SitesBLAST
Comparing GFF3619 PGA1_262p00230 betaine aldehyde dehydrogenase BetB 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)
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)
39% identity, 93% coverage: 34:494/494 of query aligns to 25:487/494 of P49189
- C116 (≠ L125) 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)
39% identity, 93% coverage: 34:494/494 of query aligns to 24:486/493 of 6vr6D
- active site: N156 (= N166), E253 (= E264), C287 (= C298), E467 (= E475)
- binding nicotinamide-adenine-dinucleotide: I152 (= I162), G153 (≠ V163), W155 (= W165), K179 (= K189), A212 (≠ I223), G215 (= G226), Q216 (≠ A227), F229 (= F240), G231 (= G242), S232 (= S243), T235 (= T246), I239 (≠ V250)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 95% coverage: 24:494/494 of query aligns to 9:482/489 of 4cazA
- active site: N152 (= N166), K175 (= K189), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E475)
- 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 (= I162), G149 (≠ V163), W151 (= W165), N152 (= N166), K175 (= K189), E178 (= E192), G208 (= G222), G212 (= G226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (= T246), V236 (= V250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E398), F388 (= F400)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 95% coverage: 24:494/494 of query aligns to 9:482/489 of 2woxA
- active site: N152 (= N166), K175 (= K189), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I162), G149 (≠ V163), W151 (= W165), N152 (= N166), K175 (= K189), S177 (≠ A191), E178 (= E192), G208 (= G222), G212 (= G226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (= T246), V236 (= V250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E398), F388 (= F400)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 95% coverage: 24:494/494 of query aligns to 9:482/489 of 2wmeA
- active site: N152 (= N166), K175 (= K189), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ V163), W151 (= W165), K175 (= K189), S177 (≠ A191), E178 (= E192), G208 (= G222), G212 (= G226), F226 (= F240), G228 (= G242), G229 (≠ S243), T232 (= T246), V236 (= V250)
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)
39% identity, 95% coverage: 24:494/494 of query aligns to 10:483/490 of Q9HTJ1
- GAWN 150:153 (≠ VPWN 163:166) binding
- K162 (≠ G175) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 189:192) binding
- G209 (= G222) binding
- GTST 230:233 (≠ SVAT 243:246) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C298) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E398) binding
- E464 (= E475) active site, Charge relay system
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
44% identity, 95% coverage: 22:492/494 of query aligns to 2:473/476 of 4yweA
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
39% identity, 96% coverage: 23:494/494 of query aligns to 22:496/503 of 1bpwA
- active site: N166 (= N166), K189 (= K189), E263 (= E264), C297 (= C298), E400 (= E398), E477 (= E475)
- binding nicotinamide-adenine-dinucleotide: I162 (= I162), L163 (≠ V163), W165 (= W165), N166 (= N166), K189 (= K189), G221 (= G222), G225 (= G226), T240 (= T241), G241 (= G242), S242 (= S243), T245 (= T246), E263 (= E264), L264 (= L265), C297 (= C298), E400 (= E398), F402 (= F400), F466 (= F464)
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)
39% identity, 96% coverage: 23:494/494 of query aligns to 22:496/503 of P56533
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)
40% identity, 97% coverage: 15:491/494 of query aligns to 2:483/497 of P17202
- I28 (≠ F41) binding
- D96 (= D107) binding
- SPW 156:158 (≠ VPW 163:165) binding
- Y160 (= Y167) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R174) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 189:192) binding
- L186 (≠ T193) binding
- SSAT 236:239 (≠ SVAT 243:246) binding
- V251 (= V258) binding in other chain
- L258 (= L265) binding
- W285 (≠ S292) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E398) binding
