SitesBLAST
Comparing SMc04385 FitnessBrowser__Smeli:SMc04385 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)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
68% identity, 95% coverage: 28:509/510 of query aligns to 18:504/504 of 6dbbA
- active site: N152 (= N162), E259 (= E264), C293 (= C298), E471 (= E476)
- binding nicotinamide-adenine-dinucleotide: I148 (= I158), S149 (= S159), A150 (= A160), F151 (= F161), N152 (= N162), K175 (= K185), S177 (= S187), R218 (= R223), T236 (= T241), G237 (= G242), S238 (= S243), M241 (= M246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E396), F393 (= F398)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I158), S149 (= S159), A150 (= A160), F151 (= F161), N152 (= N162), K175 (= K185), S177 (= S187), R218 (= R223), T236 (= T241), G237 (= G242), S238 (= S243), M241 (= M246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E396), F393 (= F398)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
63% identity, 98% coverage: 9:507/510 of query aligns to 9:508/509 of 6rtsA
- active site: N162 (= N162), E263 (= E264), C297 (= C298), E477 (= E476)
- binding nicotinamide-adenine-dinucleotide: I158 (= I158), S159 (= S159), A160 (= A160), F161 (= F161), N162 (= N162), K185 (= K185), S187 (= S187), E188 (= E188), A222 (≠ R223), G225 (= G226), T240 (= T241), G241 (= G242), S242 (= S243), M245 (= M246), E263 (= E264), L264 (= L265), C297 (= C298), E397 (= E396), F399 (= F398)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
63% identity, 98% coverage: 9:507/510 of query aligns to 8:507/508 of 6rttA
- active site: N161 (= N162), E262 (= E264), C296 (= C298), E476 (= E476)
- binding pyridine-2-carboxylic acid: A159 (= A160), F162 (= F163), V166 (= V167), W169 (= W170), G240 (= G242), S241 (= S243), R295 (= R297), C296 (= C298), T297 (= T299), E396 (= E396), F398 (= F398), P421 (≠ A421), K469 (= K469), E470 (= E470)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
62% identity, 98% coverage: 9:507/510 of query aligns to 8:504/505 of 6rtuA
- active site: N161 (= N162), E259 (= E264), C293 (= C298), E473 (= E476)
- binding 2-aminohexanedioic acid: E115 (= E116), F162 (= F163), R292 (= R297), C293 (= C298), T294 (= T299), S454 (= S457), G455 (= G458), A456 (= A459), F462 (= F465)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
48% identity, 96% coverage: 16:507/510 of query aligns to 11:509/509 of 2jg7A
- active site: N166 (= N162), K189 (= K185), E267 (= E264), C301 (= C298), E398 (= E396), E478 (= E476)
- binding nicotinamide-adenine-dinucleotide: I162 (= I158), T163 (≠ S159), A164 (= A160), F165 (= F161), N166 (= N162), K189 (= K185), P192 (≠ E188), A226 (≠ R223), G229 (= G226), T230 (≠ E227), F243 (≠ A240), T244 (= T241), G245 (= G242), S246 (= S243), V249 (≠ M246), E267 (= E264), L268 (= L265), C301 (= C298), E398 (= E396), F400 (= F398)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
50% identity, 93% coverage: 33:508/510 of query aligns to 36:509/509 of 4zulA
- active site: N165 (= N162), K188 (= K185), E266 (= E264), C300 (= C298), E397 (= E396), E477 (= E476)
- binding 2-aminohexanedioic acid: E119 (= E116), F166 (= F163), R299 (= R297), C300 (= C298), T301 (= T299), G459 (= G458), A460 (= A459), F466 (= F465)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
50% identity, 93% coverage: 33:508/510 of query aligns to 36:509/509 of 4x0tA
- active site: N165 (= N162), K188 (= K185), E266 (= E264), C300 (= C298), E397 (= E396), E477 (= E476)
