SitesBLAST
Comparing PfGW456L13_3316 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3316 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: 24:522/526 of query aligns to 7:504/504 of 1eyyA
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
29% identity, 86% coverage: 4:455/526 of query aligns to 1:437/486 of 3ju8A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E377 (= E391)
- 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), E377 (= E391), F379 (= F393)
Sites not aligning to the query:
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
27% identity, 81% coverage: 3:429/526 of query aligns to 3:418/454 of 3ty7B
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)
27% identity, 84% coverage: 7:450/526 of query aligns to 6:432/475 of Q59931
- R103 (= R106) binding
- S151 (≠ G157) binding
- K177 (= K185) binding
- T180 (≠ S188) binding
- D215 (≠ E225) binding
- 230:251 (vs. 240:265, 31% identical) binding
- E377 (= E391) binding
Sites not aligning to the query:
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
29% identity, 79% coverage: 9:426/526 of query aligns to 9:420/489 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 (= G221), 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:
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 84% coverage: 7:450/526 of query aligns to 5:431/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ E264), C283 (= C301), E376 (= E391)
- 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), K328 (≠ T339), S329 (≠ L340), Y332 (= Y343)
Sites not aligning to the query:
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)
25% identity, 80% coverage: 4:423/526 of query aligns to 8:423/487 of Q9H2A2
- R109 (≠ K116) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N160) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 84% coverage: 7:450/526 of query aligns to 5:431/474 of 1qi1B
- active site: N153 (= N160), K176 (= K185), E249 (= E264), S283 (≠ C301), E376 (= E391)
- 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:
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 77% coverage: 8:413/526 of query aligns to 5:409/483 of 4npiA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), W160 (≠ G170), E251 (= E264), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), K175 (= K185), E178 (≠ S188), G208 (= G222), G213 (= G224), E214 (= E225), F227 (= F238), G229 (= G240), E230 (≠ S241), T233 (≠ G244), G253 (≠ S266), C285 (= C301), K335 (= K349), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 77% coverage: 8:413/526 of query aligns to 5:409/483 of 4i2rA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), E251 (= E264), L252 (≠ M265), G253 (≠ S266), C285 (= C301), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 77% coverage: 8:413/526 of query aligns to 5:409/483 of 4i25A
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G213 (= G224), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), E251 (= E264), L252 (≠ M265), C285 (= C301), E387 (= E391), F389 (= F393)
Sites not aligning to the query:
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
26% identity, 77% coverage: 8:413/526 of query aligns to 5:409/483 of 5kllA
- active site: D152 (≠ N160), K175 (= K185), E251 (= E264), C285 (= C301), E387 (= E391)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R106), D152 (≠ N160), L157 (≠ F165), W160 (≠ G170), C285 (= C301)
Sites not aligning to the query:
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
26% identity, 77% coverage: 8:413/526 of query aligns to 6:410/484 of 5kj5B
- active site: D153 (≠ N160), K176 (= K185), E252 (= E264), C286 (= C301), E388 (= E391)
- binding nicotinamide-adenine-dinucleotide: I149 (≠ F156), S150 (≠ G157), P151 (≠ A158), W152 (≠ S159), D153 (≠ N160), L158 (≠ F165), K176 (= K185), G209 (= G222), K210 (vs. gap), G214 (= G224), F228 (= F238), T229 (= T239), G230 (= G240), E231 (≠ S241), T234 (≠ G244), E252 (= E264), L253 (≠ M265), C286 (= C301), E388 (= E391), F390 (= F393)
Sites not aligning to the query:
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
27% identity, 77% coverage: 8:413/526 of query aligns to 5:409/483 of 4ou2A
- active site: N152 (= N160), K175 (= K185), A251 (= A263), C285 (= C301), E387 (= E391)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), C285 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), G208 (= G222), G213 (= G224), E214 (= E225), F227 (= F238), T228 (= T239), G229 (= G240), E230 (≠ S241), T233 (≠ G244), A251 (= A263), L252 (≠ M265), G253 (≠ S266), C285 (= C301), E387 (= E391), F389 (= F393)
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)
26% identity, 80% coverage: 8:429/526 of query aligns to 13:424/484 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 (≠ K207) 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.
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
30% identity, 52% coverage: 3:273/526 of query aligns to 1:255/488 of 5u0mA
- active site: N148 (= N160), K171 (= K185), E246 (= E264)
- binding nicotinamide-adenine-dinucleotide: F144 (= F156), Y147 (≠ S159), N148 (= N160), K171 (= K185), S173 (≠ H187), E174 (≠ S188), G207 (= G224), T222 (= T239), G223 (= G240), S224 (= S241), V227 (≠ G244), E246 (= E264), M247 (= M265), G248 (≠ S266)
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)
30% identity, 52% coverage: 3:273/526 of query aligns to 1:255/488 of 5u0lA
Sites not aligning to the query:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
27% identity, 80% coverage: 3:423/526 of query aligns to 1:420/485 of 4u3wA
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
29% identity, 56% coverage: 160:455/526 of query aligns to 147:438/476 of 4yweA
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)
26% identity, 75% coverage: 9:404/526 of query aligns to 21:413/498 of 4go2A
- active site: N170 (= N160), K193 (= K185), E269 (= E264), C303 (= C301), E400 (= E391)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (vs. gap), I167 (vs. gap), P168 (vs. gap), W169 (≠ S159), K193 (= K185), A195 (≠ H187), Q196 (≠ S188), S225 (≠ G221), G226 (= G222), G230 (= G224), Q231 (≠ E225), F244 (= F238), G246 (= G240), S247 (= S241), V250 (≠ G244), I254 (≠ L248), E269 (= E264), G271 (≠ S266), C303 (= C301), E400 (= E391), F402 (= F393)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_3316 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3316
MTRILGHNYIGGQRSAAGSIKLQSVDATTGEALPHAFYQATVQEVDAAAGAAAAAYPANR
SLSAERRAQFLEAIADELDALGDDFVAVVCRETALPAGRIQGERGRTSGQMRLFAKVLRR
GDFYGARIDRALPERQPLPRPDLRQYRIGLGPVAVFGASNFPLAFSTAGGDTASALAAGC
PVVFKAHSGHMATAEWVADAIIRAAEKTGMPAGVFNMIYGGGVGEALVKHPAIQAVGFTG
SLKGGRALCDMAAARAQPIPVFAEMSSINPVIVLPEALQARADTVARDLTASVVQGCGQF
CTNPGLVIGIRSAPFSAFVQQVAGLMGDQPAQTMLNAGTLSSYGQGLQKLLAHPGIEHLA
GNPQQGNQAQPQLFKADVSLLLDGDEVLQEEVFGPTTVVVEVADHAQLMAALNGLHGQLT
ATVIGEPEDFEQFAGLTALLEQKVGRILLNGYPTGVEVCDSMVHGGPYPATSDARGTSVG
TLAIDRFLRPVCFQNYPDSLLPDALKNGNPLRIQRLVDGQSSREAL
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