SitesBLAST
Comparing SMc04397 FitnessBrowser__Smeli:SMc04397 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)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
49% identity, 96% coverage: 18:500/504 of query aligns to 9:490/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W167), K180 (= K191), A182 (≠ S193), T212 (= T223), G213 (= G224), G217 (= G228), F231 (= F242), G233 (= G244), S234 (= S245), V237 (≠ I248), Q337 (≠ H347), E388 (= E398), F390 (= F400)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
49% identity, 96% coverage: 18:500/504 of query aligns to 8:489/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I164), T153 (= T165), P154 (= P166), W155 (= W167), N156 (= N168), I161 (= I173), K179 (= K191), A181 (≠ S193), E182 (= E194), T211 (= T223), G212 (= G224), G216 (= G228), Q217 (≠ A229), F230 (= F242), T231 (= T243), G232 (= G244), S233 (= S245), V236 (≠ I248), E255 (= E266), L256 (= L267), G257 (= G268), A289 (≠ C300), E387 (= E398), F389 (= F400)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
49% identity, 96% coverage: 20:501/504 of query aligns to 22:504/505 of 3u4jA
Sites not aligning to the query:
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)
41% identity, 96% coverage: 21:502/504 of query aligns to 21:501/501 of Q56YU0
- G152 (= G151) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A415) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
42% identity, 94% coverage: 16:490/504 of query aligns to 2:476/486 of 4pxlA
- active site: N154 (= N168), K177 (= K191), E253 (= E266), C287 (= C300), E384 (= E398), D461 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I150 (= I164), V151 (≠ T165), P152 (= P166), W153 (= W167), K177 (= K191), E180 (= E194), G210 (= G224), G214 (= G228), A215 (= A229), F228 (= F242), G230 (= G244), S231 (= S245), V234 (≠ I248), E253 (= E266), G255 (= G268), C287 (= C300), Q334 (≠ H347), K337 (= K350), E384 (= E398), F386 (= F400)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 97% coverage: 4:494/504 of query aligns to 2:490/491 of 5gtlA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E398), E471 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I164), P163 (= P166), K188 (= K191), A190 (≠ S193), E191 (= E194), Q192 (≠ L195), G221 (= G224), G225 (= G228), G241 (= G244), S242 (= S245), T245 (≠ I248), L264 (= L267), C297 (= C300), E394 (= E398), F396 (= F400)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 97% coverage: 4:494/504 of query aligns to 2:490/491 of 5gtkA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E398), E471 (= E475)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (≠ T165), P163 (= P166), W164 (= W167), K188 (= K191), E191 (= E194), G221 (= G224), G225 (= G228), A226 (= A229), F239 (= F242), G241 (= G244), S242 (= S245), T245 (≠ I248), Y248 (≠ L251), L264 (= L267), C297 (= C300), Q344 (≠ H347), R347 (≠ K350), E394 (= E398), F396 (= F400)
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)
39% identity, 95% coverage: 21:499/504 of query aligns to 19:496/505 of 4neaA
- active site: N166 (= N168), K189 (= K191), E264 (= E266), C298 (= C300), E399 (= E398), E476 (= E475)
- binding nicotinamide-adenine-dinucleotide: P164 (= P166), K189 (= K191), E192 (= E194), G222 (= G224), G226 (= G228), G242 (= G244), G243 (≠ S245), T246 (≠ I248), H249 (≠ L251), I250 (≠ T252), C298 (= C300), E399 (= E398), F401 (= F400)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
42% identity, 96% coverage: 15:500/504 of query aligns to 3:493/494 of 4pz2B
- active site: N159 (= N168), K182 (= K191), E258 (= E266), C292 (= C300), E392 (= E398), D469 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I155 (= I164), I156 (≠ T165), P157 (= P166), W158 (= W167), N159 (= N168), M164 (≠ I173), K182 (= K191), A184 (≠ S193), E185 (= E194), G215 (= G224), G219 (= G228), F233 (= F242), T234 (= T243), G235 (= G244), S236 (= S245), V239 (≠ I248), E258 (= E266), L259 (= L267), C292 (= C300), E392 (= E398), F394 (= F400)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 96% coverage: 22:503/504 of query aligns to 12:501/505 of O24174
- N164 (= N168) 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 (≠ Q176) 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.
