SitesBLAST
Comparing AZOBR_RS31000 FitnessBrowser__azobra:AZOBR_RS31000 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
51% identity, 100% coverage: 2:478/479 of query aligns to 9:483/485 of 6x9lA
- active site: N154 (= N149), E252 (= E247), A286 (≠ C281), E462 (= E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), T151 (= T146), W153 (= W148), N154 (= N149), Q159 (= Q154), K177 (= K172), E180 (= E175), G210 (= G205), P211 (≠ A206), G214 (= G209), T229 (= T224), G230 (= G225), S231 (= S226), E252 (= E247), L253 (= L248), A286 (≠ C281), E386 (= E381), F388 (= F383), F451 (= F446)
- binding octanal: W155 (= W150), S285 (= S280)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
43% identity, 99% coverage: 1:474/479 of query aligns to 2:451/454 of 3ty7B
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
41% identity, 98% coverage: 5:472/479 of query aligns to 6:475/483 of 3b4wA
- active site: N154 (= N149), K177 (= K172), E251 (= E247), C285 (= C281), E384 (= E381), E460 (= E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), V151 (≠ T146), W153 (= W148), N154 (= N149), K177 (= K172), I210 (≠ A206), G213 (= G209), T228 (= T224), G229 (= G225), S230 (= S226), V233 (≠ A229), E236 (≠ S232), E251 (= E247), L252 (= L248), C285 (= C281), E384 (= E381), F386 (= F383)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 98% coverage: 6:475/479 of query aligns to 18:489/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E381), E471 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (≠ S174), E191 (= E175), Q192 (≠ F176), G221 (= G205), G225 (= G209), G241 (= G225), S242 (= S226), T245 (≠ A229), L264 (= L248), C297 (= C281), E394 (= E381), F396 (= F383)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 98% coverage: 6:475/479 of query aligns to 18:489/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E381), E471 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ T146), P163 (= P147), W164 (= W148), K188 (= K172), E191 (= E175), G221 (= G205), G225 (= G209), A226 (≠ P210), F239 (≠ L223), G241 (= G225), S242 (= S226), T245 (≠ A229), Y248 (≠ S232), L264 (= L248), C297 (= C281), Q344 (= Q328), R347 (= R331), E394 (= E381), F396 (= F383)
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)
37% identity, 99% coverage: 4:475/479 of query aligns to 17:494/505 of 4neaA
- active site: N166 (= N149), K189 (= K172), E264 (= E247), C298 (= C281), E399 (= E381), E476 (= E457)
- binding nicotinamide-adenine-dinucleotide: P164 (= P147), K189 (= K172), E192 (= E175), G222 (= G205), G226 (= G209), G242 (= G225), G243 (≠ S226), T246 (≠ A229), H249 (≠ S232), I250 (≠ V233), C298 (= C281), E399 (= E381), F401 (= F383)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 97% coverage: 6:472/479 of query aligns to 7:476/486 of 4pxlA
- active site: N154 (= N149), K177 (= K172), E253 (= E247), C287 (= C281), E384 (= E381), D461 (≠ E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), V151 (≠ T146), P152 (= P147), W153 (= W148), K177 (= K172), E180 (= E175), G210 (= G205), G214 (= G209), A215 (≠ P210), F228 (≠ L223), G230 (= G225), S231 (= S226), V234 (≠ A229), E253 (= E247), G255 (= G249), C287 (= C281), Q334 (= Q328), K337 (≠ R331), E384 (= E381), F386 (= F383)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
39% identity, 97% coverage: 8:472/479 of query aligns to 30:501/515 of 2d4eC
- active site: N173 (= N149), K196 (= K172), E271 (= E247), C305 (= C281), E409 (= E381), E486 (= E457)
- binding nicotinamide-adenine-dinucleotide: I169 (= I145), T170 (= T146), P171 (= P147), W172 (= W148), K196 (= K172), A198 (≠ S174), G229 (= G205), G233 (= G209), A234 (≠ P210), T248 (= T224), G249 (= G225), E250 (≠ S226), T253 (≠ A229), E271 (= E247), L272 (= L248), C305 (= C281), E409 (= E381), F411 (= F383), F475 (= F446)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 98% coverage: 5:472/479 of query aligns to 10:487/505 of O24174
- N164 (= N149) 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 (≠ C157) 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.
