SitesBLAST
Comparing CCNA_01274 FitnessBrowser__Caulo:CCNA_01274 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
64% identity, 94% coverage: 33:507/507 of query aligns to 26:504/504 of 6dbbA
- active site: N152 (= N159), E259 (= E261), C293 (= C295), E471 (= E474)
- binding nicotinamide-adenine-dinucleotide: I148 (= I155), S149 (= S156), A150 (= A157), F151 (= F158), N152 (= N159), K175 (= K182), S177 (= S184), R218 (= R220), T236 (= T238), G237 (= G239), S238 (= S240), M241 (= M243), E259 (= E261), L260 (= L262), G261 (= G263), C293 (= C295), E391 (= E394), F393 (= F396)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I155), S149 (= S156), A150 (= A157), F151 (= F158), N152 (= N159), K175 (= K182), S177 (= S184), R218 (= R220), T236 (= T238), G237 (= G239), S238 (= S240), M241 (= M243), E259 (= E261), L260 (= L262), G261 (= G263), C293 (= C295), E391 (= E394), F393 (= F396)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
63% identity, 98% coverage: 10:505/507 of query aligns to 12:508/509 of 6rtsA
- active site: N162 (= N159), E263 (= E261), C297 (= C295), E477 (= E474)
- binding nicotinamide-adenine-dinucleotide: I158 (= I155), S159 (= S156), A160 (= A157), F161 (= F158), N162 (= N159), K185 (= K182), S187 (= S184), E188 (= E185), A222 (≠ R220), G225 (= G223), T240 (= T238), G241 (= G239), S242 (= S240), M245 (= M243), E263 (= E261), L264 (= L262), C297 (= C295), E397 (= E394), F399 (= F396)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
63% identity, 98% coverage: 10:505/507 of query aligns to 11:507/508 of 6rttA
- active site: N161 (= N159), E262 (= E261), C296 (= C295), E476 (= E474)
- binding pyridine-2-carboxylic acid: A159 (= A157), F162 (= F160), V166 (= V164), W169 (= W167), G240 (= G239), S241 (= S240), R295 (= R294), C296 (= C295), T297 (= T296), E396 (= E394), F398 (= F396), P421 (= P419), K469 (= K467), E470 (= E468)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
62% identity, 98% coverage: 10:505/507 of query aligns to 11:504/505 of 6rtuA
- active site: N161 (= N159), E259 (= E261), C293 (= C295), E473 (= E474)
- binding 2-aminohexanedioic acid: E115 (= E113), F162 (= F160), R292 (= R294), C293 (= C295), T294 (= T296), S454 (= S455), G455 (= G456), A456 (= A457), F462 (= F463)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
50% identity, 90% coverage: 51:505/507 of query aligns to 58:509/509 of 2jg7A
- active site: N166 (= N159), K189 (= K182), E267 (= E261), C301 (= C295), E398 (= E394), E478 (= E474)
- binding nicotinamide-adenine-dinucleotide: I162 (= I155), T163 (≠ S156), A164 (= A157), F165 (= F158), N166 (= N159), K189 (= K182), P192 (≠ E185), A226 (≠ R220), G229 (= G223), T230 (≠ E224), F243 (≠ A237), T244 (= T238), G245 (= G239), S246 (= S240), V249 (≠ M243), E267 (= E261), L268 (= L262), C301 (= C295), E398 (= E394), F400 (= F396)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
48% identity, 92% coverage: 35:500/507 of query aligns to 37:498/498 of 4pxnA
- active site: N161 (= N159), K184 (= K182), E262 (= E261), C296 (= C295), E392 (= E394), E472 (= E474)
- binding nicotinamide-adenine-dinucleotide: I157 (= I155), T158 (≠ S156), A159 (= A157), F160 (= F158), N161 (= N159), K184 (= K182), T221 (≠ R220), G224 (= G223), Q225 (≠ E224), F238 (≠ A237), T239 (= T238), G240 (= G239), S241 (= S240), A244 (≠ M243), V248 (= V247), E262 (= E261), L263 (= L262), S264 (≠ G263), C296 (= C295), E392 (= E394), F394 (= F396), F461 (= F463)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