- A441 (≠ Q449) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G458) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F464) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R468) binding
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 95% coverage: 21:491/494 of query aligns to 10:488/505 of O24174
- N164 (= N166) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ R174) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
40% identity, 95% coverage: 24:494/494 of query aligns to 7:479/489 of 4o6rA
- active site: N150 (= N166), K173 (= K189), E248 (= E264), C282 (= C298), E383 (= E398), E460 (= E475)
- binding adenosine monophosphate: I146 (= I162), V147 (= V163), K173 (= K189), G206 (= G222), G210 (= G226), Q211 (≠ A227), F224 (= F240), G226 (= G242), S227 (= S243), T230 (= T246), R233 (≠ G249)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 95% coverage: 24:490/494 of query aligns to 9:476/486 of 4pxlA
- active site: N154 (= N166), K177 (= K189), E253 (= E264), C287 (= C298), E384 (= E398), D461 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I150 (= I162), V151 (= V163), P152 (= P164), W153 (= W165), K177 (= K189), E180 (= E192), G210 (= G222), G214 (= G226), A215 (= A227), F228 (= F240), G230 (= G242), S231 (= S243), V234 (≠ T246), E253 (= E264), G255 (= G266), C287 (= C298), Q334 (≠ N340), K337 (≠ R343), E384 (= E398), F386 (= F400)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
40% identity, 96% coverage: 16:491/494 of query aligns to 1:481/495 of 4v37A
- active site: N157 (= N166), K180 (= K189), E255 (= E264), A289 (≠ C298), E388 (= E398), E465 (= E475)
- binding 3-aminopropan-1-ol: C448 (≠ G458), W454 (≠ F464)
- binding nicotinamide-adenine-dinucleotide: I153 (= I162), S154 (≠ V163), P155 (= P164), W156 (= W165), N157 (= N166), M162 (≠ T171), K180 (= K189), S182 (≠ A191), E183 (= E192), G213 (= G222), G217 (= G226), A218 (= A227), T232 (= T241), G233 (= G242), S234 (= S243), T237 (= T246), E255 (= E264), L256 (= L265), A289 (≠ C298), E388 (= E398), F390 (= F400)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 97% coverage: 13:492/494 of query aligns to 11:493/501 of Q56YU0
- G152 (≠ A149) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A415) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 95% coverage: 21:491/494 of query aligns to 8:486/503 of Q84LK3
- N162 (= N166) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ R174) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
37% identity, 95% coverage: 24:494/494 of query aligns to 17:490/497 of 8skfA
- binding calcium ion: T33 (≠ S40), I34 (≠ F41), D100 (= D107), V187 (≠ T193)
- binding nicotinamide-adenine-dinucleotide: I156 (= I162), G157 (≠ V163), A158 (≠ P164), W159 (= W165), K183 (= K189), E186 (= E192), G216 (= G222), G220 (= G226), T235 (= T241), G236 (= G242), G237 (≠ S243), S240 (≠ T246), K243 (≠ G249), E259 (= E264), C293 (= C298), F396 (= F400)
P54115 Magnesium-activated aldehyde dehydrogenase, cytosolic; Mg(2+)-activated acetaldehyde dehydrogenase; Mg(2+)-ACDH; EC 1.2.1.-; EC 1.2.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
36% identity, 98% coverage: 13:494/494 of query aligns to 18:500/500 of P54115
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 3 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
37% identity, 95% coverage: 24:494/494 of query aligns to 8:481/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
37% identity, 95% coverage: 24:494/494 of query aligns to 8:481/488 of 8vr0A
Query Sequence
>GFF3619 PGA1_262p00230 betaine aldehyde dehydrogenase BetB
MSVDGLIAAYFDTGALPDLPRDHFIDGRAVAPGAGGRMESFDPGRGTAFDDFAAGDAADV
DHAVTSAVAGFEIWSATPPARRCAILNEAARLMRHEAEHLAVVECVDSGKTLAEARGDIA
GSARLLEYYAGAADKLDGRSVNLGNDNAAFTLREPVGVTAHIVPWNYPSSTLVRGIAPAL
AAGCSAVVKPAETTPFTALMIADLLIRAGLPAGVVNVVTGTGIAAGAPLVRDPRVRHVTF
TGSVATGVGVMQSVAPNVTGLTLELGGKSPLVAFGDANVDAVVEGALWAIFSNAGQICSA
GSRLVIHRSLHAEVRDKLVARAQRLRVGHGLRGPDIGAVNSARHLAQIDDHVSRARTRGV
EIVTGGEILTDVESGKGWFYAPTILDDLAANDDAVLQEIFGPVLAIQVFEDEAEALALAN
GTEFALAAGIYTRDIATALRMARRVDAGQVTVNDYWAGGIELPFGGNRKSGFGREKGLEG
LDAYTRSKAVTLAV
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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