SitesBLAST
Comparing Ac3H11_1605 FitnessBrowser__acidovorax_3H11:Ac3H11_1605 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
67% identity, 98% coverage: 13:511/511 of query aligns to 3:504/504 of 6dbbA
- active site: N152 (= N162), E259 (= E265), C293 (= C299), E471 (= E478)
- binding nicotinamide-adenine-dinucleotide: I148 (= I158), S149 (= S159), A150 (= A160), F151 (= F161), N152 (= N162), K175 (= K185), S177 (= S187), R218 (= R224), T236 (= T242), G237 (= G243), S238 (= S244), M241 (= M247), E259 (= E265), L260 (= L266), G261 (= G267), C293 (= C299), E391 (= E398), F393 (= F400)
- 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 (= R224), T236 (= T242), G237 (= G243), S238 (= S244), M241 (= M247), E259 (= E265), L260 (= L266), G261 (= G267), C293 (= C299), E391 (= E398), F393 (= F400)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
63% identity, 97% coverage: 15:509/511 of query aligns to 14:507/508 of 6rttA
- active site: N161 (= N162), E262 (= E265), C296 (= C299), E476 (= E478)
- binding pyridine-2-carboxylic acid: A159 (= A160), F162 (= F163), V166 (= V167), W169 (= W170), G240 (= G243), S241 (= S244), R295 (= R298), C296 (= C299), T297 (= T300), E396 (= E398), F398 (= F400), P421 (≠ G423), K469 (= K471), E470 (= E472)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
63% identity, 97% coverage: 15:509/511 of query aligns to 15:508/509 of 6rtsA
- active site: N162 (= N162), E263 (= E265), C297 (= C299), E477 (= E478)
- binding nicotinamide-adenine-dinucleotide: I158 (= I158), S159 (= S159), A160 (= A160), F161 (= F161), N162 (= N162), K185 (= K185), S187 (= S187), E188 (= E188), A222 (≠ R224), G225 (= G227), T240 (= T242), G241 (= G243), S242 (= S244), M245 (= M247), E263 (= E265), L264 (= L266), C297 (= C299), E397 (= E398), F399 (= F400)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
62% identity, 97% coverage: 15:509/511 of query aligns to 14:504/505 of 6rtuA
- active site: N161 (= N162), E259 (= E265), C293 (= C299), E473 (= E478)
- binding 2-aminohexanedioic acid: E115 (= E116), F162 (= F163), R292 (= R298), C293 (= C299), T294 (= T300), S454 (= S459), G455 (= G460), A456 (= A461), F462 (= F467)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
49% identity, 94% coverage: 29:509/511 of query aligns to 33:509/509 of 2jg7A
- active site: N166 (= N162), K189 (= K185), E267 (= E265), C301 (= C299), E398 (= E398), E478 (= E478)
- binding nicotinamide-adenine-dinucleotide: I162 (= I158), T163 (≠ S159), A164 (= A160), F165 (= F161), N166 (= N162), K189 (= K185), P192 (≠ E188), A226 (≠ R224), G229 (= G227), T230 (≠ E228), F243 (≠ A241), T244 (= T242), G245 (= G243), S246 (= S244), V249 (≠ M247), E267 (= E265), L268 (= L266), C301 (= C299), E398 (= E398), F400 (= F400)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
49% identity, 94% coverage: 30:509/511 of query aligns to 33:508/509 of 4zulA
- active site: N165 (= N162), K188 (= K185), E266 (= E265), C300 (= C299), E397 (= E398), E477 (= E478)
- binding 2-aminohexanedioic acid: E119 (= E116), F166 (= F163), R299 (= R298), C300 (= C299), T301 (= T300), G459 (= G460), A460 (= A461), F466 (= F467)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
49% identity, 94% coverage: 30:509/511 of query aligns to 33:508/509 of 4x0tA
- active site: N165 (= N162), K188 (= K185), E266 (= E265), C300 (= C299), E397 (= E398), E477 (= E478)
