SitesBLAST
Comparing GFF3742 PGA1_262p01460 aldehyde dehydrogenase 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)
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)
33% identity, 96% coverage: 20:496/497 of query aligns to 18:497/505 of 4neaA
- active site: N166 (= N165), K189 (= K188), E264 (= E263), C298 (= C297), E399 (= E396), E476 (= E475)
- binding nicotinamide-adenine-dinucleotide: P164 (= P163), K189 (= K188), E192 (≠ N191), G222 (= G221), G226 (= G225), G242 (= G241), G243 (≠ S242), T246 (≠ V245), H249 (≠ G248), I250 (= I249), C298 (= C297), E399 (= E396), F401 (= F398)
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)
35% identity, 96% coverage: 20:495/497 of query aligns to 7:484/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 162:165) binding
- K162 (= K174) active site, Charge relay system
- KPSE 176:179 (≠ KPAN 188:191) binding
- G209 (= G221) binding
- GTST 230:233 (≠ SVPV 242:245) binding
- E252 (= E263) active site, Proton acceptor
- C286 (= C297) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E396) binding
- E464 (= E475) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
35% identity, 96% coverage: 20:495/497 of query aligns to 6:483/489 of 4cazA
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C297), E386 (= E396), 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 (= I161), G149 (≠ S162), W151 (= W164), N152 (= N165), K175 (= K188), E178 (≠ N191), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ V245), V236 (≠ I249), E251 (= E263), L252 (≠ M264), C285 (= C297), E386 (= E396), F388 (= F398)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
35% identity, 96% coverage: 20:495/497 of query aligns to 6:483/489 of 2woxA
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C297), E386 (= E396), E463 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I161), G149 (≠ S162), W151 (= W164), N152 (= N165), K175 (= K188), S177 (≠ A190), E178 (≠ N191), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ V245), V236 (≠ I249), E251 (= E263), L252 (≠ M264), C285 (= C297), E386 (= E396), F388 (= F398)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
35% identity, 96% coverage: 20:495/497 of query aligns to 6:483/489 of 2wmeA
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C297), E386 (= E396), E463 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S162), W151 (= W164), K175 (= K188), S177 (≠ A190), E178 (≠ N191), G208 (= G221), G212 (= G225), F226 (= F239), G228 (= G241), G229 (≠ S242), T232 (≠ V245), V236 (≠ I249)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
36% identity, 92% coverage: 39:493/497 of query aligns to 25:478/489 of 4o6rA
- active site: N150 (= N165), K173 (= K188), E248 (= E263), C282 (= C297), E383 (= E396), E460 (= E475)
- binding adenosine monophosphate: I146 (= I161), V147 (≠ S162), K173 (= K188), G206 (= G221), G210 (= G225), Q211 (= Q226), F224 (= F239), G226 (= G241), S227 (= S242), T230 (≠ V245), R233 (≠ G248)
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)
33% identity, 95% coverage: 20:492/497 of query aligns to 11:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 95% coverage: 20:492/497 of query aligns to 10:479/481 of 3jz4A
- active site: N156 (= N165), K179 (= K188), E254 (= E263), C288 (= C297), E385 (= E396), E462 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P163), W155 (= W164), K179 (= K188), A181 (= A190), S182 (≠ N191), A212 (≠ G221), G216 (= G225), G232 (= G241), S233 (= S242), I236 (≠ V245), C288 (= C297), K338 (≠ E347), E385 (= E396), F387 (= F398)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
38% identity, 91% coverage: 45:495/497 of query aligns to 32:482/489 of 6wsbA
- active site: N152 (= N165), E250 (= E263), C284 (= C297), E462 (= E475)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), G149 (≠ S162), A150 (≠ P163), W151 (= W164), N152 (= N165), K175 (= K188), E178 (≠ N191), G208 (= G221), G211 (= G225), A212 (≠ Q226), F225 (= F239), T226 (= T240), G227 (= G241), G228 (≠ S242), T231 (≠ V245), V235 (≠ I249), E250 (= E263), L251 (≠ M264), G252 (= G265), C284 (= C297), E385 (= E396), F387 (= F398)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
35% identity, 97% coverage: 8:489/497 of query aligns to 91:578/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K188), S310 (= S220), G311 (= G221), G315 (= G225), G331 (= G241), S332 (= S242), V335 (= V245)
- binding 4'-phosphopantetheine: K201 (= K114), F382 (≠ G291), N387 (≠ K296), C388 (= C297), N545 (≠ T454)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
35% identity, 97% coverage: 8:489/497 of query aligns to 6:493/498 of 4go2A
- active site: N170 (= N165), K193 (= K188), E269 (= E263), C303 (= C297), E400 (= E396), D479 (≠ E475)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (≠ S162), P168 (= P163), W169 (= W164), K193 (= K188), A195 (= A190), Q196 (≠ N191), S225 (= S220), G226 (= G221), G230 (= G225), Q231 (= Q226), F244 (= F239), G246 (= G241), S247 (= S242), V250 (= V245), I254 (= I249), E269 (= E263), G271 (= G265), C303 (= C297), E400 (= E396), F402 (= F398)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
