SitesBLAST
Comparing BPHYT_RS28455 FitnessBrowser__BFirm:BPHYT_RS28455 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
46% identity, 94% coverage: 20:521/533 of query aligns to 2:502/504 of 1eyyA
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)
26% identity, 81% coverage: 2:435/533 of query aligns to 5:433/487 of Q9H2A2
- R109 (≠ K117) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N161) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
25% identity, 80% coverage: 64:489/533 of query aligns to 70:480/503 of Q84LK3
- N162 (= N161) 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 (≠ G171) 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).
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
30% identity, 84% coverage: 9:456/533 of query aligns to 5:437/486 of 3ju8A
- active site: N147 (= N161), K170 (= K186), E245 (= E265), C279 (= C302), E377 (= E392)
- binding nicotinamide-adenine-dinucleotide: G144 (= G158), Y146 (≠ S160), N147 (= N161), L152 (≠ V168), K170 (= K186), S172 (≠ H188), F220 (= F239), T221 (= T240), G222 (= G241), S223 (= S242), T226 (≠ G245), E245 (= E265), M246 (= M266), G247 (≠ S267), C279 (= C302), E377 (= E392), F379 (= F394)
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
27% identity, 56% coverage: 161:456/533 of query aligns to 147:438/476 of 4yweA
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)
29% identity, 56% coverage: 45:340/533 of query aligns to 49:326/482 of P25526
Sites not aligning to the query:
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)
25% identity, 83% coverage: 9:453/533 of query aligns to 13:448/494 of P49189
- C116 (≠ V118) 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)
25% identity, 83% coverage: 9:453/533 of query aligns to 12:447/493 of 6vr6D
- active site: N156 (= N161), E253 (= E265), C287 (= C302)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ F157), G153 (= G158), W155 (≠ S160), K179 (= K186), A212 (≠ E222), G215 (= G225), Q216 (≠ A226), F229 (= F239), G231 (= G241), S232 (= S242), T235 (≠ G245), I239 (≠ L249)
Sites not aligning to the query:
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)
24% identity, 85% coverage: 6:458/533 of query aligns to 14:466/511 of 6fkuA
- active site: N159 (= N161), E261 (= E265), C295 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (≠ F157), T156 (≠ G158), N159 (= N161), K182 (= K186), S184 (≠ H188), E185 (≠ S189), G214 (≠ E222), G215 (≠ R223), K216 (≠ V224), G220 (vs. gap), Q221 (vs. gap), F237 (= F239), T238 (= T240), G239 (= G241), S240 (= S242), V243 (≠ G245), E261 (= E265), L262 (≠ M266), C295 (= C302), R342 (≠ G339), F343 (≠ I340), E404 (= E392), F406 (= F394)
Sites not aligning to the query:
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
26% identity, 77% coverage: 45:453/533 of query aligns to 42:440/489 of 4o6rA
- active site: N150 (= N161), K173 (= K186), E248 (≠ F263), C282 (= C302), E383 (= E392)
- binding adenosine monophosphate: I146 (≠ F157), V147 (≠ G158), K173 (= K186), G206 (= G221), G210 (= G225), Q211 (≠ A226), F224 (= F239), G226 (= G241), S227 (= S242), T230 (≠ G245), R233 (≠ A248)
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)
24% identity, 81% coverage: 1:430/533 of query aligns to 1:424/484 of Q8NMB0
- N157 (= N161) 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 (= K186) 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 (≠ R208) 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 (= E265) 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 (= C302) 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.
