SitesBLAST
Comparing AO353_14870 FitnessBrowser__pseudo3_N2E3:AO353_14870 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)
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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (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
- S151 (≠ G157) binding
- K177 (= K185) binding
- T180 (≠ S188) binding
- D215 (≠ E225) binding
- 230:251 (vs. 240:265, 31% identical) binding
Sites not aligning to the query:
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
- active site: N652 (= N160), K675 (= K185), E752 (= E264), C786 (= C301), E878 (= E391)
- binding nicotinamide-adenine-dinucleotide: I648 (≠ F156), S649 (≠ G157), P650 (≠ A158), W651 (≠ S159), N652 (= N160), I657 (≠ F165), K675 (= K185), P676 (≠ A186), A677 (≠ H187), G708 (= G222), G711 (= G224), A712 (≠ E225), T726 (= T239), G727 (= G240), S728 (= S241), V731 (≠ G244), I735 (≠ L248), E752 (= E264), T753 (≠ M265), C786 (= C301), E878 (= E391), F880 (= F393)
Sites not aligning to the query:
- active site: 960
- binding flavin-adenine dinucleotide: 272, 273, 306, 333, 335, 336, 337, 338, 339, 340, 358, 359, 360, 361, 364, 387, 388, 389, 390, 435, 460, 461
- binding nicotinamide-adenine-dinucleotide: 948
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
26% identity, 71% coverage: 44:417/529 of query aligns to 42:410/489 of 4o6rA
- active site: N150 (= N160), K173 (= K185), E248 (≠ F262), C282 (= C301), E383 (= E391)
- binding adenosine monophosphate: I146 (vs. gap), V147 (vs. gap), K173 (= K185), G206 (= G220), G210 (= G224), Q211 (≠ E225), F224 (= F238), G226 (= G240), S227 (= S241), T230 (≠ G244), R233 (≠ A247)
Sites not aligning to the query:
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
29% identity, 38% coverage: 54:253/529 of query aligns to 520:707/959 of 5ur2B
Sites not aligning to the query:
- active site: 722, 756, 851, 931
- binding N-propargylglycine-modified flavin adenine dinucleotide: 174, 215, 216, 249, 278, 279, 280, 281, 283, 300, 301, 302, 303, 306, 329, 330, 331, 332, 356, 357, 358, 379, 398, 403, 405
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
26% identity, 49% coverage: 150:408/529 of query aligns to 146:407/493 of 6vr6D
- active site: N156 (= N160), E253 (= E264), C287 (= C301)
- binding nicotinamide-adenine-dinucleotide: I152 (≠ F156), G153 (= G157), W155 (≠ S159), K179 (= K185), A212 (= A221), G215 (= G224), Q216 (≠ E225), F229 (= F238), G231 (= G240), S232 (= S241), T235 (≠ G244), I239 (≠ L248)
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
26% identity, 56% coverage: 160:455/529 of query aligns to 147:438/476 of 4yweA
Sites not aligning to the query:
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
26% identity, 63% coverage: 151:483/529 of query aligns to 623:946/981 of 7na0A
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 226, 227, 256, 258, 285, 287, 288, 289, 290, 291, 292, 309, 310, 311, 312, 315, 338, 339, 340, 341, 367, 388, 407, 413, 414
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
26% identity, 63% coverage: 151:483/529 of query aligns to 620:943/977 of 4nmaA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 226, 227, 258, 285, 287, 288, 289, 290, 291, 292, 309, 310, 311, 312, 315, 338, 339, 340, 341, 365, 367, 407, 413, 414
- binding tetrahydrofuran-2-carboxylic acid: 185, 388, 400, 403, 404
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
26% identity, 63% coverage: 151:483/529 of query aligns to 615:938/972 of 4nmeA
Sites not aligning to the query:
- binding N-propargylglycine-modified flavin adenine dinucleotide: 183, 224, 225, 254, 256, 283, 285, 286, 287, 288, 290, 307, 308, 309, 310, 313, 336, 337, 338, 339, 363, 365, 383, 402, 409
Query Sequence
>AO353_14870 FitnessBrowser__pseudo3_N2E3:AO353_14870
MSAIIGHNFIGFGRSAAGDHVLHSVDAHSGEPLPYDFSQASAEEIDNAAHFAATAYPIYR
NLPATVRAGFLETIAEEIDALGDDFIAIVCRETALPAARIQGERARTSGQLRLFARVLRQ
GDFLGARIDRALPERQPFPRPDVRQWRIGLGPVAVFGASNFPLAFSTAGGDTAAALAAGC
PVVFKAHSGHMATAELVAAAIIRAAQRSGMPEGVFNMIYGAGVGEALVKHPAIQAVGFTG
SLKGGRALCDMAAARPQPIPVFAEMSSINPVLLLPAALAARSASIASELSASIVLGGGQF
CTNPGLIIGLRSAAFSAFIEQLTAQINEKPPQTLLNSGTRRSYESGVQRLLEHPRVTRLS
GNLVPGNQVQPQLFKADVSLLLEGDEVLQEEVFGPASIVLEVADERELRLALCALHGQLT
ATLIAEPQDLVLCAQLIPILEQKAGRLLLNGYPTGVEVCDAMVHGGPYPATSDARGTSVG
SLAIERFLRPVCYQNCPDRLLPDALKNANPLGILRLVDGVNTREGWGDE
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