SitesBLAST
Comparing BPHYT_RS05370 FitnessBrowser__BFirm:BPHYT_RS05370 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)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
86% identity, 99% coverage: 4:479/479 of query aligns to 1:476/476 of 4yweA
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 99% coverage: 2:477/479 of query aligns to 15:489/491 of 5gtlA
- active site: N165 (= N150), K188 (= K173), E263 (= E248), C297 (= C282), E394 (= E381), E471 (= E459)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I146), P163 (= P148), K188 (= K173), A190 (= A175), E191 (= E176), Q192 (≠ D177), G221 (= G206), G225 (= G210), G241 (= G226), S242 (= S227), T245 (= T230), L264 (= L249), C297 (= C282), E394 (= E381), F396 (= F383)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
42% identity, 99% coverage: 2:477/479 of query aligns to 15:489/491 of 5gtkA
- active site: N165 (= N150), K188 (= K173), E263 (= E248), C297 (= C282), E394 (= E381), E471 (= E459)
- binding nicotinamide-adenine-dinucleotide: I161 (= I146), I162 (≠ V147), P163 (= P148), W164 (= W149), K188 (= K173), E191 (= E176), G221 (= G206), G225 (= G210), A226 (= A211), F239 (= F224), G241 (= G226), S242 (= S227), T245 (= T230), Y248 (≠ L233), L264 (= L249), C297 (= C282), Q344 (= Q328), R347 (= R331), E394 (= E381), F396 (= F383)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
43% identity, 99% coverage: 3:477/479 of query aligns to 3:478/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E248), C282 (= C282), E383 (= E381), E460 (= E459)
- binding adenosine monophosphate: I146 (= I146), V147 (= V147), K173 (= K173), G206 (= G206), G210 (= G210), Q211 (≠ A211), F224 (= F224), G226 (= G226), S227 (= S227), T230 (= T230), R233 (≠ L233)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
42% identity, 98% coverage: 5:474/479 of query aligns to 7:476/486 of 4pxlA
- active site: N154 (= N150), K177 (= K173), E253 (= E248), C287 (= C282), E384 (= E381), D461 (≠ E459)
- binding nicotinamide-adenine-dinucleotide: I150 (= I146), V151 (= V147), P152 (= P148), W153 (= W149), K177 (= K173), E180 (= E176), G210 (= G206), G214 (= G210), A215 (= A211), F228 (= F224), G230 (= G226), S231 (= S227), V234 (≠ T230), E253 (= E248), G255 (= G250), C287 (= C282), Q334 (= Q328), K337 (≠ R331), E384 (= E381), F386 (= F383)
7radA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 7:477/479 of query aligns to 16:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ V147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (= E176), G218 (= G206), G222 (= G210), A223 (= A211), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ A105), F163 (≠ Y151), E285 (≠ S272), F289 (≠ Q276), N450 (≠ G439), V452 (≠ G442)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 7:477/479 of query aligns to 16:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ V147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (= E176), G218 (= G206), G222 (= G210), F236 (= F224), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A105), E285 (≠ S272), F289 (≠ Q276), N450 (≠ G439), V452 (≠ G442)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 7:477/479 of query aligns to 16:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ V147), P160 (= P148), W161 (= W149), N162 (= N150), K185 (= K173), E188 (= E176), G218 (= G206), G222 (= G210), T237 (= T225), G238 (= G226), S239 (= S227), V242 (≠ T230), E261 (= E248), L262 (= L249), C295 (= C282), E392 (= E381), F394 (= F383)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
39% identity, 100% coverage: 1:477/479 of query aligns to 35:512/518 of O94788
- E50 (≠ S16) to G: in dbSNP:rs34266719
- A110 (≠ S74) to V: in dbSNP:rs35365164
- Q182 (≠ H145) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 147:149) binding
- KPAE 210:213 (= KPAE 173:176) binding
- STE 264:266 (≠ SPD 227:229) binding
- C320 (= C282) active site, Nucleophile
- R347 (≠ L309) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R310) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ KQQRR 327:331) binding
- A383 (≠ I344) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E381) binding
- E436 (≠ T400) to K: in dbSNP:rs34744827
- S461 (≠ A425) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
39% identity, 100% coverage: 1:477/479 of query aligns to 9:486/492 of 6b5hA
- active site: N161 (= N150), E260 (= E248), C294 (= C282), E468 (= E459)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ A101), G116 (≠ A105), F162 (≠ Y151), W169 (≠ R158), Q284 (≠ S272), F288 (≠ Q276), T295 (≠ S283), N449 (≠ G439), L451 (≠ G441), N452 (≠ G442), F457 (= F448)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), I158 (≠ V147), W160 (= W149), N161 (= N150), K184 (= K173), G217 (= G206), G221 (= G210), F235 (= F224), T236 (= T225), G237 (= G226), S238 (= S227), V241 (≠ T230), E260 (= E248), L261 (= L249), C294 (= C282), F393 (= F383)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
39% identity, 100% coverage: 1:477/479 of query aligns to 9:486/492 of 6b5gA
