SitesBLAST
Comparing CA265_RS24850 FitnessBrowser__Pedo557:CA265_RS24850 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)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 100% coverage: 1:452/454 of query aligns to 40:495/503 of O14293
- S248 (= S205) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
31% identity, 100% coverage: 1:453/454 of query aligns to 22:476/477 of 2opxA
- active site: N151 (= N130), K174 (= K153), E249 (= E226), C283 (= C261), E381 (= E358), A458 (≠ T435)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ G84), F152 (≠ Y131), N284 (≠ C262), F312 (≠ T290), G313 (= G291), R318 (≠ E296), D320 (vs. gap), I321 (≠ V298), A322 (≠ Y299), Y362 (= Y339), F440 (≠ R417), F440 (≠ R417), E441 (≠ V418)
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
31% identity, 100% coverage: 1:453/454 of query aligns to 22:476/477 of 2impA
- active site: N151 (= N130), K174 (= K153), E249 (= E226), C283 (= C261), E381 (= E358), A458 (≠ T435)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I126), L148 (≠ S127), P149 (≠ A128), W150 (= W129), K174 (= K153), E177 (= E156), F178 (≠ Y157), G207 (≠ K186), G211 (≠ S190), Q212 (≠ A191), S228 (= S205), A231 (≠ T208), K234 (≠ L211), R334 (≠ V311)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
31% identity, 100% coverage: 1:453/454 of query aligns to 22:476/477 of 2iluA
- active site: N151 (= N130), K174 (= K153), E249 (= E226), C283 (= C261), E381 (= E358), A458 (≠ T435)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I126), L148 (≠ S127), P149 (≠ A128), W150 (= W129), K174 (= K153), S176 (= S155), E177 (= E156), R206 (≠ A185), G207 (≠ K186), G211 (≠ S190), Q212 (≠ A191), S228 (= S205), A231 (≠ T208), K234 (≠ L211), I235 (= I212), N328 (≠ R305), R334 (≠ V311), F383 (= F360)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 100% coverage: 1:453/454 of query aligns to 24:478/479 of P25553
- L150 (≠ S127) binding
- R161 (≠ N138) binding
- KPSE 176:179 (= KPSE 153:156) binding
- F180 (≠ Y157) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A191) binding
- S230 (= S205) binding
- E251 (= E226) binding
- N286 (≠ C262) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ V311) binding
- E443 (≠ V418) binding
- H449 (≠ W424) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
33% identity, 95% coverage: 1:431/454 of query aligns to 37:472/501 of Q56YU0
- G152 (≠ E113) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A375) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
31% identity, 99% coverage: 1:448/454 of query aligns to 28:476/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
30% identity, 99% coverage: 1:448/454 of query aligns to 27:475/481 of 3jz4A
- active site: N156 (= N130), K179 (= K153), E254 (= E226), C288 (= C261), E385 (= E358), E462 (≠ T435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A128), W155 (= W129), K179 (= K153), A181 (≠ S155), S182 (≠ E156), A212 (= A185), G216 (= G189), G232 (= G204), S233 (= S205), I236 (≠ T208), C288 (= C261), K338 (≠ V311), E385 (= E358), F387 (= F360)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
33% identity, 97% coverage: 5:446/454 of query aligns to 32:477/494 of 4pz2B
- active site: N159 (= N130), K182 (= K153), E258 (= E226), C292 (= C261), E392 (= E358), D469 (≠ H438)
- binding nicotinamide-adenine-dinucleotide: I155 (= I126), I156 (≠ S127), P157 (≠ A128), W158 (= W129), N159 (= N130), M164 (≠ V135), K182 (= K153), A184 (≠ S155), E185 (= E156), G215 (≠ K186), G219 (≠ S190), F233 (= F202), T234 (= T203), G235 (= G204), S236 (= S205), V239 (≠ T208), E258 (= E226), L259 (= L227), C292 (= C261), E392 (= E358), F394 (= F360)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 99% coverage: 3:452/454 of query aligns to 21:475/477 of 6j76A
- active site: N148 (= N130), E246 (= E226), C280 (= C261), E458 (≠ T435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I126), T145 (≠ S127), A146 (= A128), W147 (= W129), N148 (= N130), K171 (= K153), T173 (≠ S155), S174 (≠ E156), G204 (≠ K186), G208 (= G189), T223 (= T203), G224 (= G204), S225 (= S205), A228 (≠ T208), S231 (≠ L211), I232 (= I212), E246 (= E226), L247 (= L227), C280 (= C261), E381 (= E358), F383 (= F360), H447 (≠ W424)
P00352 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 Homo sapiens (Human) (see 7 papers)
33% identity, 98% coverage: 3:448/454 of query aligns to 40:490/501 of P00352
- N121 (= N80) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ SAWN 127:130) binding
- I177 (≠ V137) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPSE 153:156) binding
- GP 226:227 (≠ KE 186:187) binding
- GS 246:247 (= GS 204:205) binding
- E269 (= E226) active site, Proton acceptor
- ELG 269:271 (= ELG 226:228) binding
- C302 (≠ S260) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C261) active site, Nucleophile
- EQYDK 349:353 (≠ EQISV 307:311) binding
- EIF 400:402 (≠ ESF 358:360) binding
