SitesBLAST
Comparing WP_068173812.1 NCBI__GCF_001592305.1:WP_068173812.1 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)
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
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 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)
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 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)
37% identity, 98% coverage: 8:478/483 of query aligns to 4:477/489 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)
37% identity, 98% coverage: 8:478/483 of query aligns to 5:478/490 of Q9HTJ1
- GAWN 150:153 (≠ APWN 152:155) binding NADPH
- K162 (= K164) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 178:181) binding NADPH
- G209 (= G211) binding NADPH
- GTST 230:233 (≠ SVST 232:235) binding NADPH
- E252 (= E253) active site, Proton acceptor
- C286 (= C287) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding NADPH
- 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)
35% identity, 96% coverage: 13:477/483 of query aligns to 11:480/497 of P17202
- I28 (≠ T28) binding K(+)
- D96 (≠ E95) binding K(+)
- SPW 156:158 (≠ APW 152:154) binding NAD(+)
- 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 NAD(+)
- L186 (= L182) binding K(+)
- SSAT 236:239 (≠ SVST 232:235) binding NAD(+)
- V251 (≠ R247) binding in other chain
- L258 (≠ M254) binding NAD(+)
- W285 (≠ F281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding NAD(+)
- 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 NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding K(+)
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
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 97% coverage: 13:481/483 of query aligns to 7:477/489 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)
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)
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