- binding 4-(diethylamino)benzaldehyde: F166 (= F163), V170 (= V167), W173 (= W170), C300 (= C299), F466 (= F467)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S159), A163 (= A160), F164 (= F161), N165 (= N162), K188 (= K185), G189 (≠ P186), A190 (≠ S187), A225 (≠ R224), G228 (= G227), T229 (≠ E228), F242 (≠ A241), T243 (= T242), G244 (= G243), S245 (= S244), V248 (≠ M247), E266 (= E265), L267 (= L266), C300 (= C299), E397 (= E398), F399 (= F400)
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)
49% identity, 94% coverage: 30:510/511 of query aligns to 63:539/539 of P49419
- 110:539 (vs. 77:510, 51% 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 227:228) binding
- GS 274:275 (= GS 243:244) binding
- EL 296:297 (= EL 265:266) binding
- C330 (= C299) active site, Nucleophile
- E427 (= E398) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ S410) to Q: in dbSNP:rs12514417
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
49% identity, 93% coverage: 29:504/511 of query aligns to 28:498/498 of 4pxnA
- active site: N161 (= N162), K184 (= K185), E262 (= E265), C296 (= C299), E392 (= E398), E472 (= E478)
- binding nicotinamide-adenine-dinucleotide: I157 (= I158), T158 (≠ S159), A159 (= A160), F160 (= F161), N161 (= N162), K184 (= K185), T221 (≠ R224), G224 (= G227), Q225 (≠ E228), F238 (≠ A241), T239 (= T242), G240 (= G243), S241 (= S244), A244 (≠ M247), V248 (= V251), E262 (= E265), L263 (= L266), S264 (≠ G267), C296 (= C299), E392 (= E398), F394 (= F400), F461 (= F467)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
49% identity, 94% coverage: 30:509/511 of query aligns to 34:509/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
49% identity, 92% coverage: 30:498/511 of query aligns to 33:497/497 of 2j6lA
- active site: N165 (= N162), K188 (= K185), E266 (= E265), C300 (= C299), E397 (= E398), E477 (= E478)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I158), T162 (≠ S159), A163 (= A160), F164 (= F161), N165 (= N162), K188 (= K185), A225 (≠ R224), G228 (= G227), T229 (≠ E228), F242 (≠ A241), T243 (= T242), G244 (= G243), S245 (= S244), V248 (≠ M247), E266 (= E265), L267 (= L266), C300 (= C299), E397 (= E398), F399 (= F400)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
47% identity, 92% coverage: 30:498/511 of query aligns to 33:487/487 of 4x0uD
- active site: N165 (= N162), K188 (= K185), E266 (= E265), C300 (= C299), E397 (= E398), E467 (= E478)
- binding 4-(diethylamino)benzaldehyde: F166 (= F163), A169 (= A166), V170 (= V167), C300 (= C299), F456 (= F467), H461 (≠ E472)
- binding magnesium ion: E119 (= E116), D122 (= D119)
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)
33% identity, 93% coverage: 30:505/511 of query aligns to 26:510/511 of 6fkuA
- active site: N159 (= N162), E261 (= E265), C295 (= C299), E483 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I158), T156 (≠ S159), N159 (= N162), K182 (= K185), S184 (= S187), E185 (= E188), G214 (vs. gap), G215 (= G222), K216 (≠ Q223), G220 (= G227), Q221 (≠ E228), F237 (≠ A241), T238 (= T242), G239 (= G243), S240 (= S244), V243 (≠ M247), E261 (= E265), L262 (= L266), C295 (= C299), R342 (≠ M345), F343 (≠ A346), E404 (= E398), F406 (= F400)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 92% coverage: 27:497/511 of query aligns to 13:477/477 of 6j76A