- binding 4-(diethylamino)benzaldehyde: F166 (= F163), V170 (= V167), W173 (= W170), C300 (= C298), F466 (= F465)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S159), A163 (= A160), F164 (= F161), N165 (= N162), K188 (= K185), G189 (≠ P186), A190 (≠ S187), A225 (≠ R223), G228 (= G226), T229 (≠ E227), F242 (≠ A240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (≠ M246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E396), F399 (= F398)
P49419 Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens (Human) (see 5 papers)
50% identity, 93% coverage: 33:508/510 of query aligns to 66:539/539 of P49419
- 110:539 (vs. 77:508, 52% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 159:161) binding
- A199 (= A166) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K185) binding
- GT 258:259 (≠ GE 226:227) binding
- GS 274:275 (= GS 242:243) binding
- EL 296:297 (= EL 264:265) binding
- C330 (= C298) active site, Nucleophile
- E427 (= E396) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ S408) to Q: in dbSNP:rs12514417
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
50% identity, 93% coverage: 33:508/510 of query aligns to 37:510/510 of 6o4dB
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
49% identity, 93% coverage: 29:502/510 of query aligns to 28:498/498 of 4pxnA
- active site: N161 (= N162), K184 (= K185), E262 (= E264), C296 (= C298), E392 (= E396), E472 (= E476)
- binding nicotinamide-adenine-dinucleotide: I157 (= I158), T158 (≠ S159), A159 (= A160), F160 (= F161), N161 (= N162), K184 (= K185), T221 (≠ R223), G224 (= G226), Q225 (≠ E227), F238 (≠ A240), T239 (= T241), G240 (= G242), S241 (= S243), A244 (≠ M246), V248 (= V250), E262 (= E264), L263 (= L265), S264 (≠ G266), C296 (= C298), E392 (= E396), F394 (= F398), F461 (= F465)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
50% identity, 91% coverage: 33:496/510 of query aligns to 36:497/497 of 2j6lA
- active site: N165 (= N162), K188 (= K185), E266 (= E264), C300 (= C298), E397 (= E396), E477 (= E476)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I158), T162 (≠ S159), A163 (= A160), F164 (= F161), N165 (= N162), K188 (= K185), A225 (≠ R223), G228 (= G226), T229 (≠ E227), F242 (≠ A240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (≠ M246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E396), F399 (= F398)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
48% identity, 91% coverage: 33:496/510 of query aligns to 36:487/487 of 4x0uD
- active site: N165 (= N162), K188 (= K185), E266 (= E264), C300 (= C298), E397 (= E396), E467 (= E476)
- binding 4-(diethylamino)benzaldehyde: F166 (= F163), A169 (= A166), V170 (= V167), C300 (= C298), F456 (= F465), H461 (≠ E470)
- binding magnesium ion: E119 (= E116), D122 (= D119)
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)
32% identity, 88% coverage: 37:486/510 of query aligns to 32:473/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
32% identity, 88% coverage: 37:486/510 of query aligns to 31:472/481 of 3jz4A
- active site: N156 (= N162), K179 (= K185), E254 (= E264), C288 (= C298), E385 (= E396), E462 (= E476)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A160), W155 (≠ F161), K179 (= K185), A181 (≠ S187), S182 (≠ E188), A212 (≠ R223), G216 (= G226), G232 (= G242), S233 (= S243), I236 (≠ M246), C288 (= C298), K338 (≠ G348), E385 (= E396), F387 (= F398)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
34% identity, 87% coverage: 61:503/510 of query aligns to 58:510/511 of 6fkuA
