SitesBLAST
Comparing 3609053 FitnessBrowser__Dino:3609053 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
47% identity, 93% coverage: 34:498/501 of query aligns to 20:484/504 of 1eyyA
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
28% identity, 85% coverage: 6:432/501 of query aligns to 5:427/454 of 3ty7B
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
28% identity, 83% coverage: 10:423/501 of query aligns to 13:421/481 of 3jz4A
- active site: N156 (= N157), K179 (= K182), E254 (= E263), C288 (= C300), E385 (= E387)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A155), W155 (≠ S156), K179 (= K182), A181 (≠ H184), S182 (= S185), A212 (≠ K219), G216 (= G223), G232 (= G239), S233 (= S240), I236 (≠ G243), C288 (= C300), K338 (≠ R346), E385 (= E387), F387 (= F389)
Sites not aligning to the query:
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)
28% identity, 83% coverage: 10:423/501 of query aligns to 14:422/482 of P25526
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
28% identity, 59% coverage: 10:304/501 of query aligns to 106:392/583 of 7rluA
Sites not aligning to the query:
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
28% identity, 59% coverage: 10:304/501 of query aligns to 21:307/498 of 4go2A
- active site: N170 (= N157), K193 (= K182), E269 (= E263), C303 (= C300)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ F153), I167 (≠ G154), P168 (≠ A155), W169 (≠ S156), K193 (= K182), A195 (≠ H184), Q196 (≠ S185), S225 (≠ G218), G226 (≠ K219), G230 (= G223), Q231 (≠ T224), F244 (= F237), G246 (= G239), S247 (= S240), V250 (≠ G243), I254 (≠ L247), E269 (= E263), G271 (= G265), C303 (= C300)
Sites not aligning to the query:
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
28% identity, 59% coverage: 10:304/501 of query aligns to 21:307/498 of 2o2rA
- active site: N170 (= N157), K193 (= K182), E269 (= E263), C303 (= C300)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ F153), I167 (≠ G154), W169 (≠ S156), K193 (= K182), A195 (≠ H184), Q196 (≠ S185), S225 (≠ G218), G226 (≠ K219), G230 (= G223), Q231 (≠ T224), F244 (= F237), S247 (= S240), V250 (≠ G243), I254 (≠ L247)
Sites not aligning to the query:
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)
28% identity, 59% coverage: 10:304/501 of query aligns to 425:711/902 of P28037
- IPW 571:573 (≠ GAS 154:156) binding
- KPAQ 597:600 (≠ KGHS 182:185) binding
- GSLVGQ 630:635 (≠ KRDVGT 219:224) binding
- GS 650:651 (= GS 239:240) binding
- E673 (= E263) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 263:264) binding
- C707 (= C300) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
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.