49% identity, 90% coverage: 53:506/507 of query aligns to 59:509/509 of 4zulA
- active site: N165 (= N159), K188 (= K182), E266 (= E261), C300 (= C295), E397 (= E394), E477 (= E474)
- binding 2-aminohexanedioic acid: E119 (= E113), F166 (= F160), R299 (= R294), C300 (= C295), T301 (= T296), G459 (= G456), A460 (= A457), F466 (= F463)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
49% identity, 90% coverage: 53:506/507 of query aligns to 59:509/509 of 4x0tA
- active site: N165 (= N159), K188 (= K182), E266 (= E261), C300 (= C295), E397 (= E394), E477 (= E474)
- binding 4-(diethylamino)benzaldehyde: F166 (= F160), V170 (= V164), W173 (= W167), C300 (= C295), F466 (= F463)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S156), A163 (= A157), F164 (= F158), N165 (= N159), K188 (= K182), G189 (≠ P183), A190 (≠ S184), A225 (≠ R220), G228 (= G223), T229 (≠ E224), F242 (≠ A237), T243 (= T238), G244 (= G239), S245 (= S240), V248 (≠ M243), E266 (= E261), L267 (= L262), C300 (= C295), E397 (= E394), F399 (= F396)
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, 90% coverage: 53:506/507 of query aligns to 89:539/539 of P49419
- 110:539 (vs. 74:506, 50% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 156:158) binding
- A199 (= A163) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K182) binding
- GT 258:259 (≠ GE 223:224) binding
- GS 274:275 (= GS 239:240) binding
- EL 296:297 (= EL 261:262) binding
- C330 (= C295) active site, Nucleophile
- E427 (= E394) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ N406) to Q: in dbSNP:rs12514417
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
49% identity, 90% coverage: 53:506/507 of query aligns to 60:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
49% identity, 87% coverage: 53:494/507 of query aligns to 59:497/497 of 2j6lA
- active site: N165 (= N159), K188 (= K182), E266 (= E261), C300 (= C295), E397 (= E394), E477 (= E474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I155), T162 (≠ S156), A163 (= A157), F164 (= F158), N165 (= N159), K188 (= K182), A225 (≠ R220), G228 (= G223), T229 (≠ E224), F242 (≠ A237), T243 (= T238), G244 (= G239), S245 (= S240), V248 (≠ M243), E266 (= E261), L267 (= L262), C300 (= C295), E397 (= E394), F399 (= F396)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
47% identity, 87% coverage: 53:494/507 of query aligns to 59:487/487 of 4x0uD
- active site: N165 (= N159), K188 (= K182), E266 (= E261), C300 (= C295), E397 (= E394), E467 (= E474)
- binding 4-(diethylamino)benzaldehyde: F166 (= F160), A169 (= A163), V170 (= V164), C300 (= C295), F456 (= F463), H461 (≠ E468)
- binding magnesium ion: E119 (= E113), D122 (= D116)
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, 90% coverage: 48:501/507 of query aligns to 48:510/511 of 6fkuA
- active site: N159 (= N159), E261 (= E261), C295 (= C295), E483 (= E474)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I155), T156 (≠ S156), N159 (= N159), K182 (= K182), S184 (= S184), E185 (= E185), G214 (≠ A219), G215 (≠ R220), K216 (≠ D221), G220 (vs. gap), Q221 (vs. gap), F237 (≠ A237), T238 (= T238), G239 (= G239), S240 (= S240), V243 (≠ M243), E261 (= E261), L262 (= L262), C295 (= C295), R342 (≠ A341), F343 (≠ A342), E404 (= E394), F406 (= F396)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 92% coverage: 30:493/507 of query aligns to 19:477/477 of 6j76A
