SitesBLAST
Comparing CA265_RS19780 FitnessBrowser__Pedo557:CA265_RS19780 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
56% identity, 95% coverage: 25:513/513 of query aligns to 16:504/504 of 6dbbA
- active site: N152 (= N165), E259 (= E266), C293 (= C300), E471 (= E480)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), S149 (= S162), A150 (= A163), F151 (= F164), N152 (= N165), K175 (= K188), S177 (= S190), R218 (= R225), T236 (= T243), G237 (= G244), S238 (= S245), M241 (= M248), E259 (= E266), L260 (= L267), G261 (= G268), C293 (= C300), E391 (= E400), F393 (= F402)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I161), S149 (= S162), A150 (= A163), F151 (= F164), N152 (= N165), K175 (= K188), S177 (= S190), R218 (= R225), T236 (= T243), G237 (= G244), S238 (= S245), M241 (= M248), E259 (= E266), L260 (= L267), G261 (= G268), C293 (= C300), E391 (= E400), F393 (= F402)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
54% identity, 98% coverage: 7:511/513 of query aligns to 11:509/509 of 2jg7A
- active site: N166 (= N165), K189 (= K188), E267 (= E266), C301 (= C300), E398 (= E400), E478 (= E480)
- binding nicotinamide-adenine-dinucleotide: I162 (= I161), T163 (≠ S162), A164 (= A163), F165 (= F164), N166 (= N165), K189 (= K188), P192 (≠ E191), A226 (≠ R225), G229 (= G228), T230 (≠ E229), F243 (≠ A242), T244 (= T243), G245 (= G244), S246 (= S245), V249 (≠ M248), E267 (= E266), L268 (= L267), C301 (= C300), E398 (= E400), F400 (= F402)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
54% identity, 98% coverage: 9:512/513 of query aligns to 12:509/509 of 4zulA
- active site: N165 (= N165), K188 (= K188), E266 (= E266), C300 (= C300), E397 (= E400), E477 (= E480)
- binding 2-aminohexanedioic acid: E119 (= E119), F166 (= F166), R299 (= R299), C300 (= C300), T301 (= T301), G459 (= G462), A460 (= A463), F466 (= F469)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
54% identity, 98% coverage: 9:512/513 of query aligns to 12:509/509 of 4x0tA
- active site: N165 (= N165), K188 (= K188), E266 (= E266), C300 (= C300), E397 (= E400), E477 (= E480)
- binding 4-(diethylamino)benzaldehyde: F166 (= F166), V170 (= V170), W173 (= W173), C300 (= C300), F466 (= F469)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S162), A163 (= A163), F164 (= F164), N165 (= N165), K188 (= K188), G189 (≠ P189), A190 (≠ S190), A225 (≠ R225), G228 (= G228), T229 (≠ E229), F242 (≠ A242), T243 (= T243), G244 (= G244), S245 (= S245), V248 (≠ M248), E266 (= E266), L267 (= L267), C300 (= C300), E397 (= E400), F399 (= F402)
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)
54% identity, 98% coverage: 9:512/513 of query aligns to 42:539/539 of P49419
- 110:539 (vs. 80:512, 57% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 162:164) binding
- A199 (= A169) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K188) binding
- GT 258:259 (≠ GE 228:229) binding
- GS 274:275 (= GS 244:245) binding
- EL 296:297 (= EL 266:267) binding
- C330 (= C300) active site, Nucleophile
- E427 (= E400) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (= K412) to Q: in dbSNP:rs12514417
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
54% identity, 98% coverage: 9:512/513 of query aligns to 13:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
54% identity, 96% coverage: 9:500/513 of query aligns to 12:497/497 of 2j6lA
- active site: N165 (= N165), K188 (= K188), E266 (= E266), C300 (= C300), E397 (= E400), E477 (= E480)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I161), T162 (≠ S162), A163 (= A163), F164 (= F164), N165 (= N165), K188 (= K188), A225 (≠ R225), G228 (= G228), T229 (≠ E229), F242 (≠ A242), T243 (= T243), G244 (= G244), S245 (= S245), V248 (≠ M248), E266 (= E266), L267 (= L267), C300 (= C300), E397 (= E400), F399 (= F402)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
