SitesBLAST
Comparing BPHYT_RS20795 FitnessBrowser__BFirm:BPHYT_RS20795 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)
56% identity, 98% coverage: 10:502/502 of query aligns to 1:492/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W167), K180 (= K191), A182 (= A193), T212 (≠ L223), G213 (= G224), G217 (= G228), F231 (= F242), G233 (= G244), S234 (= S245), V237 (= V248), Q337 (= Q347), E388 (= E398), F390 (= F400)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
56% identity, 98% coverage: 11:502/502 of query aligns to 1:491/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (≠ V164), T153 (= T165), P154 (= P166), W155 (= W167), N156 (= N168), I161 (= I173), K179 (= K191), A181 (= A193), E182 (= E194), T211 (≠ L223), G212 (= G224), G216 (= G228), Q217 (= Q229), F230 (= F242), T231 (= T243), G232 (= G244), S233 (= S245), V236 (= V248), E255 (= E266), L256 (= L267), G257 (= G268), A289 (≠ C300), E387 (= E398), F389 (= F400)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
50% identity, 96% coverage: 19:501/502 of query aligns to 21:504/505 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)
42% identity, 98% coverage: 8:501/502 of query aligns to 9:501/501 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, 96% coverage: 20:501/502 of query aligns to 6:486/486 of 4pxlA
- active site: N154 (= N168), K177 (= K191), E253 (= E266), C287 (= C300), E384 (= E398), D461 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V164), V151 (≠ T165), P152 (= P166), W153 (= W167), K177 (= K191), E180 (= E194), G210 (= G224), G214 (= G228), A215 (≠ Q229), F228 (= F242), G230 (= G244), S231 (= S245), V234 (= V248), E253 (= E266), G255 (= G268), C287 (= C300), Q334 (= Q347), K337 (= K350), E384 (= E398), F386 (= F400)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
42% identity, 96% coverage: 20:501/502 of query aligns to 11:494/494 of 4pz2B
- active site: N159 (= N168), K182 (= K191), E258 (= E266), C292 (= C300), E392 (= E398), D469 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V164), I156 (≠ T165), P157 (= P166), W158 (= W167), N159 (= N168), M164 (≠ I173), K182 (= K191), A184 (= A193), E185 (= E194), G215 (= G224), G219 (= G228), F233 (= F242), T234 (= T243), G235 (= G244), S236 (= S245), V239 (= V248), E258 (= E266), L259 (= L267), C292 (= C300), E392 (= E398), F394 (= F400)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
42% identity, 94% coverage: 22:495/502 of query aligns to 25:498/503 of O14293
- S248 (= S245) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 97% coverage: 14:498/502 of query aligns to 4:495/505 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 (≠ E176) 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.
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
44% identity, 94% coverage: 23:494/502 of query aligns to 21:495/495 of 5iuwA
- active site: N166 (= N168), K189 (= K191), E265 (= E266), C300 (= C300), E399 (= E398), D476 (≠ E475)
- binding 1h-indol-3-ylacetic acid: F167 (= F169), M170 (≠ F172), C300 (= C300), D457 (≠ I456), F465 (≠ I464)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V164), V163 (≠ T165), P164 (= P166), W165 (= W167), N166 (= N168), K189 (= K191), G222 (= G224), G226 (= G228), K227 (≠ Q229), F240 (= F242), T241 (= T243), G242 (= G244), S243 (= S245), I246 (≠ V248), Y253 (≠ A255), E265 (= E266), A266 (≠ L267), C300 (= C300), E399 (= E398), F401 (= F400)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
44% identity, 94% coverage: 23:494/502 of query aligns to 21:495/495 of 5iuvA
- active site: N166 (= N168), K189 (= K191), E265 (= E266), C300 (= C300), E399 (= E398), D476 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V164), V163 (≠ T165), P164 (= P166), W165 (= W167), N166 (= N168), K189 (= K191), S191 (≠ A193), G222 (= G224), G226 (= G228), K227 (≠ Q229), F240 (= F242), T241 (= T243), G242 (= G244), S243 (= S245), I246 (≠ V248), Y253 (≠ A255), E265 (= E266), A266 (≠ L267), C300 (= C300), E399 (= E398), F401 (= F400)
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: 22:498/502 of query aligns to 10:490/497 of P17202
