SitesBLAST
Comparing Echvi_3822 FitnessBrowser__Cola:Echvi_3822 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
49% identity, 100% coverage: 1:452/453 of query aligns to 2:452/453 of 4itbA
- active site: N130 (= N130), K153 (= K153), E227 (= E227), C261 (= C261), E358 (= E358), E435 (= E435)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (= V126), M127 (= M127), P128 (= P128), W129 (= W129), N130 (= N130), K153 (= K153), A155 (= A155), S156 (= S156), A186 (≠ S186), V189 (= V189), G205 (= G205), S206 (= S206), A209 (= A209), S212 (≠ K212), L228 (= L228), C261 (= C261), E358 (= E358), F360 (= F360)
- binding 4-oxobutanoic acid: E227 (= E227), C261 (= C261), S418 (= S418)
3vz3A Structural insights into substrate and cofactor selection by sp2771 (see paper)
49% identity, 100% coverage: 1:452/453 of query aligns to 2:452/453 of 3vz3A
- active site: N130 (= N130), K153 (= K153), E227 (= E227), A261 (≠ C261), E358 (= E358), E435 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V126 (= V126), M127 (= M127), W129 (= W129), N130 (= N130), Q135 (= Q135), R138 (= R138), K153 (= K153), A155 (= A155), S156 (= S156), A186 (≠ S186), V189 (= V189), T204 (= T204), G205 (= G205), S206 (= S206), A209 (= A209), E227 (= E227), L228 (= L228), G229 (= G229), A261 (≠ C261), F360 (= F360)
- binding 4-oxobutanoic acid: F131 (= F131), W134 (= W134), S260 (= S260), A261 (≠ C261), I262 (= I262), S418 (= S418)
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
45% identity, 99% coverage: 3:451/453 of query aligns to 8:455/459 of 3efvA
- active site: N134 (= N130), E231 (= E227), C265 (= C261), E439 (= E435)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ V126), M131 (= M127), P132 (= P128), W133 (= W129), N134 (= N130), Q139 (= Q135), R142 (= R138), K157 (= K153), A159 (= A155), N190 (≠ S186), V193 (= V189), T208 (= T204), G209 (= G205), S210 (= S206), A213 (= A209), E231 (= E227), L232 (= L228), G233 (= G229), C265 (= C261), E362 (= E358), F364 (= F360), F428 (= F424)
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
39% identity, 100% coverage: 2:452/453 of query aligns to 3:453/455 of 4ywuA
- active site: N131 (= N130), K154 (= K153), E228 (= E227), C262 (= C261), E359 (= E358), E436 (= E435)
- binding 4-oxobutanoic acid: N131 (= N130), Q136 (= Q135), R139 (= R138), E228 (= E227), V261 (≠ S260), C262 (= C261), F425 (= F424)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
39% identity, 100% coverage: 2:452/453 of query aligns to 3:453/455 of 4ohtA
- active site: N131 (= N130), K154 (= K153), E228 (= E227), C262 (= C261), E359 (= E358), E436 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (= V126), E128 (≠ M127), P129 (= P128), W130 (= W129), K154 (= K153), H155 (= H154), A156 (= A155), S157 (= S156), Y187 (≠ S186), S207 (= S206), I214 (= I213)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 99% coverage: 5:453/453 of query aligns to 32:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 99% coverage: 5:453/453 of query aligns to 31:480/481 of 3jz4A
- active site: N156 (= N130), K179 (= K153), E254 (= E227), C288 (= C261), E385 (= E358), E462 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P128), W155 (= W129), K179 (= K153), A181 (= A155), S182 (= S156), A212 (≠ S186), G216 (≠ A190), G232 (= G205), S233 (= S206), I236 (≠ A209), C288 (= C261), K338 (≠ E311), E385 (= E358), F387 (= F360)
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
33% identity, 99% coverage: 2:450/453 of query aligns to 29:482/493 of 6vr6D
- active site: N156 (= N130), E253 (= E227), C287 (= C261), E467 (= E435)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ V126), G153 (≠ M127), W155 (= W129), K179 (= K153), A212 (≠ S186), G215 (≠ V189), Q216 (≠ A190), F229 (≠ L203), G231 (= G205), S232 (= S206), T235 (≠ A209), I239 (= I213)
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)
33% identity, 99% coverage: 2:450/453 of query aligns to 30:483/494 of P49189
- C116 (= C89) 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
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)
31% identity, 99% coverage: 4:450/453 of query aligns to 28:482/497 of P17202
- I28 (= I4) binding
- D96 (≠ E70) binding
- SPW 156:158 (≠ MPW 127:129) binding
- Y160 (≠ F131) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R138) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KHAS 153:156) binding
- L186 (≠ N157) binding
- SSAT 236:239 (≠ SEKA 206:209) binding
- V251 (≠ I221) binding in other chain
- L258 (= L228) binding
- W285 (≠ I255) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E358) binding
- A441 (= A409) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S418) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F424) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K428) binding