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)
38% identity, 95% coverage: 21:501/504 of query aligns to 9:493/497 of P17202
- I28 (≠ V40) binding
- D96 (≠ E108) binding
- SPW 156:158 (≠ TPW 165:167) binding
- Y160 (≠ F169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ Q176) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 191:194) binding
- L186 (= L195) binding
- SSAT 236:239 (≠ STGI 245:248) binding
- V251 (≠ L260) binding in other chain
- L258 (= L267) binding
- W285 (≠ F294) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E398) binding
- A441 (≠ T449) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G458) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F464) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R468) binding
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 95% coverage: 19:495/504 of query aligns to 5:483/489 of 4cazA
- active site: N152 (= N168), K175 (= K191), E251 (= E266), C285 (= C300), E386 (= E398), E463 (= E475)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I164), G149 (≠ T165), W151 (= W167), N152 (= N168), K175 (= K191), E178 (= E194), G208 (= G224), G212 (= G228), F226 (= F242), T227 (= T243), G228 (= G244), G229 (≠ S245), T232 (≠ I248), V236 (≠ T252), E251 (= E266), L252 (= L267), C285 (= C300), E386 (= E398), F388 (= F400)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 95% coverage: 19:495/504 of query aligns to 5:483/489 of 2woxA
- active site: N152 (= N168), K175 (= K191), E251 (= E266), C285 (= C300), E386 (= E398), E463 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I164), G149 (≠ T165), W151 (= W167), N152 (= N168), K175 (= K191), S177 (= S193), E178 (= E194), G208 (= G224), G212 (= G228), F226 (= F242), T227 (= T243), G228 (= G244), G229 (≠ S245), T232 (≠ I248), V236 (≠ T252), E251 (= E266), L252 (= L267), C285 (= C300), E386 (= E398), F388 (= F400)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 95% coverage: 19:495/504 of query aligns to 5:483/489 of 2wmeA
- active site: N152 (= N168), K175 (= K191), E251 (= E266), C285 (= C300), E386 (= E398), E463 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T165), W151 (= W167), K175 (= K191), S177 (= S193), E178 (= E194), G208 (= G224), G212 (= G228), F226 (= F242), G228 (= G244), G229 (≠ S245), T232 (≠ I248), V236 (≠ T252)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
39% identity, 95% coverage: 19:495/504 of query aligns to 6:484/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 165:168) binding
- K162 (= K177) active site, Charge relay system
- KPSE 176:179 (= KPSE 191:194) binding
- G209 (= G224) binding
- GTST 230:233 (≠ STGI 245:248) binding
- E252 (= E266) active site, Proton acceptor
- C286 (= C300) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E398) binding
- E464 (= E475) active site, Charge relay system
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 95% coverage: 21:501/504 of query aligns to 7:491/495 of 4v37A
- active site: N157 (= N168), K180 (= K191), E255 (= E266), A289 (≠ C300), E388 (= E398), E465 (= E475)
- binding 3-aminopropan-1-ol: C448 (≠ G458), W454 (≠ F464)
- binding nicotinamide-adenine-dinucleotide: I153 (= I164), S154 (≠ T165), P155 (= P166), W156 (= W167), N157 (= N168), M162 (≠ I173), K180 (= K191), S182 (= S193), E183 (= E194), G213 (= G224), G217 (= G228), A218 (= A229), T232 (= T243), G233 (= G244), S234 (= S245), T237 (≠ I248), E255 (= E266), L256 (= L267), A289 (≠ C300), E388 (= E398), F390 (= F400)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
38% identity, 97% coverage: 9:498/504 of query aligns to 21:511/512 of P47895
- R89 (≠ P76) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K191) binding
- E207 (= E194) binding
- GSTEVG 257:262 (≠ GSTGIG 244:249) binding
- Q361 (≠ H347) binding
- E411 (= E398) binding
- A493 (= A480) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
38% identity, 97% coverage: 9:495/504 of query aligns to 2:489/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I164), T159 (= T165), P160 (= P166), W161 (= W167), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), F236 (= F242), S239 (= S245), V242 (≠ I248)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
41% identity, 94% coverage: 21:494/504 of query aligns to 5:479/489 of 4o6rA
- active site: N150 (= N168), K173 (= K191), E248 (= E266), C282 (= C300), E383 (= E398), E460 (= E475)
- binding adenosine monophosphate: I146 (= I164), V147 (≠ T165), K173 (= K191), G206 (= G224), G210 (= G228), Q211 (≠ A229), F224 (= F242), G226 (= G244), S227 (= S245), T230 (≠ I248), R233 (≠ L251)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
38% identity, 96% coverage: 9:494/504 of query aligns to 3:489/489 of 7a6qB
- active site: N163 (= N168), E262 (= E266), C296 (= C300), E470 (= E475)
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), W162 (= W167), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), S240 (= S245), V243 (≠ I248), K342 (≠ Q346)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ E38), T33 (≠ R39), C34 (≠ V40), P36 (= P42), D103 (≠ E108), E189 (= E194), Q190 (≠ L195), F218 (≠ T223), I339 (= I343), D340 (≠ T344)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (= G122), D141 (≠ G146), N143 (≠ G148), N451 (≠ M456), L453 (≠ G458), A455 (≠ S460)
Query Sequence
>SMc04397 FitnessBrowser__Smeli:SMc04397
MVMTVVVRPKALGDYDTREFRMLIDGQWVDGAEGRTIERVAPGHGVVVSRYQAAAKADAE
RAIAAARRAFDEGPWPRMTASERSLILLRAADMIAARADELAFLDAVESGKPISQAKGEL
AGAADIWRYAAALARELSGESYNTLGEGTLGVVLREPIGVVSIITPWNFPFLIVSQKLPF
ALAAGCTTVVKPSELTSASTLVLGEILEAAGVPQGVVNIIVGTGPEAGAPLTTHPHVDMV
SFTGSTGIGQLTMANAAQTLKKVSLELGGKNPQIVFPDANLDEFIDAAVFGAYFNAGECC
NAGSRLILHRDIAEEVTARIASLSAKVKVGDPLDPETQVGAIITPQHLQKIAGYVSSASN
EGARIAHGGTTLDLGMGQFMAPTILSAVRPEMAVAREEVFGPVLSVLTFEKTEEAIRIAN
SIDYGLSAGVWSRDFDTCLTIGRRVRAGTVWMNTFMDGASELPFGGYRQSGLGRELGRHA
VEDYTETKTLNMHIGRRSNWWMPR
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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