SitesBLAST
Comparing PP_2585 FitnessBrowser__Putida:PP_2585 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)
47% identity, 95% coverage: 19:519/526 of query aligns to 2:501/504 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)
25% identity, 77% coverage: 22:425/526 of query aligns to 25:425/487 of Q9H2A2
- R109 (= R112) 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.
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
27% identity, 71% coverage: 44:414/526 of query aligns to 44:406/454 of 3ty7B
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
29% identity, 86% coverage: 8:459/526 of query aligns to 5:441/486 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:
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, 76% coverage: 10:410/526 of query aligns to 15:405/484 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 (≠ G207) 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.
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
29% identity, 58% coverage: 22:327/526 of query aligns to 23:309/489 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)
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)
26% identity, 72% coverage: 43:423/526 of query aligns to 40:409/475 of Q59931
- R103 (≠ I100) 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:
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
24% identity, 78% coverage: 1:410/526 of query aligns to 3:400/490 of 5ekcE
- active site: N154 (= N160), K177 (= K185), E252 (= E264), C286 (= C301), E381 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ F156), T151 (≠ G157), P152 (≠ A158), W153 (≠ S159), K177 (= K185), S180 (= S188), G210 (= G222), G214 (= G224), F228 (= F238), G230 (= G240), E231 (≠ S241), T234 (≠ G244), N331 (≠ R341), R333 (≠ Y343), Q334 (= Q344)
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)
30% identity, 48% coverage: 25:277/526 of query aligns to 20:268/482 of P25526
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
30% identity, 48% coverage: 25:277/526 of query aligns to 19:267/481 of 3jz4A
- active site: N156 (= N160), K179 (= K185), E254 (= E264)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A158), W155 (≠ S159), K179 (= K185), A181 (≠ H187), S182 (= S188), A212 (vs. gap), G216 (= G224), G232 (= G240), S233 (= S241), I236 (≠ G244)
Sites not aligning to the query:
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
24% identity, 77% coverage: 8:410/526 of query aligns to 3:393/482 of 5ek6A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E374 (= E391)
- binding 2-methylpropanal: I152 (≠ F165), K155 (≠ A168), T222 (= T239), E245 (= E264)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F156), T144 (≠ G157), W146 (≠ S159), N147 (= N160), I152 (≠ F165), K170 (= K185), A172 (≠ H187), S173 (= S188), P202 (≠ A221), G203 (= G222), G207 (= G224), F221 (= F238), T222 (= T239), G223 (= G240), E224 (≠ S241), T227 (≠ G244), I231 (≠ L248), E245 (= E264), L246 (≠ M265), C279 (= C301), E374 (= E391)
Sites not aligning to the query:
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
24% identity, 77% coverage: 8:410/526 of query aligns to 3:393/482 of 4h73A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301), E374 (= E391)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F156), T144 (≠ G157), P145 (≠ A158), W146 (≠ S159), K170 (= K185), A172 (≠ H187), S173 (= S188), G203 (= G222), G207 (= G224), F221 (= F238), G223 (= G240), E224 (≠ S241), T227 (≠ G244)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
24% identity, 85% coverage: 39:487/526 of query aligns to 50:480/491 of 5gtlA
- active site: N165 (= N160), K188 (= K185), E263 (= E264), C297 (= C301), E394 (= E391), E471 (≠ S478)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (vs. gap), P163 (vs. gap), K188 (= K185), A190 (≠ H187), E191 (≠ S188), Q192 (≠ G189), G221 (= G222), G225 (= G224), G241 (= G240), S242 (= S241), T245 (≠ G244), L264 (≠ M265), C297 (= C301), E394 (= E391), F396 (= F393)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
24% identity, 85% coverage: 39:487/526 of query aligns to 50:480/491 of 5gtkA
- active site: N165 (= N160), K188 (= K185), E263 (= E264), C297 (= C301), E394 (= E391), E471 (≠ S478)
- binding nicotinamide-adenine-dinucleotide: I161 (vs. gap), I162 (vs. gap), P163 (vs. gap), W164 (≠ S159), K188 (= K185), E191 (≠ S188), G221 (= G222), G225 (= G224), A226 (≠ E225), F239 (= F238), G241 (= G240), S242 (= S241), T245 (≠ G244), Y248 (≠ A247), L264 (≠ M265), C297 (= C301), Q344 (vs. gap), R347 (vs. gap), E394 (= E391), F396 (= F393)
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
33% identity, 40% coverage: 45:253/526 of query aligns to 41:243/485 of 4u3wA
Sites not aligning to the query:
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 72% coverage: 43:423/526 of query aligns to 39:408/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ E264), C283 (= C301), E376 (= E391)
- binding glyceraldehyde-3-phosphate: R102 (≠ I100), 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:
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 72% coverage: 43:423/526 of query aligns to 39:408/474 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:
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
25% identity, 65% coverage: 67:410/526 of query aligns to 74:412/503 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).
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
27% identity, 70% coverage: 114:483/526 of query aligns to 580:945/979 of 4nmdA
Sites not aligning to the query:
- binding dihydroflavine-adenine dinucleotide: 226, 227, 256, 258, 285, 287, 288, 289, 290, 292, 309, 310, 311, 312, 315, 338, 339, 340, 341, 365, 366, 367, 388, 414
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
27% identity, 70% coverage: 114:483/526 of query aligns to 580:945/979 of 4nmfB
Sites not aligning to the query:
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: 184, 290, 387, 399, 402, 403
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: 184, 366, 399, 402
- binding N-propargylglycine-modified flavin adenine dinucleotide: 184, 225, 226, 255, 257, 284, 286, 287, 288, 289, 291, 308, 309, 310, 311, 314, 337, 338, 339, 340, 364, 366, 387, 406, 411, 412, 413
Query Sequence
>PP_2585 FitnessBrowser__Putida:PP_2585
MSIEHRLNHIAGQLSGHGDVLLHSLDAHTGETLPYAFHQATGDEVEAAAQAAEVAYPSYR
STRPDQRAAFLDAIASELDALGDDFIQDVMRETALPEARIRGERSRTSNQLRLFAEVVRR
GDFYAARIDRALPQRTPLPRPDLRQYRIGVGPVAVFGASNFPLAFSTAGGDTASALAAGC
PVVFKAHSGHMLTAAHVAAAIDRAVTGSGMPAGVFNMIYGAGVGEALVKHPAIQAVGFTG
SLRGGRALCDMAAARPQPIPVFAEMSSINPVVVLPQALQARGEQVATELAASVVLGCGQF
CTNPGLVVGIRSPHFEHFLQTLVARMADQGPQTMLNAGTLRSYQNAVQHLLAHPGIQHLA
GQPQTGNQAQPQLFKADVSLLLNGDPLLQEEVFGPCTVVVEVADAQQLAEALRHLQGQLT
ATLIAEPDDLRTFASLVPLLERKAGRLLLNGYPTGVEVSDAMVHGGPYPATSDARGTSVG
TLAIDRFLRPVCFQNYPDALLPDALKNANPLGIARLLEGVSSREAV
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