- active site: N159 (= N162), E261 (= E264), C295 (= C298), E483 (= E476)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I158), T156 (≠ S159), N159 (= N162), K182 (= K185), S184 (= S187), E185 (= E188), G214 (vs. gap), G215 (= G221), K216 (≠ D222), G220 (= G226), Q221 (≠ E227), F237 (≠ A240), T238 (= T241), G239 (= G242), S240 (= S243), V243 (≠ M246), E261 (= E264), L262 (= L265), C295 (= C298), R342 (≠ A344), F343 (≠ A345), E404 (= E396), F406 (= F398)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
32% identity, 92% coverage: 26:495/510 of query aligns to 12:477/477 of 6j76A
- active site: N148 (= N162), E246 (= E264), C280 (= C298), E458 (= E476)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I158), T145 (≠ S159), A146 (= A160), W147 (≠ F161), N148 (= N162), K171 (= K185), T173 (≠ S187), S174 (≠ E188), G204 (vs. gap), G208 (= G226), T223 (= T241), G224 (= G242), S225 (= S243), A228 (≠ M246), S231 (≠ E249), I232 (≠ V250), E246 (= E264), L247 (= L265), C280 (= C298), E381 (= E396), F383 (= F398), H447 (≠ F465)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 88% coverage: 37:487/510 of query aligns to 28:471/479 of P25553
- L150 (≠ S159) binding
- R161 (≠ W170) binding
- KPSE 176:179 (= KPSE 185:188) binding
- F180 (≠ K189) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E227) binding
- S230 (= S243) binding
- E251 (= E264) binding
- N286 (≠ T299) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ G348) binding
- E443 (≠ G458) binding
- H449 (≠ F465) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
31% identity, 88% coverage: 37:487/510 of query aligns to 26:469/477 of 2impA
- active site: N151 (= N162), K174 (= K185), E249 (= E264), C283 (= C298), E381 (= E396), A458 (≠ E476)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I158), L148 (≠ S159), P149 (≠ A160), W150 (≠ F161), K174 (= K185), E177 (= E188), F178 (≠ K189), G207 (vs. gap), G211 (= G226), Q212 (≠ E227), S228 (= S243), A231 (≠ M246), K234 (≠ E249), R334 (≠ G348)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
31% identity, 88% coverage: 37:487/510 of query aligns to 26:469/477 of 2iluA
- active site: N151 (= N162), K174 (= K185), E249 (= E264), C283 (= C298), E381 (= E396), A458 (≠ E476)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I158), L148 (≠ S159), P149 (≠ A160), W150 (≠ F161), K174 (= K185), S176 (= S187), E177 (= E188), R206 (≠ D222), G207 (vs. gap), G211 (= G226), Q212 (≠ E227), S228 (= S243), A231 (≠ M246), K234 (≠ E249), I235 (≠ V250), N328 (≠ D342), R334 (≠ G348), F383 (= F398)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
30% identity, 93% coverage: 26:497/510 of query aligns to 24:491/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I158), I160 (≠ S159), P161 (≠ A160), W162 (≠ F161), N163 (= N162), K186 (= K185), E189 (= E188), G219 (≠ D222), G223 (= G226), F237 (≠ A240), T238 (= T241), G239 (= G242), S240 (= S243), V243 (≠ M246), E262 (= E264), G264 (= G266), Q343 (≠ A345), K346 (≠ G348), E393 (= E396), F395 (= F398)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W170), H286 (≠ F288), Y290 (≠ G292), I297 (≠ T299), G451 (= G455)
Query Sequence
>SMc04385 FitnessBrowser__Smeli:SMc04385
MNIAAKKIDVASEAAALLDKMGVAKDLYTGGDMPSFSPVTGEKIASLKTVSAAEAAGKIE
KADEAFRAWRLVPAPKRGELVRLLGEELRAFKADLGRLVSIEAGKIPSEGLGEVQEMIDI
CDFAVGLSRQLYGLTIATERPGHRMMETWHPLGVVGIISAFNFPVAVWSWNAALALVCGD
AVVWKPSEKTPLTALACQAILERAIARFGDAPEGLSQVLIGDRAIGEVLVDHPKVPLVSA
TGSTRMGREVGPRLAKRFARAILELGGNNAGIVCPSADLDMALRAIAFGAMGTAGQRCTT
LRRLFVHESVYDQLVPRLKKAYQSVSVGNPLESAALVGPLVDKAAFDGMQKAIAEAKNHG
GAVTGGERVELGHENGYYVKPALVEMPKQEGPVLEETFAPILYVMKYSDFDAVLAEHNAV
AAGLSSSIFTRDMQESERFLAADGSDCGIANVNIGTSGAEIGGAFGGEKETGGGRESGSD
AWKAYMRRATNTVNYSKALPLAQGVSFDIE
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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