
- G152 (≠ N145) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A412) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
8rwkA Cryoem structure of the central ald4 filament determined by filamentid (see paper)
42% identity, 97% coverage: 4:487/501 of query aligns to 9:489/495 of 8rwkA