SitesBLAST
Comparing Ac3H11_612 FitnessBrowser__acidovorax_3H11:Ac3H11_612 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)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
39% identity, 97% coverage: 12:478/483 of query aligns to 29:500/515 of 2d4eC
- active site: N173 (= N155), K196 (= K178), E271 (= E253), C305 (= C287), E409 (= E385), E486 (= E464)
- binding nicotinamide-adenine-dinucleotide: I169 (= I151), T170 (≠ A152), P171 (= P153), W172 (= W154), K196 (= K178), A198 (= A180), G229 (= G211), G233 (= G215), A234 (≠ Q216), T248 (= T230), G249 (= G231), E250 (≠ S232), T253 (= T235), E271 (= E253), L272 (≠ M254), C305 (= C287), E409 (= E385), F411 (= F387), F475 (= F452)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 94% coverage: 27:478/483 of query aligns to 25:477/489 of 4cazA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I151), G149 (≠ A152), W151 (= W154), N152 (= N155), K175 (= K178), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (≠ M254), C285 (= C287), E386 (= E385), F388 (= F387)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
38% identity, 94% coverage: 27:478/483 of query aligns to 25:477/489 of 2woxA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I151), G149 (≠ A152), W151 (= W154), N152 (= N155), K175 (= K178), S177 (≠ A180), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), T227 (= T230), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (≠ M254), C285 (= C287), E386 (= E385), F388 (= F387)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
38% identity, 94% coverage: 27:478/483 of query aligns to 25:477/489 of 2wmeA
- active site: N152 (= N155), K175 (= K178), E251 (= E253), C285 (= C287), E386 (= E385), E463 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ A152), W151 (= W154), K175 (= K178), S177 (≠ A180), E178 (= E181), G208 (= G211), G212 (= G215), F226 (= F229), G228 (= G231), G229 (≠ S232), T232 (= T235), V236 (≠ I239)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
38% identity, 94% coverage: 27:478/483 of query aligns to 26:478/490 of Q9HTJ1
- GAWN 150:153 (≠ APWN 152:155) binding
- K162 (= K164) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 178:181) binding
- G209 (= G211) binding
- GTST 230:233 (≠ SVAT 232:235) binding
- E252 (= E253) active site, Proton acceptor
- C286 (= C287) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding
- E464 (= E464) active site, Charge relay system
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)
36% identity, 96% coverage: 13:477/483 of query aligns to 11:480/497 of P17202
- I28 (≠ T28) binding
- D96 (≠ E95) binding
- SPW 156:158 (≠ APW 152:154) binding
- Y160 (≠ F156) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 178:181) binding
- L186 (= L182) binding
- SSAT 236:239 (≠ SVAT 232:235) binding
- V251 (≠ R247) binding in other chain
- L258 (≠ M254) binding
- W285 (≠ F281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding
- A441 (≠ M436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V446) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F452) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 96% coverage: 13:477/483 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N155), K180 (= K178), E255 (= E253), A289 (≠ C287), E388 (= E385), E465 (= E464)
- binding 3-aminopropan-1-ol: C448 (≠ V446), W454 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I151), S154 (≠ A152), P155 (= P153), W156 (= W154), N157 (= N155), M162 (≠ I160), K180 (= K178), S182 (≠ A180), E183 (= E181), G213 (= G211), G217 (= G215), A218 (≠ Q216), T232 (= T230), G233 (= G231), S234 (= S232), T237 (= T235), E255 (= E253), L256 (≠ M254), A289 (≠ C287), E388 (= E385), F390 (= F387)
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)
35% identity, 98% coverage: 7:477/483 of query aligns to 15:489/505 of 4neaA
- active site: N166 (= N155), K189 (= K178), E264 (= E253), C298 (= C287), E399 (= E385), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P153), K189 (= K178), E192 (= E181), G222 (= G211), G226 (= G215), G242 (= G231), G243 (≠ S232), T246 (= T235), H249 (≠ R238), I250 (= I239), C298 (= C287), E399 (= E385), F401 (= F387)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
38% identity, 94% coverage: 29:481/483 of query aligns to 25:477/489 of 4o6rA
- active site: N150 (= N155), K173 (= K178), E248 (= E253), C282 (= C287), E383 (= E385), E460 (= E464)
- binding adenosine monophosphate: I146 (= I151), V147 (≠ A152), K173 (= K178), G206 (= G211), G210 (= G215), Q211 (= Q216), F224 (= F229), G226 (= G231), S227 (= S232), T230 (= T235), R233 (= R238)
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)
37% identity, 100% coverage: 1:481/483 of query aligns to 1:478/482 of P25526
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)
36% identity, 92% coverage: 33:478/483 of query aligns to 36:482/494 of P49189
- C116 (≠ I113) 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
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
36% identity, 92% coverage: 33:478/483 of query aligns to 35:481/493 of 6vr6D
- active site: N156 (= N155), E253 (= E253), C287 (= C287), E467 (= E464)
- binding nicotinamide-adenine-dinucleotide: I152 (= I151), G153 (≠ A152), W155 (= W154), K179 (= K178), A212 (≠ R212), G215 (= G215), Q216 (= Q216), F229 (= F229), G231 (= G231), S232 (= S232), T235 (= T235), I239 (= I239)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 99% coverage: 2:481/483 of query aligns to 1:477/481 of 3jz4A
- active site: N156 (= N155), K179 (= K178), E254 (= E253), C288 (= C287), E385 (= E385), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P153), W155 (= W154), K179 (= K178), A181 (= A180), S182 (≠ E181), A212 (≠ G211), G216 (= G215), G232 (= G231), S233 (= S232), I236 (≠ T235), C288 (= C287), K338 (≠ Q337), E385 (= E385), F387 (= F387)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
36% identity, 92% coverage: 29:474/483 of query aligns to 33:493/511 of 6fkuA
- active site: N159 (= N155), E261 (= E253), C295 (= C287), E483 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I151), T156 (≠ A152), N159 (= N155), K182 (= K178), S184 (≠ A180), E185 (= E181), G214 (≠ S210), G215 (= G211), K216 (≠ R212), G220 (= G215), Q221 (= Q216), F237 (= F229), T238 (= T230), G239 (= G231), S240 (= S232), V243 (≠ T235), E261 (= E253), L262 (≠ M254), C295 (= C287), R342 (≠ N333), F343 (≠ Q334), E404 (= E385), F406 (= F387)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
33% identity, 97% coverage: 12:478/483 of query aligns to 12:482/487 of Q9H2A2
- R109 (= R109) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N155) mutation to A: Complete loss of activity.