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)
37% identity, 97% coverage: 6:472/479 of query aligns to 21:491/501 of Q56YU0
- G152 (vs. gap) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A398) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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, 98% coverage: 5:472/479 of query aligns to 8:482/497 of P17202
- I28 (≠ L26) binding
- D96 (≠ E92) binding
- SPW 156:158 (≠ TPW 146:148) binding
- Y160 (≠ W150) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ C157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 172:175) binding
- L186 (≠ F176) binding
- SSAT 236:239 (≠ STRA 226:229) binding
- V251 (≠ I241) binding in other chain
- L258 (= L248) binding
- W285 (≠ S275) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ M432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ I440) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F446) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K450) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
36% identity, 98% coverage: 5:472/479 of query aligns to 6:480/495 of 4v37A
- active site: N157 (= N149), K180 (= K172), E255 (= E247), A289 (≠ C281), E388 (= E381), E465 (= E457)
- binding 3-aminopropan-1-ol: C448 (≠ I440), W454 (≠ F446)
- binding nicotinamide-adenine-dinucleotide: I153 (= I145), S154 (≠ T146), P155 (= P147), W156 (= W148), N157 (= N149), M162 (≠ Q154), K180 (= K172), S182 (= S174), E183 (= E175), G213 (= G205), G217 (= G209), A218 (≠ P210), T232 (= T224), G233 (= G225), S234 (= S226), T237 (≠ A229), E255 (= E247), L256 (= L248), A289 (≠ C281), E388 (= E381), F390 (= F383)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 12:484/493 of 4fr8A
- active site: N162 (= N149), K185 (= K172), Q261 (≠ E247), C295 (= C281), E392 (= E381), E469 (= E457)
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ T146), W161 (= W148), K185 (= K172), G218 (= G205), G222 (= G209), A223 (≠ P210), F236 (≠ L223), G238 (= G225), S239 (= S226), I242 (≠ A229), Q342 (= Q328), K345 (≠ R331), E392 (= E381), F394 (= F383)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ W150), L166 (≠ N153), W170 (≠ C157), F289 (≠ S275), S294 (= S280), C295 (= C281), D450 (≠ S439), F452 (≠ D441)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 15:487/496 of 4fr8C
- active site: N165 (= N149), K188 (= K172), Q264 (≠ E247), C298 (= C281), E395 (= E381), E472 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ T146), W164 (= W148), K188 (= K172), G221 (= G205), G225 (= G209), A226 (≠ P210), F239 (≠ L223), G241 (= G225), S242 (= S226), I245 (≠ A229), Q345 (= Q328), E395 (= E381), F397 (= F383)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 5l13A
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ W150), M168 (≠ Q154), W171 (≠ C157), F290 (≠ S275), C295 (≠ S280), C296 (= C281), C297 (≠ N282), D451 (≠ S439), F453 (≠ D441)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 4kwgA
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ W150), M168 (≠ Q154), C295 (≠ S280), C296 (= C281), C297 (≠ N282), D451 (≠ S439), F453 (≠ D441)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 4kwfA
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ W150), M168 (≠ Q154), W171 (≠ C157), E262 (= E247), C295 (≠ S280), C296 (= C281), C297 (≠ N282), D451 (≠ S439), F453 (≠ D441), F459 (= F446)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 3sz9A
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ W150), C295 (≠ S280), C296 (= C281), D451 (≠ S439), F453 (≠ D441), F459 (= F446)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 3injA
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ A99), F164 (≠ W150), L167 (≠ N153), F286 (≠ R271), F290 (≠ S275), D451 (≠ S439), F453 (≠ D441)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
39% identity, 98% coverage: 4:472/479 of query aligns to 13:485/494 of 2vleA
- active site: N163 (= N149), K186 (= K172), E262 (= E247), C296 (= C281), E393 (= E381), E470 (= E457)
- binding daidzin: M118 (≠ A99), F164 (≠ W150), M168 (≠ Q154), W171 (≠ C157), F286 (≠ R271), F290 (≠ S275), C295 (≠ S280), C296 (= C281), D451 (≠ S439), V452 (≠ I440), F453 (≠ D441)
Query Sequence
>AZOBR_RS31000 FitnessBrowser__azobra:AZOBR_RS31000
MKTCQSFYIGGAWTEPAAGATVMEVLNPATEQVSGTVALGGPEDAQRAVAAAHAAFDGFS
RTPLNERLELLAAVCALFEKRMDEVADAITEEMGAPLAALSKPAQAFMGLAHFKTALEAA
REYPFERTRGTTRILREPVGVCAMITPWNWPINQIACKVAPALATGCTMVLKPSEFAPYS
AWIFAEILHEAGVPAGVFNMFYGDGAVVGPVLASHPLVDMVSLTGSTRAGASVSHNAADS
IKRVSLELGGKSANIICESADLTKAVTHGVRSMMSNTGQSCNAPSRMYVPASRLDEAETI
AAQVCARLVVGDPRGDRTGVGPIANQRQYERVQRLIQAGIEEGATLLCGGPGRPDGLERG
FYAKPTVFSRATDGMTIMREEIFGPVLTIRPYEDIEEAIRSANDSLYGLSGYVYAGTVDE
ARAVAKRLRTGMVHLNGASIDLAAPFGGYKQSGIGREWGEVGFEEFLETKSVYGNEPAA
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