SitesBLAST
Comparing CCNA_02485 FitnessBrowser__Caulo:CCNA_02485 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)
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
51% identity, 100% coverage: 2:470/470 of query aligns to 15:484/484 of 4jz6A
- active site: N150 (= N137), K173 (= K160), E251 (= E238), C285 (= C272), E380 (= E366), F458 (= F444)
- binding salicylaldehyde: W97 (= W84), G151 (≠ A138), V154 (≠ I141), R247 (≠ P234), C248 (≠ V235), I284 (= I271), C285 (= C272), M286 (= M273), Y447 (≠ F433), Y455 (= Y441)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
37% identity, 94% coverage: 28:470/470 of query aligns to 45:485/490 of 5ekcE
- active site: N154 (= N137), K177 (= K160), E252 (= E238), C286 (= C272), E381 (= E366), E459 (≠ F444)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I133), T151 (≠ A134), P152 (= P135), W153 (= W136), K177 (= K160), S180 (≠ E163), G210 (≠ A192), G214 (≠ A196), F228 (= F214), G230 (= G216), E231 (≠ S217), T234 (≠ V220), N331 (≠ D316), R333 (≠ K318), Q334 (≠ T319)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
37% identity, 94% coverage: 28:470/470 of query aligns to 38:478/482 of 5ek6A
- active site: N147 (= N137), K170 (= K160), E245 (= E238), C279 (= C272), E374 (= E366), E452 (≠ F444)
- binding 2-methylpropanal: I152 (≠ L142), K155 (≠ R145), T222 (= T215), E245 (= E238), F441 (= F433)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I133), T144 (≠ A134), W146 (= W136), N147 (= N137), I152 (≠ L142), K170 (= K160), A172 (≠ S162), S173 (≠ E163), P202 (vs. gap), G203 (≠ A192), G207 (≠ A196), F221 (= F214), T222 (= T215), G223 (= G216), E224 (≠ S217), T227 (≠ V220), I231 (= I224), E245 (= E238), L246 (= L239), C279 (= C272), E374 (= E366)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
37% identity, 94% coverage: 28:470/470 of query aligns to 38:478/482 of 4h73A
- active site: N147 (= N137), K170 (= K160), E245 (= E238), C279 (= C272), E374 (= E366), E452 (≠ F444)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I133), T144 (≠ A134), P145 (= P135), W146 (= W136), K170 (= K160), A172 (≠ S162), S173 (≠ E163), G203 (≠ A192), G207 (≠ A196), F221 (= F214), G223 (= G216), E224 (≠ S217), T227 (≠ V220)
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)
36% identity, 96% coverage: 12:461/470 of query aligns to 32:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 96% coverage: 12:461/470 of query aligns to 31:479/481 of 3jz4A
- active site: N156 (= N137), K179 (= K160), E254 (= E238), C288 (= C272), E385 (= E366), E462 (≠ F444)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P135), W155 (= W136), K179 (= K160), A181 (≠ S162), S182 (≠ E163), A212 (= A196), G216 (≠ V200), G232 (= G216), S233 (= S217), I236 (≠ V220), C288 (= C272), K338 (≠ H322), E385 (= E366), F387 (= F368)
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)
38% identity, 96% coverage: 12:462/470 of query aligns to 32:482/484 of Q8NMB0
- N157 (= N137) 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 (= K160) 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 (≠ A178) 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 (= E238) 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 (= C272) 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.
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
34% identity, 98% coverage: 2:462/470 of query aligns to 35:495/503 of 1bpwA
- active site: N166 (= N137), K189 (= K160), E263 (= E238), C297 (= C272), E400 (= E366), E477 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I162 (= I133), L163 (≠ A134), W165 (= W136), N166 (= N137), K189 (= K160), G221 (≠ A192), G225 (≠ V200), T240 (= T215), G241 (= G216), S242 (= S217), T245 (≠ V220), E263 (= E238), L264 (= L239), C297 (= C272), E400 (= E366), F402 (= F368), F466 (= F433)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
34% identity, 98% coverage: 2:462/470 of query aligns to 35:495/503 of P56533
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)
35% identity, 97% coverage: 6:462/470 of query aligns to 23:486/487 of Q9H2A2
- R109 (≠ L91) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N137) mutation to A: Complete loss of activity.
