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Comparing BPHYT_RS32650 FitnessBrowser__BFirm:BPHYT_RS32650 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
61% identity, 100% coverage: 1:498/499 of query aligns to 2:504/504 of 6dbbA
- active site: N152 (= N150), E259 (= E252), C293 (= C286), E471 (= E465)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (= S147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R211), T236 (= T229), G237 (= G230), S238 (= S231), M241 (= M234), E259 (= E252), L260 (= L253), G261 (= G254), C293 (= C286), E391 (= E385), F393 (= F387)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I146), S149 (= S147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R211), T236 (= T229), G237 (= G230), S238 (= S231), M241 (= M234), E259 (= E252), L260 (= L253), G261 (= G254), C293 (= C286), E391 (= E385), F393 (= F387)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
59% identity, 99% coverage: 3:497/499 of query aligns to 14:509/509 of 6rtsA
- active site: N162 (= N150), E263 (= E252), C297 (= C286), E477 (= E465)
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), S159 (= S147), A160 (= A148), F161 (= F149), N162 (= N150), K185 (= K173), S187 (= S175), E188 (= E176), A222 (≠ R211), G225 (= G214), T240 (= T229), G241 (= G230), S242 (= S231), M245 (= M234), E263 (= E252), L264 (= L253), C297 (= C286), E397 (= E385), F399 (= F387)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
59% identity, 99% coverage: 3:497/499 of query aligns to 13:508/508 of 6rttA
- active site: N161 (= N150), E262 (= E252), C296 (= C286), E476 (= E465)
- binding pyridine-2-carboxylic acid: A159 (= A148), F162 (= F151), V166 (= V155), W169 (= W158), G240 (= G230), S241 (= S231), R295 (= R285), C296 (= C286), T297 (= T287), E396 (= E385), F398 (= F387), P421 (≠ V410), K469 (= K458), E470 (= E459)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
59% identity, 99% coverage: 3:497/499 of query aligns to 13:505/505 of 6rtuA
- active site: N161 (= N150), E259 (= E252), C293 (= C286), E473 (= E465)
- binding 2-aminohexanedioic acid: E115 (= E104), F162 (= F151), R292 (= R285), C293 (= C286), T294 (= T287), S454 (= S446), G455 (= G447), A456 (= A448), F462 (= F454)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
51% identity, 96% coverage: 21:497/499 of query aligns to 36:509/509 of 4zulA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- binding 2-aminohexanedioic acid: E119 (= E104), F166 (= F151), R299 (= R285), C300 (= C286), T301 (= T287), G459 (= G447), A460 (= A448), F466 (= F454)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
51% identity, 96% coverage: 21:497/499 of query aligns to 36:509/509 of 4x0tA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), V170 (= V155), W173 (= W158), C300 (= C286), F466 (= F454)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), G189 (≠ P174), A190 (≠ S175), A225 (≠ R211), G228 (= G214), T229 (≠ A215), F242 (≠ A228), T243 (= T229), G244 (= G230), S245 (= S231), V248 (≠ M234), E266 (= E252), L267 (= L253), C300 (= C286), E397 (= E385), F399 (= F387)
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)
51% identity, 96% coverage: 21:497/499 of query aligns to 66:539/539 of P49419
- 110:539 (vs. 65:497, 52% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 147:149) binding
- A199 (= A154) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K173) binding
- GT 258:259 (≠ GA 214:215) binding
- GS 274:275 (= GS 230:231) binding
- EL 296:297 (= EL 252:253) binding
- C330 (= C286) active site, Nucleophile
- E427 (= E385) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ T397) to Q: in dbSNP:rs12514417
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
50% identity, 96% coverage: 21:497/499 of query aligns to 37:510/510 of 6o4dB
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
50% identity, 95% coverage: 21:496/499 of query aligns to 37:509/509 of 2jg7A
- active site: N166 (= N150), K189 (= K173), E267 (= E252), C301 (= C286), E398 (= E385), E478 (= E465)
- binding nicotinamide-adenine-dinucleotide: I162 (= I146), T163 (≠ S147), A164 (= A148), F165 (= F149), N166 (= N150), K189 (= K173), P192 (≠ E176), A226 (≠ R211), G229 (= G214), T230 (≠ A215), F243 (≠ A228), T244 (= T229), G245 (= G230), S246 (= S231), V249 (≠ M234), E267 (= E252), L268 (= L253), C301 (= C286), E398 (= E385), F400 (= F387)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
50% identity, 93% coverage: 21:485/499 of query aligns to 36:497/497 of 2j6lA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I146), T162 (≠ S147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), A225 (≠ R211), G228 (= G214), T229 (≠ A215), F242 (≠ A228), T243 (= T229), G244 (= G230), S245 (= S231), V248 (≠ M234), E266 (= E252), L267 (= L253), C300 (= C286), E397 (= E385), F399 (= F387)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
49% identity, 94% coverage: 25:491/499 of query aligns to 36:498/498 of 4pxnA