- active site: N161 (= N150), E260 (= E248), C294 (= C282), E468 (= E459)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y151), L165 (≠ Q154), W169 (≠ R158), F288 (≠ Q276), C293 (≠ T281), C294 (= C282), T295 (≠ S283), N449 (≠ G439), L451 (≠ G441)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), I158 (≠ V147), P159 (= P148), W160 (= W149), N161 (= N150), M166 (≠ I155), K184 (= K173), E187 (= E176), G217 (= G206), G221 (= G210), F235 (= F224), T236 (= T225), G237 (= G226), S238 (= S227), V241 (≠ T230), E260 (= E248), L261 (= L249), C294 (= C282), E391 (= E381), F393 (= F383)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
39% identity, 100% coverage: 1:477/479 of query aligns to 9:486/492 of 6aljA
- active site: N161 (= N150), E260 (= E248), C294 (= C282), E468 (= E459)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A105), F162 (≠ Y151), L165 (≠ Q154), M166 (≠ I155), W169 (≠ R158), E260 (= E248), C293 (≠ T281), C294 (= C282), L451 (≠ G441), N452 (≠ G442), A453 (≠ G443)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), I158 (≠ V147), P159 (= P148), W160 (= W149), N161 (= N150), K184 (= K173), E187 (= E176), G217 (= G206), G221 (= G210), F235 (= F224), G237 (= G226), S238 (= S227), V241 (≠ T230), Q341 (= Q328), K344 (≠ R331), E391 (= E381), F393 (= F383)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
43% identity, 98% coverage: 5:474/479 of query aligns to 12:484/494 of 4pz2B
- active site: N159 (= N150), K182 (= K173), E258 (= E248), C292 (= C282), E392 (= E381), D469 (≠ E459)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), I156 (≠ V147), P157 (= P148), W158 (= W149), N159 (= N150), M164 (≠ I155), K182 (= K173), A184 (= A175), E185 (= E176), G215 (= G206), G219 (= G210), F233 (= F224), T234 (= T225), G235 (= G226), S236 (= S227), V239 (≠ T230), E258 (= E248), L259 (= L249), C292 (= C282), E392 (= E381), F394 (= F383)
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)
39% identity, 99% coverage: 5:476/479 of query aligns to 21:493/501 of Q56YU0
- G152 (= G130) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A398) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
38% identity, 100% coverage: 1:477/479 of query aligns to 35:512/518 of Q63639
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
37% identity, 100% coverage: 1:477/479 of query aligns to 11:488/494 of 7jwwA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E381), E470 (= E459)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ A105), T122 (≠ Y109), F164 (≠ Y151), M168 (≠ I155), Y290 (≠ Q276), C295 (≠ T281), C296 (= C282), I297 (≠ S283), V453 (≠ G441), F459 (= F448)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
37% identity, 100% coverage: 1:477/479 of query aligns to 11:488/494 of 7jwvA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E381), E470 (= E459)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ A105), T122 (≠ Y109), F164 (≠ Y151), M168 (≠ I155), Y290 (≠ Q276), C295 (≠ T281), I297 (≠ S283), V453 (≠ G441), F459 (= F448)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
37% identity, 100% coverage: 1:477/479 of query aligns to 11:488/494 of 7jwuA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E381), E470 (= E459)
- binding nicotinamide-adenine-dinucleotide: I159 (= I146), I160 (≠ V147), P161 (= P148), W162 (= W149), N163 (= N150), K186 (= K173), E189 (= E176), G219 (= G206), G223 (= G210), A224 (= A211), F237 (= F224), T238 (= T225), G239 (= G226), S240 (= S227), V243 (≠ T230), L263 (= L249), C296 (= C282), Q343 (= Q328), K346 (≠ R331), E393 (= E381), F395 (= F383)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-(pyridin-2-yl)ethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: T122 (≠ Y109), F164 (≠ Y151), W171 (≠ R158), Y290 (≠ Q276), C295 (≠ T281), I297 (≠ S283), V453 (≠ G441), F459 (= F448)
7jwtA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
37% identity, 100% coverage: 1:477/479 of query aligns to 11:488/494 of 7jwtA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E381), E470 (= E459)
- binding 6-{[(1R)-1-(3-hydroxyphenyl)ethyl]sulfanyl}-1-methyl-5-phenyl-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ A105), T122 (≠ Y109), F164 (≠ Y151), M168 (≠ I155), W171 (≠ R158), Y290 (≠ Q276), C295 (≠ T281), V453 (≠ G441), F459 (= F448)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
38% identity, 99% coverage: 4:479/479 of query aligns to 13:489/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I146), T159 (≠ V147), P160 (= P148), W161 (= W149), K185 (= K173), E188 (= E176), G218 (= G206), G222 (= G210), F236 (= F224), S239 (= S227), V242 (≠ T230)
Query Sequence
>BPHYT_RS05370 FitnessBrowser__BFirm:BPHYT_RS05370
MEEARHFIGGEWSAASGGETIAVLDPSDGQPFTQLARGTAADIDAAVHAARRAFEGPWGQ
ASAAERGRILYRLSMLVAARQEELAQLEARDTGKPLKQARADSAALARYFEFYAGAADKL
HGETLPYQTGYTVLTIREPHGVTGHIVPWNYPMQIFGRSVGAALATGNACVVKPAEDACL
SVLRVAELAAEAGLPAGALNIVTGFGHEAGAALARHPGIDHISFTGSPDTGKLVTQMAAE
NHVPVTLELGGKSPQIVFADADLDAALPVLVSAIVQNAGQTCSAGSRVLIDRAIYEPLLD
RLSSAFHALRVGPSQADLDCGPLISAKQQRRVWDFLSDAQHDGIAMAAHGEVIPEAPESG
FYQAPTLLRDVPASHRLARDEVFGPVLAAMSFSDEDEALTLANGTPFGLVAGIWTRDGAR
QMRLARRLRSGQVFINNYGAGGGVELPFGGVKHSGHGREKGFEALYGFTALKTIAIKHG
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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