SitesBLAST
Comparing WP_108402347.1 NCBI__GCF_003063475.1:WP_108402347.1 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)
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)
36% identity, 97% coverage: 9:480/485 of query aligns to 22:495/505 of 4neaA
- active site: N166 (= N151), K189 (= K174), E264 (= E250), C298 (= C284), E399 (= E384), E476 (≠ L461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P149), K189 (= K174), E192 (≠ P177), G222 (= G208), G226 (≠ A212), G242 (= G228), G243 (≠ S229), T246 (= T232), H249 (≠ R235), I250 (= I236), C298 (= C284), E399 (= E384), F401 (= F386)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
35% identity, 97% coverage: 8:479/485 of query aligns to 20:489/491 of 5gtlA
- active site: N165 (= N151), K188 (= K174), E263 (= E250), C297 (= C284), E394 (= E384), E471 (≠ L461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I147), P163 (= P149), K188 (= K174), A190 (= A176), E191 (≠ P177), Q192 (= Q178), G221 (= G208), G225 (≠ A212), G241 (= G228), S242 (= S229), T245 (= T232), L264 (= L251), C297 (= C284), E394 (= E384), F396 (= F386)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
35% identity, 97% coverage: 8:479/485 of query aligns to 20:489/491 of 5gtkA
- active site: N165 (= N151), K188 (= K174), E263 (= E250), C297 (= C284), E394 (= E384), E471 (≠ L461)
- binding nicotinamide-adenine-dinucleotide: I161 (= I147), I162 (≠ V148), P163 (= P149), W164 (= W150), K188 (= K174), E191 (≠ P177), G221 (= G208), G225 (≠ A212), A226 (≠ Q213), F239 (= F226), G241 (= G228), S242 (= S229), T245 (= T232), Y248 (≠ R235), L264 (= L251), C297 (= C284), Q344 (≠ S331), R347 (= R334), E394 (= E384), F396 (= F386)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
37% identity, 97% coverage: 8:476/485 of query aligns to 14:484/494 of 4pz2B
- active site: N159 (= N151), K182 (= K174), E258 (= E250), C292 (= C284), E392 (= E384), D469 (≠ L461)
- binding nicotinamide-adenine-dinucleotide: I155 (= I147), I156 (≠ V148), P157 (= P149), W158 (= W150), N159 (= N151), M164 (≠ L156), K182 (= K174), A184 (= A176), E185 (≠ P177), G215 (= G208), G219 (≠ A212), F233 (= F226), T234 (= T227), G235 (= G228), S236 (= S229), V239 (≠ T232), E258 (= E250), L259 (= L251), C292 (= C284), E392 (= E384), F394 (= F386)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
37% identity, 97% coverage: 8:476/485 of query aligns to 13:477/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E250), C288 (= C284), E385 (= E384), E462 (≠ L461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (= A176), S182 (≠ P177), A212 (≠ G208), G216 (≠ A212), G232 (= G228), S233 (= S229), I236 (≠ T232), C288 (= C284), K338 (≠ R334), E385 (= E384), F387 (= F386)
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)
37% identity, 97% coverage: 8:476/485 of query aligns to 14:478/482 of P25526
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)
33% identity, 97% coverage: 8:479/485 of query aligns to 11:485/497 of P17202
- I28 (≠ V25) binding K(+)
- D96 (≠ E92) binding K(+)
- SPW 156:158 (≠ VPW 148:150) binding NAD(+)
- Y160 (≠ A152) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPS-E 182:185 (≠ KPAPQ 174:178) binding NAD(+)
- L186 (≠ T179) binding K(+)
- SSAT 236:239 (≠ SNAT 229:232) binding NAD(+)
- V251 (≠ M244) binding in other chain
- L258 (= L251) binding NAD(+)
- W285 (≠ I278) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E384) binding NAD(+)
- A441 (≠ T435) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ L444) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ T450) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R454) 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)
34% identity, 97% coverage: 8:476/485 of query aligns to 23:491/501 of Q56YU0
- G152 (≠ S134) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A401) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
35% identity, 97% coverage: 8:476/485 of query aligns to 9:476/486 of 4pxlA
- active site: N154 (= N151), K177 (= K174), E253 (= E250), C287 (= C284), E384 (= E384), D461 (≠ L461)
- binding nicotinamide-adenine-dinucleotide: I150 (= I147), V151 (= V148), P152 (= P149), W153 (= W150), K177 (= K174), E180 (≠ P177), G210 (= G208), G214 (≠ A212), A215 (≠ Q213), F228 (= F226), G230 (= G228), S231 (= S229), V234 (≠ T232), E253 (= E250), G255 (= G252), C287 (= C284), Q334 (≠ S331), K337 (≠ R334), E384 (= E384), F386 (= F386)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
33% identity, 97% coverage: 8:479/485 of query aligns to 9:483/495 of 4v37A