35% identity, 97% coverage: 8:489/497 of query aligns to 6:493/498 of 2o2rA
- active site: N170 (= N165), K193 (= K188), E269 (= E263), C303 (= C297), E400 (= E396), D479 (≠ E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (≠ S162), W169 (= W164), K193 (= K188), A195 (= A190), Q196 (≠ N191), S225 (= S220), G226 (= G221), G230 (= G225), Q231 (= Q226), F244 (= F239), S247 (= S242), V250 (= V245), I254 (= I249)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
35% identity, 97% coverage: 8:489/497 of query aligns to 410:897/902 of P28037
- IPW 571:573 (≠ SPW 162:164) binding
- KPAQ 597:600 (≠ KPAN 188:191) binding
- GSLVGQ 630:635 (≠ GRSIGQ 221:226) binding
- GS 650:651 (= GS 241:242) binding
- E673 (= E263) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (≠ EM 263:264) binding
- C707 (= C297) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ E347) binding
- ESF 804:806 (≠ EMF 396:398) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
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)
34% identity, 95% coverage: 23:496/497 of query aligns to 11:493/503 of Q8VWZ1
- N27 (= N37) binding
- I28 (≠ R38) binding
- D99 (≠ E105) binding
- L189 (≠ I192) binding
- 238:245 (vs. 241:248, 38% identical) binding
- C294 (= C297) binding
- E393 (= E396) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
34% identity, 95% coverage: 23:496/497 of query aligns to 6:488/497 of 3iwkH
- active site: N157 (= N165), K180 (= K188), E255 (= E263), C289 (= C297), E388 (= E396), E465 (= E475)
- binding nicotinamide-adenine-dinucleotide: W156 (= W164), G213 (= G221), G217 (= G225), A218 (≠ Q226), G233 (= G241), S234 (= S242), T237 (≠ V245), K240 (≠ G248), C289 (= C297), Q336 (= Q344), E388 (= E396), F390 (= F398)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
34% identity, 97% coverage: 8:489/497 of query aligns to 6:493/498 of 7yjjC
O75891 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; EC 1.5.1.6 from Homo sapiens (Human) (see 2 papers)
34% identity, 97% coverage: 8:489/497 of query aligns to 410:897/902 of O75891
- A511 (≠ E106) to V: in a colorectal cancer sample; somatic mutation; dbSNP:rs768309358
Sites not aligning to the query:
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity.
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
33% identity, 95% coverage: 24:497/497 of query aligns to 10:490/496 of 4i9bA
- active site: N157 (= N165), K180 (= K188), E255 (= E263), C290 (= C297), E389 (= E396), D466 (≠ E475)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C297), W455 (≠ F463)
- binding nicotinamide-adenine-dinucleotide: I153 (= I161), T154 (≠ S162), W156 (= W164), K180 (= K188), S182 (≠ A190), E183 (≠ N191), G213 (= G221), G217 (= G225), G218 (≠ Q226), F231 (= F239), S234 (= S242), T237 (≠ V245), I241 (= I249)
Q56R04 Aminoaldehyde dehydrogenase 1; SlAMADH1; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Betaine aldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Solanum lycopersicum (Tomato) (Lycopersicon esculentum) (see paper)
33% identity, 95% coverage: 24:497/497 of query aligns to 15:495/504 of Q56R04
- I31 (vs. gap) binding
- D99 (≠ E105) binding
- TPW 159:161 (≠ SPW 162:164) binding
- KPSE 185:188 (≠ KPAN 188:191) binding
- L189 (≠ I192) binding
- GSGPT 238:242 (≠ GSVPV 241:245) binding
- E260 (= E263) active site, Proton acceptor
- L261 (≠ M264) binding
- C295 (= C297) active site, Nucleophile
- E394 (= E396) binding
- W460 (≠ F463) binding
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
34% identity, 96% coverage: 22:496/497 of query aligns to 29:507/515 of 2d4eC
- active site: N173 (= N165), K196 (= K188), E271 (= E263), C305 (= C297), E409 (= E396), E486 (= E475)
- binding nicotinamide-adenine-dinucleotide: I169 (= I161), T170 (≠ S162), P171 (= P163), W172 (= W164), K196 (= K188), A198 (= A190), G229 (= G221), G233 (= G225), A234 (≠ Q226), T248 (= T240), G249 (= G241), E250 (≠ S242), T253 (≠ V245), E271 (= E263), L272 (≠ M264), C305 (= C297), E409 (= E396), F411 (= F398), F475 (= F463)
Query Sequence
>GFF3742 PGA1_262p01460 aldehyde dehydrogenase
MSIPMETEFCVRPLTMTDIQKNLIAGEWLAGESEVENRNPSDLSDLVGIFAQASADQLEA
TLDQAQVAQREWAAYGLERKQAVLNAIGNEMMARAEELGTLLSREEGKPLAEGKGEVYRA
GQFFTYYAAECLRQIGENADSVRPDIEVDVRREAVGTVAIISPWNFPTATASWKIAPALC
YGNAVVWKPANITPASAVALAEIIERQDIPKGLFSLVMGSGRSIGQRLVESPKVNAISFT
GSVPVGKGIASAAIQNLTKVQMEMGSKNALAVMDDADLDLAVTLALGGAFGGTGQKCTAS
SRLVVHAGIHDAFVEKLVTGAKAMKVGHALEAGVQMGPVVSEQQLNENLAYVDLGKTEGA
ELACGGQRLEMPHQGFYMSPGVFLNTTNDMRINREEMFAPLTSVIKVGSYDEALSVVNDT
NFGLTSGIVTQSLARATHFRRNARTGVVTVNLPTAGTDYHVPFGGRGDSSYGPREQGKAA
AEFYTTVKTAYISAGPV
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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