55% identity, 93% coverage: 34:511/513 of query aligns to 30:507/508 of 6rttA
- active site: N161 (= N165), E262 (= E266), C296 (= C300), E476 (= E480)
- binding pyridine-2-carboxylic acid: A159 (= A163), F162 (= F166), V166 (= V170), W169 (= W173), G240 (= G244), S241 (= S245), R295 (= R299), C296 (= C300), T297 (= T301), E396 (= E400), F398 (= F402), P421 (= P425), K469 (= K473), E470 (= E474)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
55% identity, 93% coverage: 34:511/513 of query aligns to 31:508/509 of 6rtsA
- active site: N162 (= N165), E263 (= E266), C297 (= C300), E477 (= E480)
- binding nicotinamide-adenine-dinucleotide: I158 (= I161), S159 (= S162), A160 (= A163), F161 (= F164), N162 (= N165), K185 (= K188), S187 (= S190), E188 (= E191), A222 (≠ R225), G225 (= G228), T240 (= T243), G241 (= G244), S242 (= S245), M245 (= M248), E263 (= E266), L264 (= L267), C297 (= C300), E397 (= E400), F399 (= F402)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
50% identity, 98% coverage: 6:506/513 of query aligns to 4:498/498 of 4pxnA
- active site: N161 (= N165), K184 (= K188), E262 (= E266), C296 (= C300), E392 (= E400), E472 (= E480)
- binding nicotinamide-adenine-dinucleotide: I157 (= I161), T158 (≠ S162), A159 (= A163), F160 (= F164), N161 (= N165), K184 (= K188), T221 (≠ R225), G224 (= G228), Q225 (≠ E229), F238 (≠ A242), T239 (= T243), G240 (= G244), S241 (= S245), A244 (≠ M248), V248 (= V252), E262 (= E266), L263 (= L267), S264 (≠ G268), C296 (= C300), E392 (= E400), F394 (= F402), F461 (= F469)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
52% identity, 96% coverage: 9:500/513 of query aligns to 12:487/487 of 4x0uD
- active site: N165 (= N165), K188 (= K188), E266 (= E266), C300 (= C300), E397 (= E400), E467 (= E480)
- binding 4-(diethylamino)benzaldehyde: F166 (= F166), A169 (= A169), V170 (= V170), C300 (= C300), F456 (= F469), H461 (≠ E474)
- binding magnesium ion: E119 (= E119), D122 (= D122)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
54% identity, 93% coverage: 34:511/513 of query aligns to 30:504/505 of 6rtuA
- active site: N161 (= N165), E259 (= E266), C293 (= C300), E473 (= E480)
- binding 2-aminohexanedioic acid: E115 (= E119), F162 (= F166), R292 (= R299), C293 (= C300), T294 (= T301), S454 (= S461), G455 (= G462), A456 (= A463), F462 (= F469)
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, 94% coverage: 28:507/513 of query aligns to 19:510/511 of 6fkuA
- active site: N159 (= N165), E261 (= E266), C295 (= C300), E483 (= E480)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I161), T156 (≠ S162), N159 (= N165), K182 (= K188), S184 (= S190), E185 (= E191), G214 (≠ D224), G215 (≠ R225), K216 (≠ E226), G220 (= G228), Q221 (≠ E229), F237 (≠ A242), T238 (= T243), G239 (= G244), S240 (= S245), V243 (≠ M248), E261 (= E266), L262 (= L267), C295 (= C300), R342 (≠ D346), F343 (≠ A347), E404 (= E400), F406 (= F402)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
33% identity, 97% coverage: 9:505/513 of query aligns to 5:487/489 of 6wsbA
- active site: N152 (= N165), E250 (= E266), C284 (= C300), E462 (= E480)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), G149 (≠ S162), A150 (= A163), W151 (≠ F164), N152 (= N165), K175 (= K188), E178 (= E191), G208 (≠ R225), G211 (= G228), A212 (≠ E229), F225 (≠ A242), T226 (= T243), G227 (= G244), G228 (≠ S245), T231 (≠ M248), V235 (= V252), E250 (= E266), L251 (= L267), G252 (= G268), C284 (= C300), E385 (= E400), F387 (= F402)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
