SitesBLAST
Comparing WP_086509630.1 NCBI__GCF_002151265.1:WP_086509630.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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: 2:497/497 of query aligns to 4:503/504 of 6dbbA
- active site: N152 (= N150), E259 (= E253), C293 (= C287), E471 (= E465)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (≠ T147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R212), T236 (= T230), G237 (= G231), S238 (= S232), M241 (= M235), E259 (= E253), L260 (= L254), G261 (= G255), C293 (= C287), E391 (= E385), F393 (= F387)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I146), S149 (≠ T147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R212), T236 (= T230), G237 (= G231), S238 (= S232), M241 (= M235), E259 (= E253), L260 (= L254), G261 (= G255), C293 (= C287), E391 (= E385), F393 (= F387)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
61% identity, 99% coverage: 6:496/497 of query aligns to 17:507/508 of 6rttA
- active site: N161 (= N150), E262 (= E253), C296 (= C287), E476 (= E465)
- binding pyridine-2-carboxylic acid: A159 (= A148), F162 (= F151), V166 (≠ P155), W169 (= W158), G240 (= G231), S241 (= S232), R295 (= R286), C296 (= C287), T297 (= T288), E396 (= E385), F398 (= F387), P421 (= P410), K469 (= K458), E470 (= E459)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
61% identity, 99% coverage: 6:496/497 of query aligns to 18:508/509 of 6rtsA
- active site: N162 (= N150), E263 (= E253), C297 (= C287), E477 (= E465)
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), S159 (≠ T147), A160 (= A148), F161 (= F149), N162 (= N150), K185 (= K173), S187 (= S175), E188 (= E176), A222 (≠ R212), G225 (= G215), T240 (= T230), G241 (= G231), S242 (= S232), M245 (= M235), E263 (= E253), L264 (= L254), C297 (= C287), E397 (= E385), F399 (= F387)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
60% identity, 99% coverage: 6:496/497 of query aligns to 17:504/505 of 6rtuA
- active site: N161 (= N150), E259 (= E253), C293 (= C287), E473 (= E465)
- binding 2-aminohexanedioic acid: E115 (= E104), F162 (= F151), R292 (= R286), C293 (= C287), T294 (= T288), S454 (= S446), G455 (= G447), A456 (= A448), F462 (= F454)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
51% identity, 96% coverage: 21:496/497 of query aligns to 36:508/509 of 4zulA
- active site: N165 (= N150), K188 (= K173), E266 (= E253), C300 (= C287), E397 (= E385), E477 (= E465)
- binding 2-aminohexanedioic acid: E119 (= E104), F166 (= F151), R299 (= R286), C300 (= C287), T301 (= T288), G459 (= G447), A460 (= A448), F466 (= F454)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
51% identity, 96% coverage: 21:496/497 of query aligns to 36:508/509 of 4x0tA
- active site: N165 (= N150), K188 (= K173), E266 (= E253), C300 (= C287), E397 (= E385), E477 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), V170 (≠ P155), W173 (= W158), C300 (= C287), F466 (= F454)
- binding nicotinamide-adenine-dinucleotide: T162 (= T147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), G189 (≠ P174), A190 (≠ S175), A225 (≠ R212), G228 (= G215), T229 (≠ E216), F242 (≠ A229), T243 (= T230), G244 (= G231), S245 (= S232), V248 (≠ M235), E266 (= E253), L267 (= L254), C300 (= C287), 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: 21:496/497 of query aligns to 66:538/539 of P49419
- TAF 192:194 (= TAF 147:149) binding NAD(+)
- A199 (= A154) to V: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K173) binding NAD(+)
- GT 258:259 (≠ GE 215:216) binding NAD(+)
- GS 274:275 (= GS 231:232) binding NAD(+)
- EL 296:297 (= EL 253:254) binding NAD(+)
- C330 (= C287) active site, Nucleophile
- E427 (= E385) binding NAD(+); to Q: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ E397) to Q: in dbSNP:rs12514417
Sites not aligning to the query:
- 110:539 natural variant: Missing (in EPEO4; loss of alpha-AASA dehydrogenase activity)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
50% identity, 96% coverage: 21:496/497 of query aligns to 37:509/510 of 6o4dB
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
49% identity, 96% coverage: 21:496/497 of query aligns to 37:509/509 of 2jg7A
- active site: N166 (= N150), K189 (= K173), E267 (= E253), C301 (= C287), E398 (= E385), E478 (= E465)
- binding nicotinamide-adenine-dinucleotide: I162 (= I146), T163 (= T147), A164 (= A148), F165 (= F149), N166 (= N150), K189 (= K173), P192 (≠ E176), A226 (≠ R212), G229 (= G215), T230 (≠ E216), F243 (≠ A229), T244 (= T230), G245 (= G231), S246 (= S232), V249 (≠ M235), E267 (= E253), L268 (= L254), C301 (= C287), E398 (= E385), F400 (= F387)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
