SitesBLAST
Comparing AO353_14870 FitnessBrowser__pseudo3_N2E3:AO353_14870 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, 95% coverage: 19:519/529 of query aligns to 2:501/504 of 1eyyA
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 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
24% identity, 86% coverage: 34:487/529 of query aligns to 33:473/484 of Q8NMB0
- N157 (= N160) 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 (= K185) 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 (≠ R207) 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 (= E264) 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 (= C301) 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.
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
25% identity, 72% coverage: 41:423/529 of query aligns to 24:392/456 of 3rhdA
- active site: N133 (= N160), H156 (≠ K185), E233 (= E264), C267 (= C301), E360 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (≠ S159), T130 (vs. gap), F132 (vs. gap), H156 (≠ K185), S158 (≠ H187), S159 (= S188), K160 (≠ G189), G193 (= G222), E194 (vs. gap), G197 (= G224), D198 (≠ E225), F211 (= F238), S214 (= S241), V217 (≠ G244)
Sites not aligning to the query:
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
28% identity, 69% coverage: 41:407/529 of query aligns to 39:394/480 of 3rhhD
- active site: N155 (= N160), K178 (= K185), E251 (= E264), C285 (= C301), E378 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ F156), P153 (≠ A158), F154 (≠ S159), K178 (= K185), P179 (vs. gap), A180 (= A186), T181 (≠ H187), G211 (= G222), G215 (= G224), D216 (≠ E225), F229 (= F238), G231 (= G240), G232 (≠ S241), T235 (≠ G244)
Sites not aligning to the query:
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)
28% identity, 55% coverage: 41:329/529 of query aligns to 38:307/475 of Q59931
- R103 (= R106) binding substrate
- S151 (≠ G157) binding NADP(+)
- K177 (= K185) binding NADP(+)
- T180 (≠ S188) binding NADP(+)
- D215 (≠ E225) binding NADP(+)
- 230:251 (vs. 240:265, 31% identical) binding NADP(+)
Sites not aligning to the query:
- 377 binding NADP(+)
- 437 binding substrate
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
29% identity, 55% coverage: 41:329/529 of query aligns to 37:306/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ P260), C283 (= C301)
- binding glyceraldehyde-3-phosphate: R102 (= R106), Y154 (≠ F161), R282 (≠ F300), C283 (= C301), T284 (= T302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ S159), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), D214 (≠ E225), F227 (= F238), S230 (= S241), I233 (≠ G244)
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)
23% identity, 66% coverage: 59:407/529 of query aligns to 66:409/503 of Q84LK3
- N162 (= N160) 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 (≠ G170) 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).
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
24% identity, 69% coverage: 38:404/529 of query aligns to 38:393/454 of 3ty7B
Sites not aligning to the query:
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
28% identity, 55% coverage: 41:329/529 of query aligns to 37:306/474 of 1qi1B
- active site: N153 (= N160), K176 (= K185), E249 (= E264), S283 (≠ C301)
- binding sn-glycerol-3-phosphate: Y154 (≠ F161), R282 (≠ F300), S283 (≠ C301), T284 (= T302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (≠ A158), F152 (≠ S159), N153 (= N160), L158 (≠ T167), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), G229 (= G240), S230 (= S241), I233 (≠ G244), E249 (= E264), L250 (≠ M265), S283 (≠ C301)
Sites not aligning to the query:
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
26% identity, 74% coverage: 16:407/529 of query aligns to 17:401/489 of 6wsbA
- active site: N152 (= N160), E250 (= E264), C284 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), G149 (= G157), A150 (= A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G211 (= G224), A212 (≠ E225), F225 (= F238), T226 (= T239), G227 (= G240), G228 (≠ S241), T231 (≠ G244), V235 (≠ L248), E250 (= E264), L251 (≠ M265), G252 (≠ S266), C284 (= C301), E385 (= E391), F387 (= F393)
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
27% identity, 57% coverage: 4:302/529 of query aligns to 1:280/486 of 3ju8A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301)
- binding nicotinamide-adenine-dinucleotide: G144 (= G157), Y146 (≠ S159), N147 (= N160), L152 (≠ F165), K170 (= K185), S172 (≠ H187), F220 (= F238), T221 (= T239), G222 (= G240), S223 (= S241), T226 (≠ G244), E245 (= E264), M246 (= M265), G247 (≠ S266), C279 (= C301)
Sites not aligning to the query:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 41% coverage: 36:253/529 of query aligns to 32:243/485 of 4u3wA
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
27% identity, 73% coverage: 10:395/529 of query aligns to 511:882/983 of 3hazA