34% identity, 89% coverage: 35:491/513 of query aligns to 23:475/490 of Q9HTJ1
- GAWN 150:153 (≠ SAFN 162:165) binding
- K162 (≠ N174) active site, Charge relay system
- KPSE 176:179 (= KPSE 188:191) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ STRM 245:248) binding
- E252 (= E266) active site, Proton acceptor
- C286 (= C300) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E400) binding
- E464 (= E480) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 89% coverage: 35:491/513 of query aligns to 22:474/489 of 4cazA
- active site: N152 (= N165), K175 (= K188), E251 (= E266), C285 (= C300), E386 (= E400), E463 (= E480)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I161), G149 (≠ S162), W151 (≠ F164), N152 (= N165), K175 (= K188), E178 (= E191), G208 (vs. gap), G212 (= G228), F226 (≠ A242), T227 (= T243), G228 (= G244), G229 (≠ S245), T232 (≠ M248), V236 (= V252), E251 (= E266), L252 (= L267), C285 (= C300), E386 (= E400), F388 (= F402)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 89% coverage: 35:491/513 of query aligns to 22:474/489 of 2woxA
- active site: N152 (= N165), K175 (= K188), E251 (= E266), C285 (= C300), E386 (= E400), E463 (= E480)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I161), G149 (≠ S162), W151 (≠ F164), N152 (= N165), K175 (= K188), S177 (= S190), E178 (= E191), G208 (vs. gap), G212 (= G228), F226 (≠ A242), T227 (= T243), G228 (= G244), G229 (≠ S245), T232 (≠ M248), V236 (= V252), E251 (= E266), L252 (= L267), C285 (= C300), E386 (= E400), F388 (= F402)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 89% coverage: 35:491/513 of query aligns to 22:474/489 of 2wmeA
- active site: N152 (= N165), K175 (= K188), E251 (= E266), C285 (= C300), E386 (= E400), E463 (= E480)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S162), W151 (≠ F164), K175 (= K188), S177 (= S190), E178 (= E191), G208 (vs. gap), G212 (= G228), F226 (≠ A242), G228 (= G244), G229 (≠ S245), T232 (≠ M248), V236 (= V252)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 93% coverage: 24:499/513 of query aligns to 7:477/477 of 6j76A
- active site: N148 (= N165), E246 (= E266), C280 (= C300), E458 (= E480)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I161), T145 (≠ S162), A146 (= A163), W147 (≠ F164), N148 (= N165), K171 (= K188), T173 (≠ S190), S174 (≠ E191), G204 (vs. gap), G208 (= G223), T223 (= T243), G224 (= G244), S225 (= S245), A228 (≠ M248), S231 (≠ A251), I232 (≠ V252), E246 (= E266), L247 (= L267), C280 (= C300), E381 (= E400), F383 (= F402), H447 (≠ F469)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 92% coverage: 35:504/513 of query aligns to 20:484/489 of 4o6rA
- active site: N150 (= N165), K173 (= K188), E248 (= E266), C282 (= C300), E383 (= E400), E460 (= E480)
- binding adenosine monophosphate: I146 (= I161), V147 (≠ S162), K173 (= K188), G206 (≠ D224), G210 (= G228), Q211 (≠ E229), F224 (≠ A242), G226 (= G244), S227 (= S245), T230 (≠ M248), R233 (≠ A251)
Query Sequence
>CA265_RS19780 FitnessBrowser__Pedo557:CA265_RS19780
MTTDIQSILNKLGINASNAAYSTGSNWGGELNVNTLESFSPVDGKLIASAKIATADDYDA
VVLKAQEAFTAWRSVPAPKRGEIVRQFGDALRENKDALGTLVSYEMGKSLQEGFGEVQEM
IDICDFAVGLSRQLYGLTMHSERPSHRMYEQWHPLGIVGIISAFNFPVAVWSWNTALALV
CGNVCIWKPSEKTPLTAIACQHIIAKVFKDNDIAEGVCNLILGDREVGERMTNDGRIPLI
SATGSTRMGKAVGAAVGARLGKSLLELGGNNAIIISEHADLDMSLIGAVFGAVGTAGQRC
TSTRRLIIHESVYDAFTAKLVKAYGQLRIGDPLDQNNHVGPLIDTDAVAAYLDSIAKCKA
EGGNFVVEGGVLSGDAYTSGCYVKPCIAEVQNDFKIVQHETFAPILYLIKYKTLDEAIAL
QNGVPQGLSSAIMTLNLREAEQFLSAKGSDCGIANVNIGTSGAEIGGAFGGEKETGGGRE
SGSDAWRAYMRRQTNTINYSNTLPLAQGIKFDL
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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