- 757 binding
- 804:806 binding
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
29% identity, 80% coverage: 8:406/501 of query aligns to 5:407/485 of 4u3wA
Sites not aligning to the query:
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
27% identity, 83% coverage: 8:425/501 of query aligns to 12:424/484 of Q8NMB0
- N157 (= N157) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K182) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (≠ R204) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E263) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C300) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
28% identity, 59% coverage: 8:302/501 of query aligns to 7:287/489 of 4cazA
- active site: N152 (= N157), K175 (= K182), E251 (= E263), C285 (= C300)
- 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 (≠ F153), G149 (= G154), W151 (≠ S156), N152 (= N157), K175 (= K182), E178 (≠ S185), G208 (≠ K219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (≠ G243), V236 (≠ L247), E251 (= E263), L252 (= L264), C285 (= C300)
Sites not aligning to the query:
- active site: 386, 463
- 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: 386, 388
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
28% identity, 59% coverage: 8:302/501 of query aligns to 7:287/489 of 2woxA
- active site: N152 (= N157), K175 (= K182), E251 (= E263), C285 (= C300)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F153), G149 (= G154), W151 (≠ S156), N152 (= N157), K175 (= K182), S177 (≠ H184), E178 (≠ S185), G208 (≠ K219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (≠ G243), V236 (≠ L247), E251 (= E263), L252 (= L264), C285 (= C300)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
28% identity, 59% coverage: 8:302/501 of query aligns to 7:287/489 of 2wmeA
- active site: N152 (= N157), K175 (= K182), E251 (= E263), C285 (= C300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G154), W151 (≠ S156), K175 (= K182), S177 (≠ H184), E178 (≠ S185), G208 (≠ K219), G212 (= G223), F226 (= F237), G228 (= G239), G229 (≠ S240), T232 (≠ G243), V236 (≠ L247)
Sites not aligning to the query:
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)
27% identity, 60% coverage: 1:302/501 of query aligns to 1:288/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 154:157) binding
- K162 (≠ D168) active site, Charge relay system
- KPSE 176:179 (≠ KGHS 182:185) binding
- G209 (≠ K219) binding
- GTST 230:233 (≠ SLAG 240:243) binding
- E252 (= E263) active site, Proton acceptor
- C286 (= C300) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
28% identity, 55% coverage: 26:301/501 of query aligns to 28:297/505 of O24174
- N164 (= N157) 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 (≠ G167) 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.
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
30% identity, 54% coverage: 9:280/501 of query aligns to 29:288/515 of 2d4eC
- active site: N173 (= N157), K196 (= K182), E271 (= E263)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F153), T170 (≠ G154), P171 (≠ A155), W172 (≠ S156), K196 (= K182), A198 (≠ H184), G229 (≠ K219), G233 (= G223), A234 (≠ T224), T248 (= T238), G249 (= G239), E250 (≠ S240), T253 (≠ G243), E271 (= E263), L272 (= L264)
Sites not aligning to the query:
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
28% identity, 48% coverage: 62:301/501 of query aligns to 72:295/503 of Q84LK3
- N162 (= N157) 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 (≠ G167) 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).
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
25% identity, 84% coverage: 3:423/501 of query aligns to 1:413/475 of Q59931
- R103 (= R103) binding
- S151 (≠ G154) binding
- K177 (= K182) binding
- T180 (≠ G189) binding
- D215 (≠ T224) binding
- 230:251 (vs. 239:264, 27% identical) binding
- E377 (= E387) binding
Sites not aligning to the query:
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
30% identity, 51% coverage: 50:303/501 of query aligns to 52:286/476 of 5x5uA
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
30% identity, 51% coverage: 50:303/501 of query aligns to 52:286/476 of 5x5tA
Sites not aligning to the query:
Query Sequence
>3609053 FitnessBrowser__Dino:3609053
MSFTPHGKHLIAGAWVGSDQTFASDPAHGPAHEFSVGTPALVDQACAAAEDAFASYGYSD
AATRAAFLNAIADEIDARAQIITGIGTQETGLPEARLQGERGRTTGQLRLFAEHILKGDC
LDRRHDPALPDRAPLPRPDLKLVQRPIGPVAVFGASNFPLAFSVAGGDTAAALAAGCPVV
VKGHSAHPGTGEIVAEAIHAAIARTGMPAGVFSLIQGGKRDVGTALVQHPLIRAVGFTGS
LAGGRALFDLCAARPEPIPFFGELGSVNPMFLLPEAIAARGAEIGAGWAGSLAMGAGQFC
TNPGIAVVLPGADAFVAAAEAALRETAAQTMLTEGIAAAYRDGVARLAAHPQTSELLGAP
CDGREAHPCLYRVAARDWLADHTLQEEVFGPLGLVVEAQDAAEMARIARSLQGQLTCTLH
MEDGDTDHARSLVPLLERKAGRMLVNGFPTGVEVADSMVHGGPYPASTNFGATSVGTLSI
RRFLRPVCYQNMPDALLPADY
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