- active site: N148 (= N159), E246 (= E261), C280 (= C295), E458 (= E474)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I155), T145 (≠ S156), A146 (= A157), W147 (≠ F158), N148 (= N159), K171 (= K182), T173 (≠ S184), S174 (≠ E185), G204 (≠ A219), G208 (= G223), T223 (= T238), G224 (= G239), S225 (= S240), A228 (≠ M243), S231 (≠ A246), I232 (≠ V247), E246 (= E261), L247 (= L262), C280 (= C295), E381 (= E394), F383 (= F396), H447 (≠ F463)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 92% coverage: 32:498/507 of query aligns to 23:484/489 of 4o6rA
- active site: N150 (= N159), K173 (= K182), E248 (= E261), C282 (= C295), E383 (= E394), E460 (= E474)
- binding adenosine monophosphate: I146 (= I155), V147 (≠ S156), K173 (= K182), G206 (≠ A219), G210 (= G223), Q211 (≠ E224), F224 (≠ A237), G226 (= G239), S227 (= S240), T230 (≠ M243), R233 (≠ A246)
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)
28% identity, 93% coverage: 20:491/507 of query aligns to 17:485/494 of P49189
- C116 (≠ I117) 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
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
28% identity, 93% coverage: 20:491/507 of query aligns to 16:484/493 of 6vr6D
- active site: N156 (= N159), E253 (= E261), C287 (= C295), E467 (= E474)
- binding nicotinamide-adenine-dinucleotide: I152 (= I155), G153 (≠ S156), W155 (≠ F158), K179 (= K182), A212 (≠ R220), G215 (= G223), Q216 (≠ E224), F229 (≠ A237), G231 (= G239), S232 (= S240), T235 (≠ M243), I239 (≠ V247)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
30% identity, 94% coverage: 13:491/507 of query aligns to 27:494/503 of 1bpwA
- active site: N166 (= N159), K189 (= K182), E263 (= E261), C297 (= C295), E400 (= E394), E477 (= E474)
- binding nicotinamide-adenine-dinucleotide: I162 (= I155), L163 (≠ S156), W165 (≠ F158), N166 (= N159), K189 (= K182), G221 (≠ A219), G225 (= G223), T240 (= T238), G241 (= G239), S242 (= S240), T245 (≠ M243), E263 (= E261), L264 (= L262), C297 (= C295), E400 (= E394), F402 (= F396), F466 (= F463)
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)
30% identity, 94% coverage: 13:491/507 of query aligns to 27:494/503 of P56533
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 91% coverage: 24:485/507 of query aligns to 19:473/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (= E261), C288 (= C295), E385 (= E394), E462 (= E474)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A157), W155 (≠ F158), K179 (= K182), A181 (≠ S184), S182 (≠ E185), A212 (≠ R220), G216 (= G223), G232 (= G239), S233 (= S240), I236 (≠ M243), C288 (= C295), K338 (≠ A345), E385 (= E394), F387 (= F396)
Query Sequence
>CCNA_01274 FitnessBrowser__Caulo:CCNA_01274
MTQVFPTPAAHAREILAKLGAPPLPADAGEPVRGPIDGAILGHVVYDDARQIEAKVAAAC
RAFADWRVVPAPRRGELVRLFGEELRAAKADLAALVTLEAGKIASEAAGEVQEMIDICDF
AVGLSRQLHGLTIASERPGHAMRETWHPLGPVAVISAFNFPVAVWAWNACLALVCGDPVI
WKPSEKTPLTALATQAILERALARFRDAPQGLSSVVLGARDAGERLARDPRIPLVSATGS
TRMGRAVAPMVAERFGRSILELGGNNAMIVTPSADLSLALRAIVFSAAGTAGQRCTSLRR
LIVHESLVDKVSDAVEAAFQRLSVGDPRDPKTLLGPLIDKAAYDAFIAAMNQVRAEGGSV
AGGERVLIDEHPDAYYVRPALARLPAPAPCMQRETFAPLLHVVPYNSFDMAIAIQNDVPQ
GLSSCVMTNDVREAERFLAAAGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDSW
KQYMRRQTATVNYSGALPLAQGVRFDL
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