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 99% coverage: 6:452/453 of query aligns to 43:494/503 of 1bpwA
- active site: N166 (= N130), K189 (= K153), E263 (= E227), C297 (= C261), E400 (= E358), E477 (= E435)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V126), L163 (≠ M127), W165 (= W129), N166 (= N130), K189 (= K153), G221 (= G185), G225 (≠ V189), T240 (= T204), G241 (= G205), S242 (= S206), T245 (≠ A209), E263 (= E227), L264 (= L228), C297 (= C261), E400 (= E358), F402 (= F360), F466 (= F424)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
31% identity, 99% coverage: 6:452/453 of query aligns to 43:494/503 of P56533
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 100% coverage: 1:452/453 of query aligns to 40:495/503 of O14293
- S248 (= S206) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 99% coverage: 4:450/453 of query aligns to 26:480/495 of 4v37A
- active site: N157 (= N130), K180 (= K153), E255 (= E227), A289 (≠ C261), E388 (= E358), E465 (= E435)
- binding 3-aminopropan-1-ol: C448 (≠ S418), W454 (≠ F424)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V126), S154 (≠ M127), P155 (= P128), W156 (= W129), N157 (= N130), M162 (≠ Q135), K180 (= K153), S182 (≠ A155), E183 (≠ S156), G213 (= G185), G217 (≠ V189), A218 (= A190), T232 (= T204), G233 (= G205), S234 (= S206), T237 (≠ A209), E255 (= E227), L256 (= L228), A289 (≠ C261), E388 (= E358), F390 (= F360)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
32% identity, 96% coverage: 19:452/453 of query aligns to 44:482/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W129), K180 (= K153), A182 (= A155), T212 (≠ S186), G213 (≠ D187), G217 (≠ N191), F231 (≠ L203), G233 (= G205), S234 (= S206), V237 (≠ A209), Q337 (≠ L308), E388 (= E358), F390 (= F360)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
32% identity, 99% coverage: 1:450/453 of query aligns to 25:485/503 of Q8VWZ1
- N27 (≠ S3) binding
- I28 (= I4) binding
- D99 (≠ E70) binding
- L189 (≠ N157) binding
- 238:245 (vs. 205:212, 50% identical) binding
- C294 (= C261) binding
- E393 (= E358) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
32% identity, 99% coverage: 1:450/453 of query aligns to 20:480/497 of 3iwkH
- active site: N157 (= N130), K180 (= K153), E255 (= E227), C289 (= C261), E388 (= E358), E465 (= E435)
- binding nicotinamide-adenine-dinucleotide: W156 (= W129), G213 (= G185), G217 (≠ V189), A218 (= A190), G233 (= G205), S234 (= S206), T237 (≠ A209), K240 (= K212), C289 (= C261), Q336 (≠ L312), E388 (= E358), F390 (= F360)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
32% identity, 99% coverage: 5:452/453 of query aligns to 24:475/494 of 5izdA
- active site: N149 (= N130), K172 (= K153), E247 (= E227), C281 (= C261), E381 (= E358), E458 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ V126), T146 (≠ M127), W148 (= W129), K172 (= K153), P173 (≠ H154), S174 (≠ A155), S175 (= S156), R204 (≠ I184), G205 (= G185), G209 (≠ V189), D210 (≠ A190), G225 (= G205), S226 (= S206), T229 (≠ A209)
7radA Crystal structure analysis of aldh1b1
31% identity, 99% coverage: 3:452/453 of query aligns to 32:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V126), I159 (≠ M127), P160 (= P128), W161 (= W129), N162 (= N130), M167 (vs. gap), K185 (= K153), E188 (≠ S156), G218 (= G185), G222 (≠ V189), A223 (= A190), T237 (= T204), G238 (= G205), S239 (= S206), V242 (≠ A209), E261 (= E227), L262 (= L228), C295 (= C261), E392 (= E358), F394 (= F360)
- 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 (≠ K84), F163 (= F131), E285 (≠ K251), F289 (≠ I255), N450 (≠ V416), V452 (≠ S418)
7mjdA Crystal structure analysis of aldh1b1
31% identity, 99% coverage: 3:452/453 of query aligns to 32:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V126), I159 (≠ M127), P160 (= P128), W161 (= W129), N162 (= N130), M167 (vs. gap), K185 (= K153), E188 (≠ S156), G218 (= G185), G222 (≠ V189), F236 (≠ L203), T237 (= T204), G238 (= G205), S239 (= S206), V242 (≠ A209), E261 (= E227), L262 (= L228), C295 (= C261), E392 (= E358), F394 (= F360)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ K84), E285 (≠ K251), F289 (≠ I255), N450 (≠ V416), V452 (≠ S418)
Query Sequence
>Echvi_3822 FitnessBrowser__Cola:Echvi_3822
MKSINPYTGELLEEFTDHTEQQVEAAIQKGQEAYLSWRELPISQRADLMKKAGQVLRDNT
DKYGKIISLEMGKVITESKSEVEKCAWVCEYYAENAEEMLADAPIALPDGKEAKVVYNPL
GIVLAVMPWNFPFWQVFRFAAPNLTAGNVGLLKHASNVPQCALAIEEVFTQAGFPEGVFQ
SLLIGSDKVANIIAHPDVKAATLTGSEKAGQKIAAQAGEQIKKTVLELGGSDPFIVLKDA
DVKEAAKTAAKGRMINFGQSCIAAKRFIIEQEVYDEFITHFKSAIESYVPGDPLDEKAGY
ACMARPDLAMELYEQVEASIQKGAEVILEGTKPEKGKAFIKPYILGKLTPDMPAYREELF
GPVASVFKANDVDEAIAIANDSAFGLGASLWTQDPQKADILSRKIESGAVFINSMVASNP
YLPFGGIKKSGYGRELAENGIKEFMNIKTVYLG
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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