- active site: N148 (= N162), E246 (= E265), C280 (= C299), E458 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I158), T145 (≠ S159), A146 (= A160), W147 (≠ F161), N148 (= N162), K171 (= K185), T173 (≠ S187), S174 (≠ E188), G204 (≠ Q223), G208 (= G227), T223 (= T242), G224 (= G243), S225 (= S244), A228 (≠ M247), S231 (≠ A250), I232 (≠ V251), E246 (= E265), L247 (= L266), C280 (= C299), E381 (= E398), F383 (= F400), H447 (≠ F467)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
33% identity, 79% coverage: 37:438/511 of query aligns to 26:421/477 of 2opxA
- active site: N151 (= N162), K174 (= K185), E249 (= E265), C283 (= C299), E381 (= E398)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ E116), F152 (= F163), N284 (≠ T300), F312 (≠ V328), G313 (= G329), R318 (≠ P334), D320 (≠ T336), I321 (≠ L337), A322 (vs. gap), Y362 (= Y380)
Sites not aligning to the query:
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)
33% identity, 79% coverage: 37:438/511 of query aligns to 28:423/479 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 (≠ E228) binding
- S230 (= S244) binding
- E251 (= E265) binding
- N286 (≠ T300) 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 (≠ G349) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
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)
33% identity, 79% coverage: 37:438/511 of query aligns to 26:421/477 of 2impA
- active site: N151 (= N162), K174 (= K185), E249 (= E265), C283 (= C299), E381 (= E398)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I158), L148 (≠ S159), P149 (≠ A160), W150 (≠ F161), K174 (= K185), E177 (= E188), F178 (≠ K189), G207 (vs. gap), G211 (= G227), Q212 (≠ E228), S228 (= S244), A231 (≠ M247), K234 (≠ A250), R334 (≠ G349)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
33% identity, 79% coverage: 37:438/511 of query aligns to 26:421/477 of 2iluA
- active site: N151 (= N162), K174 (= K185), E249 (= E265), C283 (= C299), E381 (= E398)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I158), L148 (≠ S159), P149 (≠ A160), W150 (≠ F161), K174 (= K185), S176 (= S187), E177 (= E188), R206 (≠ Q223), G207 (vs. gap), G211 (= G227), Q212 (≠ E228), S228 (= S244), A231 (≠ M247), K234 (≠ A250), I235 (≠ V251), N328 (≠ D343), R334 (≠ G349), F383 (= F400)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
30% identity, 91% coverage: 27:489/511 of query aligns to 21:473/481 of 3jz4A
- active site: N156 (= N162), K179 (= K185), E254 (= E265), C288 (= C299), E385 (= E398), E462 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A160), W155 (≠ F161), K179 (= K185), A181 (≠ S187), S182 (≠ E188), A212 (≠ R224), G216 (= G227), G232 (= G243), S233 (= S244), I236 (≠ M247), C288 (= C299), K338 (≠ G349), E385 (= E398), F387 (= F400)
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, 91% coverage: 27:489/511 of query aligns to 22:474/482 of P25526
Query Sequence
>Ac3H11_1605 FitnessBrowser__acidovorax_3H11:Ac3H11_1605
MSATPAATPLVSEVDQLLQRLGVPRAAYTGGTLAARSPITGEVLAQVPQQSAADATAAIG
RAHAAFLAWRNVPAPRRGELVRLLGEELRAAKGDLGLLVTIEAGKIPSEGLGEVQEMIDI
CDFAVGLSRQLYGLTIATERPGHRMMETWHPLGVCGVISAFNFPVAVWSWNAALALVCGD
SVVWKPSEKTPLTALATHAIAQRAIARFGTDAPEGLLELIVGQRDIGEVLVDDARVPVLS
ATGSTAMGRAVGPRLAARFARGILELGGNNAAIVAPTADLNLALRGIAFAAMGTAGQRCT
TLRRLFVHASIYDQLVPQLAKVYANVQVGDPRTPGTLVGPLIDRMAFDGMQKALEQSRAL
GATVHGGGRVEGVGGADAYYVRPALVELQKHEGPALHETFAPILYVVRYSAIDEAIAMNN
AVGAGLSSSIFTLNVREAEQFMSAAGSDCGIANVNIGPSGAEIGGAFGGEKETGGGREAG
SDSWKAYMRRATNTINYSTALPLAQGVTFDV
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