SitesBLAST
Comparing WP_010177305.1 NCBI__GCF_000255455.1:WP_010177305.1 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)
44% identity, 96% coverage: 15:462/469 of query aligns to 1:448/485 of P51648
- I45 (= I63) to F: in SLS; severe loss of activity
- V64 (≠ L82) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (= L124) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N130) mutation to A: Loss of enzyme activity.
- P114 (= P132) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P139) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T202) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G203) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E225) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A232) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R246) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A255) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C259) active site; mutation to S: Loss of enzyme activity.
- D245 (= D263) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ A281) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (≠ F295) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ EP 330:331) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P331) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E347) mutation to Q: Loss of enzyme activity.
- S365 (= S381) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y426) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H427) to Y: in SLS; severe loss of activity
- S415 (= S431) to N: in SLS; severe loss of activity
- F419 (= F435) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K439) to H: in SLS; severe loss of activity; dbSNP:rs768290318
- K447 (= K461) to E: in SLS; severe loss of activity; dbSNP:rs67939114
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.
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)
43% identity, 95% coverage: 17:462/469 of query aligns to 2:450/453 of P30838
- S134 (≠ T149) to A: in dbSNP:rs887241
- E210 (= E225) active site
- C244 (= C259) active site; mutation to S: Abolishes activity.
- P329 (≠ A342) to A: in allele ALDH3A1*2; dbSNP:rs2228100
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione (see paper)
43% identity, 95% coverage: 17:462/469 of query aligns to 1:449/452 of 4l1oB
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E347), Y412 (= Y426)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (≠ F131), N118 (= N134), L119 (≠ I135), E209 (= E225), T242 (≠ I258), C243 (= C259), I391 (= I405), I394 (≠ F408), F401 (= F415), H413 (= H427)
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
43% identity, 93% coverage: 17:453/469 of query aligns to 1:439/447 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)
43% identity, 93% coverage: 17:453/469 of query aligns to 1:439/447 of 3szbA
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
43% identity, 93% coverage: 17:453/469 of query aligns to 1:439/446 of 4l2oA
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E347), Y412 (= Y426)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ T77), Y65 (≠ P81), Y115 (≠ F131), N118 (= N134), L119 (≠ I135), M237 (≠ L253), C243 (= C259), I391 (= I405), I394 (≠ F408), T395 (= T409), F401 (= F415), H413 (= H427)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ A128), W113 (= W129), N114 (= N130), L119 (≠ I135), E140 (= E156), V169 (≠ I185), T186 (= T202), G187 (= G203), S188 (= S204), V191 (= V207), E209 (= E225), L210 (= L226), G211 (= G227), C243 (= C259), H289 (≠ N303), E333 (= E347), F335 (= F349), F401 (= F415)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
43% identity, 93% coverage: 17:453/469 of query aligns to 1:439/446 of 4h80A
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E347), Y412 (= Y426)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ T77), Y65 (≠ P81), Y115 (≠ F131), N118 (= N134), W233 (≠ S249), T242 (≠ I258), C243 (= C259), V244 (≠ I260), I394 (≠ F408), T395 (= T409), F401 (= F415)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
40% identity, 96% coverage: 17:468/469 of query aligns to 10:468/484 of Q70DU8
- C45 (≠ L52) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E156) 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 (≠ I185) 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 (≠ V207) 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 (≠ L253) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C259) mutation to S: No effect on solubility, but loss of activity.
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
45% identity, 89% coverage: 27:445/469 of query aligns to 10:430/446 of 1ad3A
- active site: N113 (= N130), K136 (= K153), E208 (= E225), C242 (= C259), E332 (= E347), Y411 (= Y426)
- binding nicotinamide-adenine-dinucleotide: A111 (= A128), W112 (= W129), N113 (= N130), E139 (= E156), V140 (≠ M157), V168 (≠ I185), G186 (= G203), V190 (= V207), H288 (≠ N303), R291 (= R306), E332 (= E347), F334 (= F349)
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
42% identity, 96% coverage: 18:469/469 of query aligns to 74:532/550 of Q8W033
- C114 (≠ Q58) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I86) mutation to S: No effect on solubility, but decreased activity.
- V263 (= V207) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ N230) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ L253) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C259) mutation to S: No effect on solubility, but loss of activity.
