SitesBLAST
Comparing WP_089303116.1 NCBI__GCF_900188115.1:WP_089303116.1 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)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
46% identity, 96% coverage: 14:498/503 of query aligns to 3:480/486 of 4pxlA
- active site: N154 (= N169), K177 (= K192), E253 (= E267), C287 (= C303), E384 (= E403), D461 (≠ E479)
- binding nicotinamide-adenine-dinucleotide: I150 (= I165), V151 (≠ L166), P152 (= P167), W153 (= W168), K177 (= K192), E180 (= E195), G210 (= G225), G214 (= G229), A215 (≠ E230), F228 (= F243), G230 (= G245), S231 (= S246), V234 (= V249), E253 (= E267), G255 (= G269), C287 (= C303), Q334 (= Q350), K337 (≠ R353), E384 (= E403), F386 (= F405)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 96% coverage: 18:498/503 of query aligns to 18:490/491 of 5gtlA
- active site: N165 (= N169), K188 (= K192), E263 (= E267), C297 (= C303), E394 (= E403), E471 (= E479)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I165), P163 (= P167), K188 (= K192), A190 (≠ S194), E191 (= E195), Q192 (≠ Y196), G221 (= G225), G225 (= G229), G241 (= G245), S242 (= S246), T245 (≠ V249), L264 (= L268), C297 (= C303), E394 (= E403), F396 (= F405)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 96% coverage: 18:498/503 of query aligns to 18:490/491 of 5gtkA
- active site: N165 (= N169), K188 (= K192), E263 (= E267), C297 (= C303), E394 (= E403), E471 (= E479)
- binding nicotinamide-adenine-dinucleotide: I161 (= I165), I162 (≠ L166), P163 (= P167), W164 (= W168), K188 (= K192), E191 (= E195), G221 (= G225), G225 (= G229), A226 (≠ E230), F239 (= F243), G241 (= G245), S242 (= S246), T245 (≠ V249), Y248 (≠ R252), L264 (= L268), C297 (= C303), Q344 (= Q350), R347 (= R353), E394 (= E403), F396 (= F405)
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: 14:498/503 of query aligns to 17:495/501 of Q56YU0
- G152 (≠ T152) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A420) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
46% identity, 96% coverage: 14:498/503 of query aligns to 8:488/494 of 4pz2B
- active site: N159 (= N169), K182 (= K192), E258 (= E267), C292 (= C303), E392 (= E403), D469 (≠ E479)
- binding nicotinamide-adenine-dinucleotide: I155 (= I165), I156 (≠ L166), P157 (= P167), W158 (= W168), N159 (= N169), M164 (≠ L174), K182 (= K192), A184 (≠ S194), E185 (= E195), G215 (= G225), G219 (= G229), F233 (= F243), T234 (= T244), G235 (= G245), S236 (= S246), V239 (= V249), E258 (= E267), L259 (= L268), C292 (= C303), E392 (= E403), F394 (= F405)
7radA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:496/503 of query aligns to 13:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ L166), P160 (= P167), W161 (= W168), N162 (= N169), M167 (≠ L174), K185 (= K192), E188 (= E195), G218 (= G225), G222 (= G229), A223 (≠ E230), T237 (= T244), G238 (= G245), S239 (= S246), V242 (= V249), E261 (= E267), L262 (= L268), C295 (= C303), E392 (= E403), F394 (= F405)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ T118), E117 (≠ A122), F163 (≠ A170), E285 (≠ G292), F289 (≠ M296), N450 (≠ Q461), V452 (vs. gap)
7mjdA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:496/503 of query aligns to 13:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ L166), P160 (= P167), W161 (= W168), N162 (= N169), M167 (≠ L174), K185 (= K192), E188 (= E195), G218 (= G225), G222 (= G229), F236 (= F243), T237 (= T244), G238 (= G245), S239 (= S246), V242 (= V249), E261 (= E267), L262 (= L268), C295 (= C303), E392 (= E403), F394 (= F405)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A122), E285 (≠ G292), F289 (≠ M296), N450 (≠ Q461), V452 (vs. gap)
7mjcA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:496/503 of query aligns to 13:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ L166), P160 (= P167), W161 (= W168), N162 (= N169), K185 (= K192), E188 (= E195), G218 (= G225), G222 (= G229), T237 (= T244), G238 (= G245), S239 (= S246), V242 (= V249), E261 (= E267), L262 (= L268), C295 (= C303), E392 (= E403), F394 (= F405)
P05091 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Homo sapiens (Human) (see 5 papers)
41% identity, 99% coverage: 2:498/503 of query aligns to 22:512/517 of P05091
- E337 (= E321) to V: in dbSNP:rs1062136
- E496 (≠ Q482) to K: in allele ALDH2*3; dbSNP:rs769724893
- E504 (= E490) to K: in AMEDS; allele ALDH2*2; drastic reduction of enzyme activity; dbSNP:rs671
Sites not aligning to the query:
5l13A Structure of aldh2 in complex with 2p3 (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 5l13A
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ A170), M168 (≠ L174), W171 (≠ Q177), F290 (≠ M296), C295 (≠ A302), C296 (= C303), C297 (≠ V304), D451 (≠ Q461), F453 (vs. gap)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 4kwgA
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ A170), M168 (≠ L174), C295 (≠ A302), C296 (= C303), C297 (≠ V304), D451 (≠ Q461), F453 (vs. gap)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 4kwfA
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ A170), M168 (≠ L174), W171 (≠ Q177), E262 (= E267), C295 (≠ A302), C296 (= C303), C297 (≠ V304), D451 (≠ Q461), F453 (vs. gap), F459 (= F468)
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)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 3sz9A
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ A170), C295 (≠ A302), C296 (= C303), D451 (≠ Q461), F453 (vs. gap), F459 (= F468)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 3injA
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ A122), F164 (≠ A170), L167 (= L173), F286 (≠ G292), F290 (≠ M296), D451 (≠ Q461), F453 (vs. gap)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 2vleA
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding daidzin: M118 (≠ A122), F164 (≠ A170), M168 (≠ L174), W171 (≠ Q177), F286 (≠ G292), F290 (≠ M296), C295 (≠ A302), C296 (= C303), D451 (≠ Q461), V452 (≠ L462), F453 (vs. gap)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 1o01B
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding (2e)-but-2-enal: C296 (= C303), C297 (≠ V304), F453 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: I159 (= I165), I160 (≠ L166), P161 (= P167), W162 (= W168), K186 (= K192), E189 (= E195), G219 (= G225), G223 (= G229), A224 (≠ E230), F237 (= F243), G239 (= G245), S240 (= S246), I243 (≠ V249), L263 (= L268), G264 (= G269), C296 (= C303), Q343 (= Q350), E393 (= E403), F395 (= F405)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 11:489/494 of 1cw3A
- active site: N163 (= N169), K186 (= K192), E262 (= E267), C296 (= C303), E393 (= E403), E470 (= E479)
- binding magnesium ion: V34 (≠ R37), D103 (= D105), Q190 (≠ Y196)
- binding nicotinamide-adenine-dinucleotide: I159 (= I165), I160 (≠ L166), P161 (= P167), W162 (= W168), K186 (= K192), G219 (= G225), G223 (= G229), A224 (≠ E230), F237 (= F243), G239 (= G245), S240 (= S246), I243 (≠ V249), L263 (= L268), G264 (= G269), C296 (= C303), Q343 (= Q350), K346 (≠ R353), E393 (= E403), F395 (= F405)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
40% identity, 99% coverage: 2:498/503 of query aligns to 1:491/496 of 4fr8C
- active site: N165 (= N169), K188 (= K192), Q264 (≠ E267), C298 (= C303), E395 (= E403), E472 (= E479)
- binding nicotinamide-adenine-dinucleotide: I161 (= I165), I162 (≠ L166), W164 (= W168), K188 (= K192), G221 (= G225), G225 (= G229), A226 (≠ E230), F239 (= F243), G241 (= G245), S242 (= S246), I245 (≠ V249), Q345 (= Q350), E395 (= E403), F397 (= F405)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
41% identity, 98% coverage: 2:496/503 of query aligns to 25:513/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
41% identity, 96% coverage: 14:498/503 of query aligns to 10:488/493 of 4fr8A
- active site: N162 (= N169), K185 (= K192), Q261 (≠ E267), C295 (= C303), E392 (= E403), E469 (= E479)
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ L166), W161 (= W168), K185 (= K192), G218 (= G225), G222 (= G229), A223 (≠ E230), F236 (= F243), G238 (= G245), S239 (= S246), I242 (≠ V249), Q342 (= Q350), K345 (≠ R353), E392 (= E403), F394 (= F405)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ A170), L166 (= L173), W170 (≠ Q177), F289 (≠ M296), S294 (≠ A302), C295 (= C303), D450 (≠ Q461), F452 (vs. gap)
Query Sequence
>WP_089303116.1 NCBI__GCF_900188115.1:WP_089303116.1
MTLSVLSHRDELGVRTGQLLVDGHWGAADGGATWTHRHPATGEVIGEFARASATDVDAAV
AAARRSFEAGTWSRARAGERIAVLQRYGRLLREHADELRGLQALDNSVPLSFGSIYATSV
GAAADVFDHHAGWVDKIGGQTLPPYQGGDHLTMTFREPLGVVAAILPWNAPFLLFAQKVA
PALAAGCSVVLKPSEYATYSVLRMVELLAEAGLPAGVLNMVTGTGEECGEALITHSDVDK
VSFTGSRGVGKRIVEASAGTLKRVSLELGGKSPAVVFDDAPDVTIAASTVVGAVTMGLSG
QACVANTRALVHRDIYDEFLEAAKGMASAITFGDPFDPGVLASPLINEQQLERVLGYIAK
GKEEGATLVMGGERLEGEYSAGNFVSPTIFADVDNSSTIAQEEIFGPVLSVVPFGDEEEA
IRLANDTEYGLGAGVFTSDVQRAFRVSRGVRAGTVGINGFQLEPHAPFGGFKQSGLGREG
GQSAFEAYTELKTVMMPLGDELM
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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