- R451 (≠ G445) mutation to A: Complete loss of activity.
7radA Crystal structure analysis of aldh1b1
37% identity, 96% coverage: 13:478/483 of query aligns to 16:483/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I151), I159 (≠ A152), P160 (= P153), W161 (= W154), N162 (= N155), M167 (≠ I160), K185 (= K178), E188 (= E181), G218 (= G211), G222 (= G215), A223 (≠ Q216), T237 (= T230), G238 (= G231), S239 (= S232), V242 (≠ T235), E261 (= E253), L262 (≠ M254), C295 (= C287), E392 (= E385), F394 (= F387)
- 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 (≠ R109), F163 (= F156), E285 (≠ Q277), F289 (= F281), N450 (≠ T443), V452 (= V446)
7mjdA Crystal structure analysis of aldh1b1
37% identity, 96% coverage: 13:478/483 of query aligns to 16:483/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I151), I159 (≠ A152), P160 (= P153), W161 (= W154), N162 (= N155), M167 (≠ I160), K185 (= K178), E188 (= E181), G218 (= G211), G222 (= G215), F236 (= F229), T237 (= T230), G238 (= G231), S239 (= S232), V242 (≠ T235), E261 (= E253), L262 (≠ M254), C295 (= C287), E392 (= E385), F394 (= F387)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R109), E285 (≠ Q277), F289 (= F281), N450 (≠ T443), V452 (= V446)
7mjcA Crystal structure analysis of aldh1b1
37% identity, 96% coverage: 13:478/483 of query aligns to 16:483/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I151), I159 (≠ A152), P160 (= P153), W161 (= W154), N162 (= N155), K185 (= K178), E188 (= E181), G218 (= G211), G222 (= G215), T237 (= T230), G238 (= G231), S239 (= S232), V242 (≠ T235), E261 (= E253), L262 (≠ M254), C295 (= C287), E392 (= E385), F394 (= F387)
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)
35% identity, 98% coverage: 6:477/483 of query aligns to 3:483/503 of Q8VWZ1
- N27 (≠ S27) binding
- I28 (≠ T28) binding
- D99 (≠ E95) binding
- L189 (= L182) binding
- 238:245 (vs. 231:238, 63% identical) binding
- C294 (= C287) binding
- E393 (= E385) binding
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
37% identity, 93% coverage: 29:477/483 of query aligns to 27:479/496 of 4i9bA
- active site: N157 (= N155), K180 (= K178), E255 (= E253), C290 (= C287), E389 (= E385), D466 (≠ E464)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C287), W455 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I151), T154 (≠ A152), W156 (= W154), K180 (= K178), S182 (≠ A180), E183 (= E181), G213 (= G211), G217 (= G215), G218 (≠ Q216), F231 (= F229), S234 (= S232), T237 (= T235), I241 (= I239)
Query Sequence
>Ac3H11_612 FitnessBrowser__acidovorax_3H11:Ac3H11_612
MKLGDLQLSPRHLINGRWEIGTTTGISTNPSDTREVVAEYARADRNQTELAVRAAADALP
TWSQSTPQRRADVLDMIGSELLARKDELGALLAREEGKTLPEGVAEVARSGQIFKFFAGE
ALRIQGELLASVRQGVQVDVTREPVGVVGIIAPWNFPFAIPAWKIAPALAYGNTVVFKPA
ELVPACGWALAEIISRSGLPAGAFNLIMGSGREVGQTLVDHPLVNALSFTGSVATGDRIL
RAASQRRAKVQLEMGGKNPLIVLADADLDQAVDCALQGSYFSTGQRCTASSRLIVEAEVH
DAFVARLRNRLASLKVGHALERGTEMGPVVDDNQLAQNLGYIDIAKSEGAEHVWGGERLE
RPTPGHYMSPALFLARPEHRVAREEIFGPVACVLRADDYDHALALANDTPFGLCAGICTT
SLKRAMHFKRHAAVGMTMVNLPTAGVDFHVPFGGRKESSYGAREQGRYAAEFYTTVKTGY
MLA
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