SitesBLAST
Comparing 7026109 FitnessBrowser__ANA3:7026109 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)
P51648 Aldehyde dehydrogenase family 3 member A2; Aldehyde dehydrogenase 10; Fatty aldehyde dehydrogenase; Microsomal aldehyde dehydrogenase; EC 1.2.1.3; EC 1.2.1.94 from Homo sapiens (Human) (see 5 papers)
37% identity, 93% coverage: 17:459/474 of query aligns to 5:442/485 of P51648
- I45 (≠ L57) to F: in SLS; severe loss of activity
- V64 (= V77) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ G119) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N125) mutation to A: Loss of enzyme activity.
- P114 (= P127) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P134) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T197) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G198) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E220) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ V227) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R241) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A250) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C254) active site; mutation to S: Loss of enzyme activity.
- D245 (= D258) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ Q279) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y291) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ AT 333:334) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (≠ T334) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E350) mutation to Q: Loss of enzyme activity.
- S365 (= S384) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y429) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H430) to Y: in SLS; severe loss of activity
- S415 (≠ G434) to N: in SLS; severe loss of activity
- F419 (= F438) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K442) to H: in SLS; severe loss of activity; dbSNP:rs768290318
Sites not aligning to the query:
- 445:485 mutation Missing: Decreased enzyme activity with dodecanal. Strongly decreased enzyme activity with hexadecanal. No effect on enzyme activity with octanal.
- 447 K → E: in SLS; severe loss of activity; dbSNP:rs67939114
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
36% identity, 97% coverage: 14:471/474 of query aligns to 13:468/484 of Q70DU8
- C45 (≠ L46) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E151) mutation to D: Small effect on NAD(+) interaction, but 40% loss of efficiency. Ability to use NADP(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to N: Ability to use NADP(+) and 33% decreased efficiency with NAD(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to Q: Loss of specificity for NAD(+) and loss of 25% efficiency. 15% efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to T: Loss of specificity and increased NADP(+) binding. Decreased catalytic efficiency. Loss of cofactor specificity and same lower efficiency with both; when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with R-178 and V-200.
- V178 (≠ A180) mutation to R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200.
- I200 (≠ V202) mutation to G: Changed coenzyme preference from NAD(+) to NADP(+), but impaired affinities for both cofactors. No effect on the interaction with the substrate. Impaired affinities for both cofactors and decreased catalytic efficiencies; when associated with D-149, Q-149, N-149 or T-149.; mutation to V: Also able to use NADP(+) as coenzyme, but no effect on the interaction with the substrate. 15% efficiency with NAD(+); when associated with Q-149. 70% loss of efficiency with NAD(+); when associated with D-149 or N-149. Loss of cofactor specificity and same lower efficiency with both; when associated with T-149. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and R-178.
- C247 (≠ L248) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C254) mutation to S: No effect on solubility, but loss of activity.
P30838 Aldehyde dehydrogenase, dimeric NADP-preferring; ALDHIII; Aldehyde dehydrogenase 3; Aldehyde dehydrogenase family 3 member A1; EC 1.2.1.5 from Homo sapiens (Human) (see 4 papers)
36% identity, 95% coverage: 10:459/474 of query aligns to 1:445/453 of P30838
- S134 (≠ H144) to A: in dbSNP:rs887241
- E210 (= E220) active site
- C244 (= C254) active site; mutation to S: Abolishes activity.
- P329 (≠ L345) to A: in allele ALDH3A1*2; dbSNP:rs2228100
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
36% identity, 95% coverage: 11:459/474 of query aligns to 1:444/447 of 8bb8A
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
36% identity, 95% coverage: 11:459/474 of query aligns to 1:444/447 of 3szbA
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
36% identity, 95% coverage: 11:459/474 of query aligns to 1:444/446 of 4l2oA
- active site: N114 (= N125), K137 (= K148), E209 (= E220), C243 (= C254), E333 (= E350), Y412 (= Y429)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ S72), Y65 (≠ P76), Y115 (≠ F126), N118 (≠ M129), L119 (= L130), M237 (≠ L248), C243 (= C254), I391 (≠ V408), I394 (≠ V411), T395 (≠ A412), F401 (= F418), H413 (= H430)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P123), W113 (= W124), N114 (= N125), L119 (= L130), E140 (= E151), V169 (≠ A180), T186 (= T197), G187 (= G198), S188 (= S199), V191 (= V202), E209 (= E220), L210 (= L221), G211 (= G222), C243 (= C254), H289 (≠ Q299), E333 (= E350), F335 (= F352), F401 (= F418)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
36% identity, 95% coverage: 11:459/474 of query aligns to 1:444/446 of 4h80A
- active site: N114 (= N125), K137 (= K148), E209 (= E220), C243 (= C254), E333 (= E350), Y412 (= Y429)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ S72), Y65 (≠ P76), Y115 (≠ F126), N118 (≠ M129), W233 (≠ Y244), T242 (≠ I253), C243 (= C254), V244 (= V255), I394 (≠ V411), T395 (≠ A412), F401 (= F418)
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
36% identity, 95% coverage: 11:459/474 of query aligns to 1:444/452 of 4l1oB
- active site: N114 (= N125), K137 (= K148), E209 (= E220), C243 (= C254), E333 (= E350), Y412 (= Y429)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (≠ F126), N118 (≠ M129), L119 (= L130), E209 (= E220), T242 (≠ I253), C243 (= C254), I391 (≠ V408), I394 (≠ V411), F401 (= F418), H413 (= H430)
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Homo sapiens (Human) (see paper)
37% identity, 97% coverage: 10:469/474 of query aligns to 1:455/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
37% identity, 92% coverage: 7:444/474 of query aligns to 5:431/435 of 5ucdA
- active site: N119 (= N125), K142 (= K148), E214 (= E220), C248 (= C254), E336 (= E350), Y416 (= Y429)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I121), G116 (≠ V122), F118 (≠ W124), N119 (= N125), K142 (= K148), S144 (= S150), E145 (= E151), R174 (≠ A180), F190 (= F196), T191 (= T197), G192 (= G198), S193 (= S199), V196 (= V202), E214 (= E220), L215 (= L221), C248 (= C254), E336 (= E350), F338 (= F352)
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
34% identity, 94% coverage: 13:459/474 of query aligns to 2:443/446 of 1ad3A
- active site: N113 (= N125), K136 (= K148), E208 (= E220), C242 (= C254), E332 (= E350), Y411 (= Y429)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P123), W112 (= W124), N113 (= N125), E139 (= E151), V140 (≠ F152), V168 (≠ A180), G186 (= G198), V190 (= V202), H288 (≠ Q299), R291 (= R302), E332 (= E350), F334 (= F352)
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
37% identity, 96% coverage: 12:468/474 of query aligns to 16:467/479 of J3QMK6
- RR 462:463 (≠ FI 463:464) mutation to AA: Reduces membrane localization.