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; Long-chain fatty aldehyde dehydrogenase; Medium-chain fatty aldehyde dehydrogenase; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7; EC 1.2.1.48 from Homo sapiens (Human) (see paper)
41% identity, 95% coverage: 22:465/469 of query aligns to 4:454/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldh3B2; Aldehyde dehydrogenase 8; Long-chain fatty aldehyde dehydrogenase; EC 1.2.1.3; EC 1.2.1.48 from Mus musculus (Mouse) (see paper)
40% identity, 98% coverage: 7:465/469 of query aligns to 5:467/479 of E9Q3E1
- W462 (≠ T460) 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.
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
39% identity, 98% coverage: 7:466/469 of query aligns to 9:468/479 of J3QMK6
- RR 462:463 (≠ TK 460:461) mutation to AA: Reduces membrane localization.
Q80VQ0 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; Long-chain fatty aldehyde dehydrogenase; Medium-chain fatty aldehyde dehydrogenase; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7; EC 1.2.1.48 from Mus musculus (Mouse) (see paper)
39% identity, 97% coverage: 12:465/469 of query aligns to 1:454/468 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.
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
39% identity, 91% coverage: 17:441/469 of query aligns to 6:431/435 of 5ucdA
- active site: N119 (= N130), K142 (= K153), E214 (= E225), C248 (= C259), E336 (= E347), Y416 (= Y426)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I126), G116 (= G127), F118 (≠ W129), N119 (= N130), K142 (= K153), S144 (= S155), E145 (= E156), R174 (≠ I185), F190 (= F201), T191 (= T202), G192 (= G203), S193 (= S204), V196 (= V207), E214 (= E225), L215 (= L226), C248 (= C259), E336 (= E347), F338 (= F349)
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
36% identity, 98% coverage: 11:469/469 of query aligns to 5:484/484 of 5nnoA
- active site: N123 (= N130), K146 (= K153), E218 (= E225), S254 (≠ C259), E360 (= E347), Y439 (= Y426)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P81), Y124 (≠ F131), L127 (≠ N134), T253 (≠ I258), S254 (≠ C259), G422 (≠ T409)
- binding nicotinamide-adenine-dinucleotide: I119 (= I126), G120 (= G127), W122 (= W129), N123 (= N130), L128 (≠ I135), K146 (= K153), E149 (= E156), V178 (≠ I185), T181 (= T188), Y194 (≠ F201), T195 (= T202), G196 (= G203), S197 (= S204), V200 (= V207), E218 (= E225), L219 (= L226), S254 (≠ C259), E360 (= E347), F362 (= F349), F428 (= F415)
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)
34% identity, 96% coverage: 17:466/469 of query aligns to 15:491/532 of Q04458
- S241 (≠ N230) mutation to L: Causes Q deficiency.
- C273 (= C259) mutation to S: Abolishes catalytic activity.
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
29% identity, 96% coverage: 2:450/469 of query aligns to 33:491/493 of 6vr6D
- active site: N156 (= N130), E253 (= E225), C287 (= C259), E467 (≠ Y426)
- binding nicotinamide-adenine-dinucleotide: I152 (= I126), G153 (= G127), W155 (= W129), K179 (= K153), A212 (≠ I185), G215 (≠ T189), Q216 (≠ A190), F229 (= F201), G231 (= G203), S232 (= S204), T235 (≠ V207), I239 (≠ V211)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
29% identity, 96% coverage: 2:450/469 of query aligns to 34:492/494 of P49189
- C116 (≠ N92) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 74% coverage: 96:441/469 of query aligns to 137:493/503 of O14293
- S248 (= S204) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
Query Sequence
>WP_010177305.1 NCBI__GCF_000255455.1:WP_010177305.1
MPNTIKKTDTEITSFETEVKALIDTQRKFFYSNATKPVSFRIAQLKKLKQLLKDNEAQLH
KAIYADLRKSEFDNLTTELLPLYSEIDYAVKNLKKWATPKRVKTTILNFPSKSYIVAEPL
GVSLIIGAWNFPYNIALIPIVGAIAAGNTSILKPSEMAPATSAIMAELINKNFPSNYLKV
LQGGIPETTAILKQRFDKIFFTGSPQVGKIVNQAAAPHLTNVTLELGGKNPAIFTKDCSL
NIGVKRMVSGKFLNAGQICITSDYVLVQKDIKEKFLTQVVAEIKKQNYSIENGNFVELIN
DKNFDRIVSLIDSQKVYYGGNYIKETRFIEPTILTNVSVDDAVMQEEIFGPVLPVIEYDT
IDEAFAIIQKFEKPLSAYLFSNNSTIKKRFLNEVSFGNGAINDSIMQFTNHNLPFGGVGN
SGTGSYHGKFSFDCFSHAKSILSKSTWIEANLKYYEHTDTKMKIIKKLF
Or try a new SitesBLAST search
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