- R451 (≠ H426) mutation to A: Complete loss of activity.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 97% coverage: 12:468/470 of query aligns to 25:487/489 of 4o6rA
- active site: N150 (= N137), K173 (= K160), E248 (= E238), C282 (= C272), E383 (= E366), E460 (≠ F444)
- binding adenosine monophosphate: I146 (= I133), V147 (≠ A134), K173 (= K160), G206 (≠ P193), G210 (≠ A197), Q211 (≠ E198), F224 (= F214), G226 (= G216), S227 (= S217), T230 (≠ V220), R233 (≠ I223)
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
33% identity, 96% coverage: 12:462/470 of query aligns to 32:485/493 of 6vr6D
- active site: N156 (= N137), E253 (= E238), C287 (= C272), E467 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I152 (= I133), G153 (≠ A134), W155 (= W136), K179 (= K160), A212 (≠ P193), G215 (≠ A196), Q216 (≠ A197), F229 (= F214), G231 (= G216), S232 (= S217), T235 (≠ V220), I239 (= I224)
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)
33% identity, 96% coverage: 12:462/470 of query aligns to 33:486/494 of P49189
- C116 (≠ M95) 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
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)
35% identity, 96% coverage: 12:464/470 of query aligns to 24:475/475 of Q59931
- R103 (≠ L91) binding
- S151 (≠ A134) binding
- K177 (= K160) binding
- T180 (≠ E163) binding
- D215 (≠ G201) binding
- 230:251 (vs. 216:239, 46% identical) binding
- E377 (= E366) binding
- R437 (≠ H426) binding
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
35% identity, 96% coverage: 12:464/470 of query aligns to 23:474/474 of 2esdA
- active site: N153 (= N137), K176 (= K160), A249 (≠ E238), C283 (= C272), E376 (= E366), Q454 (≠ F444)
- binding glyceraldehyde-3-phosphate: R102 (≠ L91), Y154 (≠ A138), R282 (≠ I271), C283 (= C272), T284 (≠ M273), Q435 (≠ V425), R436 (≠ H426)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ W136), K176 (= K160), P178 (≠ S162), T179 (≠ E163), G209 (≠ A196), G213 (≠ V200), D214 (≠ G201), F227 (= F214), S230 (= S217), I233 (≠ V220), K328 (= K318), S329 (≠ T319), Y332 (≠ H322)
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
37% identity, 91% coverage: 33:462/470 of query aligns to 48:477/478 of 6tgwA
- active site: N155 (= N137), E254 (= E238), C288 (= C272), E459 (≠ F444)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (vs. gap), G110 (≠ L91), F156 (≠ A138), Q278 (≠ F262), F282 (≠ M266), L442 (≠ H426), A444 (= A429)
- binding nicotinamide-adenine-dinucleotide: I151 (= I133), T152 (≠ A134), P153 (= P135), W154 (= W136), K178 (= K160), G211 (≠ A196), G215 (≠ V200), F229 (= F214), G231 (= G216), S232 (= S217), V235 (= V220)
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
35% identity, 96% coverage: 12:464/470 of query aligns to 23:474/474 of 1qi1B
- active site: N153 (= N137), K176 (= K160), E249 (= E238), S283 (≠ C272), E376 (= E366), Q454 (≠ F444)
- binding sn-glycerol-3-phosphate: Y154 (≠ A138), R282 (≠ I271), S283 (≠ C272), T284 (≠ M273), R436 (≠ H426)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (= P135), F152 (≠ W136), N153 (= N137), L158 (= L142), K176 (= K160), P178 (≠ S162), T179 (≠ E163), G209 (≠ A196), G213 (≠ V200), G229 (= G216), S230 (= S217), I233 (≠ V220), E249 (= E238), L250 (= L239), S283 (≠ C272)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
36% identity, 95% coverage: 13:457/470 of query aligns to 26:469/480 of 3rhhD
- active site: N155 (= N137), K178 (= K160), E251 (= E238), C285 (= C272), E378 (= E366), Q456 (≠ F444)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (= I133), P153 (= P135), F154 (≠ W136), K178 (= K160), P179 (≠ A161), A180 (≠ S162), T181 (≠ E163), G211 (≠ A197), G215 (= G201), D216 (vs. gap), F229 (= F214), G231 (= G216), G232 (≠ S217), T235 (≠ V220)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
37% identity, 91% coverage: 33:462/470 of query aligns to 56:488/489 of 7a6qB
- active site: N163 (= N137), E262 (= E238), C296 (= C272), E470 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I159 (= I133), W162 (= W136), K186 (= K160), E189 (= E163), G219 (≠ A196), G223 (≠ V200), S240 (= S217), V243 (= V220), K342 (= K318)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: D103 (≠ E77), E189 (= E163), Q190 (≠ S164), F218 (≠ D195), I339 (≠ V315), D340 (= D316)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L91), D141 (= D114), N143 (≠ G117), N451 (≠ T424), L453 (≠ H426), A455 (= A429)
Sites not aligning to the query:
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
37% identity, 91% coverage: 33:462/470 of query aligns to 56:488/489 of 7a6qA
- active site: N163 (= N137), E262 (= E238), C296 (= C272), E470 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I159 (= I133), T160 (≠ A134), W162 (= W136), K186 (= K160), A188 (≠ S162), E189 (= E163), G219 (≠ A196), G223 (≠ V200), S240 (= S217), V243 (= V220), K342 (= K318), K346 (≠ H322)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L91), D141 (= D114), N143 (≠ G117), N451 (≠ T424), L453 (≠ H426), Y454 (≠ E428)
Query Sequence
>CCNA_02485 FitnessBrowser__Caulo:CCNA_02485
MSSPQAVFERRDPVTGAVATTSIAMTADQARVAVDAAQAALPTWSALGPNARRALLSKAA
AALEARADDFVAAMMGEIGATEGWARFNLMLAASMVREAAALTTQVSGEVIPSDKPGCLA
MAVREPVGVILGIAPWNAPIILGVRAVATPLACGNTVVLKASESCPRTHELIAEAFAAAG
LPEGALSIVTNAPADAAEVVGALIDHPAVRRINFTGSTAVGKIIAKRAAEHLKPVLLELG
GKAPLIVLEDADLDEAVKAAAFGAFMNQGQICMSTERIIVVDAIADAFVAKFAAKASSLA
VGDPREGKTPLGAVVDLKTVTHVQGLVADALADGAVQVSGGPANGVLMPATVVDKVTPAM
RLFREESFGPVVAVIRARDEEHAIALANDTEYGLSASVFTRDIARGLKVARRIQSGICHV
NGPTVHDEAQMPFGGVKASGYGRFGGKAGVDAFTELRWITVETQPGHFPI
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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