- I28 (≠ K40) 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 (≠ E176) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 191:194) binding
- L186 (= L195) binding
- SSAT 236:239 (≠ STPV 245:248) binding
- V251 (≠ M260) binding in other chain
- L258 (= L267) binding
- W285 (≠ F294) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E398) binding
- A441 (≠ R449) 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 (≠ I464) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K468) binding
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
44% identity, 94% coverage: 23:494/502 of query aligns to 21:495/495 of 7jsoA
- active site: N166 (= N168), E265 (= E266), A300 (≠ C300), D476 (≠ E475)
- binding 1h-indol-3-ylacetic acid: F167 (= F169), W174 (≠ E176), V299 (≠ C299), A300 (≠ C300), T301 (≠ V301), D457 (≠ I456), F465 (≠ I464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (≠ V164), V163 (≠ T165), P164 (= P166), W165 (= W167), K189 (= K191), E192 (= E194), G222 (= G224), G226 (= G228), K227 (≠ Q229), F240 (= F242), G242 (= G244), S243 (= S245), I246 (≠ V248), A266 (≠ L267), G267 (= G268), A300 (≠ C300), E399 (= E398), F401 (= F400)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 5l13A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F169), M168 (≠ I173), W171 (≠ E176), F290 (= F294), C295 (= C299), C296 (= C300), C297 (≠ V301), D451 (≠ I456), F453 (≠ G458)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 4kwgA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F169), M168 (≠ I173), C295 (= C299), C296 (= C300), C297 (≠ V301), D451 (≠ I456), F453 (≠ G458)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 4kwfA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F169), M168 (≠ I173), W171 (≠ E176), E262 (= E266), C295 (= C299), C296 (= C300), C297 (≠ V301), D451 (≠ I456), F453 (≠ G458), F459 (≠ I464)
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)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 3sz9A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F169), C295 (= C299), C296 (= C300), D451 (≠ I456), F453 (≠ G458), F459 (≠ I464)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 3injA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ A122), F164 (= F169), L167 (≠ F172), F286 (= F290), F290 (= F294), D451 (≠ I456), F453 (≠ G458)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 2vleA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding daidzin: M118 (≠ A122), F164 (= F169), M168 (≠ I173), W171 (≠ E176), F286 (= F290), F290 (= F294), C295 (= C299), C296 (= C300), D451 (≠ I456), V452 (≠ T457), F453 (≠ G458)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 1o01B
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding (2e)-but-2-enal: C296 (= C300), C297 (≠ V301), F453 (≠ G458)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V164), I160 (≠ T165), P161 (= P166), W162 (= W167), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), A224 (≠ Q229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), E393 (= E398), F395 (= F400)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
42% identity, 92% coverage: 37:497/502 of query aligns to 26:492/494 of 1cw3A
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding magnesium ion: V34 (vs. gap), D103 (≠ E108), Q190 (≠ L195)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V164), I160 (≠ T165), P161 (= P166), W162 (= W167), K186 (= K191), G219 (= G224), G223 (= G228), A224 (≠ Q229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), K346 (= K350), E393 (= E398), F395 (= F400)
Query Sequence
>BPHYT_RS20795 FitnessBrowser__BFirm:BPHYT_RS20795
MSNLNELAATLRLPAEPLRTPMFIDGKDYAGNTGEFVTRKSPGHGVPVTATPRACVDDLN
AAVASARRAFDDGRWSRLSGEQRATVLLKTARLIRDKVETLAYLETLESGKPIGQSRGEI
NAAAGIWEYAAGLARVVHGDSHDTLGADLFGLTVRQPIGVVGIVTPWNFPFFILSERLPF
VLAAGCTAVVKPAELTSTTTLKLAALLTEAGLPDGVVNVVTGLGAVVGQALAEHMDVDMM
SFTGSTPVGRSVLAAAGGNMKKVGLELGGKNPQIVFADADLDDAADAIAFGICFNAGQCC
VSGSRLVVHRSVEEELVARVKAVFEKVRVGDPLDASNHVGAIVEARQFDKIRGFIDAGRR
DGAQLVHGGESTSHGERFFIQPTLFRNVQPQSALAQEEIFGPVLSVTSFDTFEEAIQLAN
GVPYGLAASIWTRDLQGAISSFREVQAGRIWVNCTITGGPEMPIGGVKQSGIGRETGRYG
VEEYTELKSVHVQLGKRPRWIA
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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