- active site: N161 (= N150), K184 (= K173), E262 (= E252), C296 (= C286), E392 (= E385), E472 (= E465)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), T158 (≠ S147), A159 (= A148), F160 (= F149), N161 (= N150), K184 (= K173), T221 (≠ R211), G224 (= G214), Q225 (≠ A215), F238 (≠ A228), T239 (= T229), G240 (= G230), S241 (= S231), A244 (≠ M234), V248 (= V238), E262 (= E252), L263 (= L253), S264 (≠ G254), C296 (= C286), E392 (= E385), F394 (= F387), F461 (= F454)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
49% identity, 93% coverage: 21:485/499 of query aligns to 36:487/487 of 4x0uD
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E467 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), A169 (= A154), V170 (= V155), C300 (= C286), F456 (= F454), H461 (≠ E459)
- binding magnesium ion: E119 (= E104), D122 (= D107)
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)
33% identity, 91% coverage: 21:475/499 of query aligns to 28:473/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 91% coverage: 21:475/499 of query aligns to 27:472/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E252), C288 (= C286), E385 (= E385), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A148), W155 (≠ F149), K179 (= K173), A181 (≠ S175), S182 (≠ E176), A212 (≠ R211), G216 (= G214), G232 (= G230), S233 (= S231), I236 (≠ M234), C288 (= C286), K338 (≠ R336), E385 (= E385), F387 (= F387)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 93% coverage: 23:484/499 of query aligns to 21:477/477 of 6j76A
- active site: N148 (= N150), E246 (= E252), C280 (= C286), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I146), T145 (≠ S147), A146 (= A148), W147 (≠ F149), N148 (= N150), K171 (= K173), T173 (≠ S175), S174 (≠ E176), G204 (= G210), G208 (= G214), T223 (= T229), G224 (= G230), S225 (= S231), A228 (≠ M234), S231 (≠ T237), I232 (≠ V238), E246 (= E252), L247 (= L253), C280 (= C286), E381 (= E385), F383 (= F387), H447 (≠ F454)
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)
32% identity, 93% coverage: 30:492/499 of query aligns to 39:510/511 of 6fkuA
- active site: N159 (= N150), E261 (= E252), C295 (= C286), E483 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I146), T156 (≠ S147), N159 (= N150), K182 (= K173), S184 (= S175), E185 (= E176), G214 (= G209), G215 (= G210), K216 (≠ R211), G220 (vs. gap), Q221 (≠ D212), F237 (≠ A228), T238 (= T229), G239 (= G230), S240 (= S231), V243 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), R342 (≠ Q332), F343 (≠ S333), E404 (= E385), F406 (= F387)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 97% coverage: 4:489/499 of query aligns to 4:484/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E252), C282 (= C286), E383 (= E385), E460 (= E465)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ S147), K173 (= K173), G206 (= G210), G210 (= G214), Q211 (≠ A215), F224 (≠ A228), G226 (= G230), S227 (= S231), T230 (≠ M234), R233 (≠ T237)
7radA Crystal structure analysis of aldh1b1
32% identity, 92% coverage: 25:483/499 of query aligns to 34:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (≠ A148), W161 (≠ F149), N162 (= N150), M167 (≠ V155), K185 (= K173), E188 (= E176), G218 (= G210), G222 (= G214), A223 (= A215), T237 (= T229), G238 (= G230), S239 (= S231), V242 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), E392 (= E385), F394 (= F387)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (= E104), F163 (= F151), E285 (≠ F276), F289 (≠ G280), N450 (= N442), V452 (≠ A448)
7mjdA Crystal structure analysis of aldh1b1
32% identity, 92% coverage: 25:483/499 of query aligns to 34:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (≠ A148), W161 (≠ F149), N162 (= N150), M167 (≠ V155), K185 (= K173), E188 (= E176), G218 (= G210), G222 (= G214), F236 (≠ A228), T237 (= T229), G238 (= G230), S239 (= S231), V242 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), E392 (= E385), F394 (= F387)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (= E104), E285 (≠ F276), F289 (≠ G280), N450 (= N442), V452 (≠ A448)
7mjcA Crystal structure analysis of aldh1b1
32% identity, 92% coverage: 25:483/499 of query aligns to 34:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (≠ A148), W161 (≠ F149), N162 (= N150), K185 (= K173), E188 (= E176), G218 (= G210), G222 (= G214), T237 (= T229), G238 (= G230), S239 (= S231), V242 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), E392 (= E385), F394 (= F387)
Query Sequence
>BPHYT_RS32650 FitnessBrowser__BFirm:BPHYT_RS32650
MDASTILADLGIAHAAQAGDIAVHSPITGDLIGRVASNTVAEVDTALARAKEAYTAWRNV
PAPRRGELVRLLGNRLREKKQALGSIITLETGKILQEGLGEVQEMIDICDFAVGLSRQLY
GLTIASERPGHRMAETWHPMGTCVVISAFNFPAAVWSWNAALALVCGNAVIWKPSEKTPL
TALAVNQILTEALQEFGDAPAGLTALINGGRDVGAKLVADPRASIVSATGSTEMGRTVGV
EVAKRFGRSLLELGGNNAGIVTQTADHELAMRGILFSAVGTAGQRCTSLRRLFVHESVYD
KTIERLKQLYSKVPIGNPLEKGTLMGPLIDKQSYGRMQEALQQATAEGGKVFGGERVDVK
GYENGYYVRPAIVEMPSQTSVVLKETFAPILYVLRYTDFADAVEANNAAVHGLSSCVFTT
DLREAERFLSDSGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWKAYMRRATN
TVNYSSALPLAQGIDFNIG
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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