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
27% identity, 53% coverage: 25:304/533 of query aligns to 22:287/480 of 3rhhD
- active site: N155 (= N161), K178 (= K186), E251 (= E265), C285 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ F157), P153 (≠ A159), F154 (≠ S160), K178 (= K186), P179 (≠ A187), A180 (≠ H188), T181 (≠ S189), G211 (vs. gap), G215 (= G225), D216 (≠ A226), F229 (= F239), G231 (= G241), G232 (≠ S242), T235 (≠ G245)
Sites not aligning to the query:
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
26% identity, 56% coverage: 153:453/533 of query aligns to 145:438/478 of 6tryA
- active site: N156 (= N161), E255 (= E265), C289 (= C302)
- binding nicotinamide-adenine-dinucleotide: I152 (vs. gap), T153 (vs. gap), W155 (≠ S160), K179 (= K186), A181 (≠ H188), E182 (≠ S189), G212 (= G221), G216 (= G225), A217 (= A226), F230 (= F239), G232 (= G241), S233 (= S242), V236 (≠ G245), K335 (≠ E349)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: L160 (≠ A165), C288 (≠ L301)
Sites not aligning to the query:
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
26% identity, 56% coverage: 153:453/533 of query aligns to 146:439/479 of 6te5B
- active site: N157 (= N161), E256 (= E265), C290 (= C302)
- binding nicotinamide-adenine-dinucleotide: I153 (vs. gap), T154 (vs. gap), W156 (≠ S160), K180 (= K186), E183 (≠ S189), G213 (= G221), F231 (= F239), S234 (= S242), V237 (≠ G245), Q337 (≠ R350), K340 (≠ N353)
Sites not aligning to the query:
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
26% identity, 56% coverage: 153:453/533 of query aligns to 144:439/478 of 6tgwA
- active site: N155 (= N161), E254 (= E265), C288 (= C302)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: F156 (= F162), Q278 (≠ E289), F282 (≠ T296)
- binding nicotinamide-adenine-dinucleotide: I151 (vs. gap), T152 (vs. gap), P153 (vs. gap), W154 (≠ S160), K178 (= K186), G211 (= G221), G215 (= G225), F229 (= F239), G231 (= G241), S232 (= S242), V235 (≠ G245)
Sites not aligning to the query:
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
29% identity, 47% coverage: 55:305/533 of query aligns to 53:286/476 of 5x5uA
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
29% identity, 47% coverage: 55:305/533 of query aligns to 53:286/476 of 5x5tA
Sites not aligning to the query:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
25% identity, 78% coverage: 40:453/533 of query aligns to 35:445/485 of 4u3wA
Sites not aligning to the query:
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
26% identity, 77% coverage: 41:451/533 of query aligns to 37:430/488 of 5u0mA
- active site: N148 (= N161), K171 (= K186), E246 (= E265), C280 (= C302), E377 (= E392)
- binding nicotinamide-adenine-dinucleotide: F144 (= F157), Y147 (≠ S160), N148 (= N161), K171 (= K186), S173 (≠ H188), E174 (≠ S189), G207 (= G225), T222 (= T240), G223 (= G241), S224 (= S242), V227 (≠ G245), E246 (= E265), M247 (= M266), G248 (≠ S267), C280 (= C302), E377 (= E392), F379 (= F394)
Sites not aligning to the query:
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
26% identity, 77% coverage: 41:451/533 of query aligns to 37:430/488 of 5u0lA
Sites not aligning to the query:
Query Sequence
>BPHYT_RS28455 FitnessBrowser__BFirm:BPHYT_RS28455
MTATIFGHNYIGGQRSACGDISLHSLSASTSEVYPVAFSQATDAEVDAAVEAAAAAFPLY
RALPSSVRADFLEAIAAEIDALGDDFIADVMRETALPNARIAGERARTSNQMRLFAKVLR
RGDFYGARIDRALPERQPLPRPDLRQYRIGVGPVAVFGASNFPLAFSVAGGDTASALAAG
CPVVVKAHSGHLVTSERMADAIERAIRRTGMPAGTFNMIYGERVGARLVQAPGIQAVGFT
GSLSGGRALCDLAAAREQPIPVFAEMSSVNPVFVLEGALQERGAALANELAASVATGCGQ
LCTSPGLVLGVRSPRFGAFIDSLGKAIERQPPQTMLNTGIFANFRAGLERASNHAGIALS
AAAQGETEQAAAQLFVADAALLFDPGRPLEEEIFGPATVVVELDSAEHLLRFASAMRGQL
TATLLASHGDLRSHRKLIERLEEKAGRLLVNGYPTGVEVSDAIVHGGPWPATSDARGTSV
GTLAIDRFLRPVCYQNYPDELLPDALKNANPLNLMRLVDGEMTQRSLDCAPGR
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