- G458 (≠ D416) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
7um9A Human aldh1a1 with bound compound cm38 (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 33:483/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I126), I160 (≠ S127), P161 (≠ A128), W162 (= W129), N163 (= N130), K186 (= K153), E189 (= E156), G219 (≠ K186), G223 (≠ S190), F237 (= F202), T238 (= T203), G239 (= G204), S240 (= S205), V243 (≠ T208), E262 (= E226), G264 (= G228), Q343 (= Q308), K346 (≠ V311), E393 (= E358), F395 (= F360)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ N138), H286 (≠ D251), Y290 (= Y255), I297 (≠ C262), G451 (≠ D416)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 33:483/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 33:483/494 of 5l2nA
- active site: N163 (= N130), K186 (= K153), E262 (= E226), C296 (= C261), E393 (= E358), E470 (≠ T435)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (≠ Y131), M168 (≠ V135), W171 (≠ N138), H286 (≠ D251), G287 (= G252), Y290 (= Y255), C295 (≠ S260), C296 (= C261), I297 (≠ C262), Y450 (≠ C415), G451 (≠ D416), V453 (= V418), F459 (≠ W424)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 33:483/494 of 5l2mA
- active site: N163 (= N130), K186 (= K153), E262 (= E226), C296 (= C261), E393 (= E358), E470 (≠ T435)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ Y131), F283 (≠ G248), H286 (≠ D251), Y290 (= Y255)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 33:483/494 of 4wpnA
- active site: N163 (= N130), K186 (= K153), E262 (= E226), C296 (= C261), E393 (= E358), E470 (≠ T435)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (≠ Y131), H286 (≠ D251), G287 (= G252), Y290 (= Y255), C295 (≠ S260), I297 (≠ C262), G451 (≠ D416), V453 (= V418)
4wb9A Human aldh1a1 complexed with nadh (see paper)
33% identity, 98% coverage: 3:448/454 of query aligns to 32:482/493 of 4wb9A
- active site: N162 (= N130), K185 (= K153), E261 (= E226), C295 (= C261), E392 (= E358), E469 (≠ T435)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I126), I159 (≠ S127), P160 (≠ A128), W161 (= W129), N162 (= N130), K185 (= K153), E188 (= E156), G218 (≠ K186), G222 (≠ S190), F236 (= F202), T237 (= T203), G238 (= G204), S239 (= S205), V242 (≠ T208), G263 (= G228), C295 (= C261), Q342 (= Q308), K345 (≠ V311), E392 (= E358), F394 (= F360)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
32% identity, 98% coverage: 5:448/454 of query aligns to 35:483/489 of 7a6qB
- active site: N163 (= N130), E262 (= E226), C296 (= C261), E470 (≠ T435)
- binding nicotinamide-adenine-dinucleotide: I159 (= I126), W162 (= W129), K186 (= K153), E189 (= E156), G219 (≠ K186), G223 (≠ S190), S240 (= S205), V243 (≠ T208), K342 (≠ E307)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: P36 (= P6), D103 (≠ E70), E189 (= E156), Q190 (≠ Y157), F218 (≠ A185), I339 (≠ T304), D340 (≠ R305)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G84), D141 (= D107), N143 (≠ G110), N451 (≠ D416), L453 (≠ V418), A455 (= A420)
Sites not aligning to the query:
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
32% identity, 98% coverage: 5:448/454 of query aligns to 35:483/489 of 7a6qA
- active site: N163 (= N130), E262 (= E226), C296 (= C261), E470 (≠ T435)
- binding nicotinamide-adenine-dinucleotide: I159 (= I126), T160 (≠ S127), W162 (= W129), K186 (= K153), A188 (≠ S155), E189 (= E156), G219 (≠ K186), G223 (≠ S190), S240 (= S205), V243 (≠ T208), K342 (≠ E307), K346 (≠ V311)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G84), D141 (= D107), N143 (≠ G110), N451 (≠ D416), L453 (≠ V418), Y454 (≠ S419)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
32% identity, 98% coverage: 5:448/454 of query aligns to 35:483/489 of 5fhzA
- active site: N163 (= N130), K186 (= K153), E262 (= E226), C296 (= C261), E393 (= E358), E470 (≠ T435)
- binding nicotinamide-adenine-dinucleotide: I159 (= I126), T160 (≠ S127), W162 (= W129), K186 (= K153), E189 (= E156), G219 (≠ K186), G223 (≠ S190), F237 (= F202), G239 (= G204), S240 (= S205), T241 (≠ Y206), V243 (≠ T208), G264 (= G228), Q343 (= Q308), E393 (= E358)
- binding retinoic acid: G118 (= G84), R121 (≠ A87), F164 (≠ Y131), M168 (≠ V135), W171 (≠ N138), C295 (≠ S260), C296 (= C261), L453 (≠ V418)
Query Sequence
>CA265_RS24850 FitnessBrowser__Pedo557:CA265_RS24850
MQIINPATAEIITSLEEDNLSTLQLKFDALQKAQPQWAGKTLQERIAVITHFSDLLEVEI
EKLASVLTSEVGKPLQQSRNEINGARARIKWMLANAEKYLADEVMTDEPGIKEIIKYEPL
GVVCNISAWNYPYLVGVNVFIPALLSGNTVMYKPSEYATLTGIEIEKLLKKAGVPDDVFH
IAIGAKETGSALLNMDFNGYFFTGSYKTGKLIYEKVAAKMVPCQLELGGKDPLYITDDVT
DVAAAAIGTADGAFYNNGQSCCAVERIYVQEKNYDDYCNAFVTEVKSWKTGIPTAEGVYI
GALTRKEQISVLENQVKDALNKGAKLLTGGKAVEGKGYYFEPTVLTDVTNDMLVMQEESF
GPIIGIMKVKDDAEALKMMKDTDYGLTASVYTASQERAEKILAQLDAGSGYWNCCDRVSA
ALPWSGRKYSGIGATLSHQGIRAFTKPKGYHLRR
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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