Q80VQ0 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Mus musculus (Mouse) (see paper)
36% identity, 96% coverage: 17:469/474 of query aligns to 8:455/468 of Q80VQ0
Sites not aligning to the query:
- 462 modified: S-palmitoyl cysteine; C→S: Reduces palmitoylation.
- 462:463 CC→SS: Abolishes palmitoylation.
- 463 modified: S-palmitoyl cysteine; C→S: Reduces palmitoylation.
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
36% identity, 98% coverage: 4:468/474 of query aligns to 7:467/479 of E9Q3E1
- W462 (≠ F463) mutation to A: Reduces lipid droplet localization.
Sites not aligning to the query:
- 469 W→A: Reduces lipid droplet localization.
- 476 C→S: Reduces lipid droplet localization.
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 97% coverage: 16:473/474 of query aligns to 78:532/550 of Q8W033
- C114 (≠ P52) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I81) mutation to S: No effect on solubility, but decreased activity.
- V263 (= V202) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S225) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ L248) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C254) mutation to S: No effect on solubility, but loss of activity.
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
36% identity, 85% coverage: 68:472/474 of query aligns to 66:484/484 of 5nnoA
- active site: N123 (= N125), K146 (= K148), E218 (= E220), S254 (≠ C254), E360 (= E350), Y439 (= Y429)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P76), Y124 (≠ F126), L127 (≠ M129), T253 (≠ I253), S254 (≠ C254), G422 (≠ A412)
- binding nicotinamide-adenine-dinucleotide: I119 (= I121), G120 (≠ V122), W122 (= W124), N123 (= N125), L128 (= L130), K146 (= K148), E149 (= E151), V178 (≠ A180), T181 (≠ A183), Y194 (≠ F196), T195 (= T197), G196 (= G198), S197 (= S199), V200 (= V202), E218 (= E220), L219 (= L221), S254 (≠ C254), E360 (= E350), F362 (= F352), F428 (= F418)
Q04458 Fatty aldehyde dehydrogenase HFD1; Hexadecenal dehydrogenase; EC 1.2.1.3; EC 1.2.1.64 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
33% identity, 89% coverage: 31:451/474 of query aligns to 45:471/532 of Q04458
- S241 (= S225) mutation to L: Causes Q deficiency.
- C273 (= C254) mutation to S: Abolishes catalytic activity.
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, 70% coverage: 111:444/474 of query aligns to 157:493/503 of O14293
- S248 (= S199) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
32% identity, 72% coverage: 107:446/474 of query aligns to 148:493/505 of 4neaA
- active site: N166 (= N125), K189 (= K148), E264 (= E220), C298 (= C254), E399 (= E350), E476 (≠ Y429)
- binding nicotinamide-adenine-dinucleotide: P164 (= P123), K189 (= K148), E192 (= E151), G222 (vs. gap), G226 (≠ A183), G242 (= G198), G243 (≠ S199), T246 (≠ V202), H249 (= H205), I250 (≠ V206), C298 (= C254), E399 (= E350), F401 (= F352)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
32% identity, 71% coverage: 110:444/474 of query aligns to 147:484/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I121), T159 (≠ V122), P160 (= P123), W161 (= W124), K185 (= K148), E188 (= E151), G218 (≠ A180), G222 (≠ A183), F236 (= F196), S239 (= S199), V242 (= V202)
Query Sequence
>7026109 FitnessBrowser__ANA3:7026109
MNMATDPAKISPLTELLQRQRASYLAAPNPDYAIRKERLLRLKAALLKFQQPLVEALSQD
YGHRSVDDSLISDIMPVVNNINYSLKNLKKWLKPSRRHAGILLAPAQVKVHYQPLGVIGI
IVPWNFPVMLSIGPLVTAIAAGNHAMLKLSEFTPATNSVIKQLLAEVFEESHVAVVEGEA
DVAAQFSALPFDHLLFTGSTTVGRHVMRAAANNLTPVTLELGGKSPVIIAPDMPLEIAVE
RMIYGKCLNAGQICVAPDYVLCPKAKVAEFIQAYQAKFQAMYGAITHNKDYGSIINARQF
ERLLTVLEDAKAKGAKVIPASNDVIDSQHRKLATQLITDTTEDMLLMQEEIFGPLLPVTG
YDNLDEAISYVNHRARPLALYVMSFDEASQQKILKQTHSGGVCINETVFHVAADDAPFGG
IGPSGMGHYHGKEGFLTFSHAKTVLSRGRFNTGKFVHPPYGTFIQRMLMKLFLR
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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