50% identity, 94% coverage: 21:485/497 of query aligns to 36:497/497 of 2j6lA
- active site: N165 (= N150), K188 (= K173), E266 (= E253), C300 (= C287), E397 (= E385), E477 (= E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I146), T162 (= T147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), A225 (≠ R212), G228 (= G215), T229 (≠ E216), F242 (≠ A229), T243 (= T230), G244 (= G231), S245 (= S232), V248 (≠ M235), E266 (= E253), L267 (= L254), C300 (= C287), E397 (= E385), F399 (= F387)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
48% identity, 95% coverage: 21:491/497 of query aligns to 32:498/498 of 4pxnA
- active site: N161 (= N150), K184 (= K173), E262 (= E253), C296 (= C287), E392 (= E385), E472 (= E465)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), T158 (= T147), A159 (= A148), F160 (= F149), N161 (= N150), K184 (= K173), T221 (≠ R212), G224 (= G215), Q225 (≠ E216), F238 (≠ A229), T239 (= T230), G240 (= G231), S241 (= S232), A244 (≠ M235), V248 (= V239), E262 (= E253), L263 (= L254), S264 (≠ G255), C296 (= C287), E392 (= E385), F394 (= F387), F461 (= F454)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
48% identity, 94% coverage: 21:485/497 of query aligns to 36:487/487 of 4x0uD
- active site: N165 (= N150), K188 (= K173), E266 (= E253), C300 (= C287), E397 (= E385), E467 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), A169 (= A154), V170 (≠ P155), C300 (= C287), F456 (= F454), H461 (≠ E459)
- binding magnesium ion: E119 (= E104), D122 (= D107)
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: 32:492/497 of query aligns to 41:510/511 of 6fkuA
- active site: N159 (= N150), E261 (= E253), C295 (= C287), E483 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I146), T156 (= T147), N159 (= N150), K182 (= K173), S184 (= S175), E185 (= E176), G214 (vs. gap), G215 (= G210), K216 (≠ E211), G220 (= G215), Q221 (≠ E216), F237 (≠ A229), T238 (= T230), G239 (= G231), S240 (= S232), V243 (≠ M235), E261 (= E253), L262 (= L254), C295 (= C287), R342 (≠ Q332), F343 (≠ A333), E404 (= E385), F406 (= F387)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
32% identity, 92% coverage: 17:475/497 of query aligns to 22:472/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E253), C288 (= C287), E385 (= E385), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A148), W155 (≠ F149), K179 (= K173), A181 (≠ S175), S182 (≠ E176), A212 (≠ R212), G216 (= G215), G232 (= G231), S233 (= S232), I236 (≠ M235), C288 (= C287), K338 (≠ T336), E385 (= E385), F387 (= F387)
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, 92% coverage: 17:475/497 of query aligns to 23:473/482 of P25526
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
30% identity, 95% coverage: 14:487/497 of query aligns to 18:489/497 of P17202
- I28 (≠ V24) binding K(+)
- D96 (≠ E90) binding K(+)
- SPW 156:158 (≠ TAF 147:149) binding NAD(+)
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 173:176) binding NAD(+)
- L186 (≠ K177) binding K(+)
- SSAT 236:239 (≠ STRM 232:235) binding NAD(+)
- V251 (≠ F247) binding in other chain
- L258 (= L254) binding NAD(+)
- W285 (≠ G281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding NAD(+)
- A441 (≠ I438) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A448) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F454) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K458) binding K(+)
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
31% identity, 92% coverage: 21:479/497 of query aligns to 2:449/453 of 4itbA
- active site: N130 (= N150), K153 (= K173), E227 (= E253), C261 (= C287), E358 (= E385), E435 (= E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (vs. gap), M127 (vs. gap), P128 (vs. gap), W129 (≠ F149), N130 (= N150), K153 (= K173), A155 (≠ S175), S156 (≠ E176), A186 (≠ R212), V189 (≠ G215), G205 (= G231), S206 (= S232), A209 (≠ M235), S212 (≠ E238), L228 (= L254), C261 (= C287), E358 (= E385), F360 (= F387)
- binding 4-oxobutanoic acid: E227 (= E253), C261 (= C287), S418 (≠ A448)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
32% identity, 95% coverage: 19:489/497 of query aligns to 19:484/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E253), C282 (= C287), E383 (= E385), E460 (= E465)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ T147), K173 (= K173), G206 (vs. gap), G210 (= G215), Q211 (≠ E216), F224 (≠ A229), G226 (= G231), S227 (= S232), T230 (≠ M235), R233 (≠ E238)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
30% identity, 95% coverage: 14:487/497 of query aligns to 16:487/495 of 4v37A
- active site: N157 (= N150), K180 (= K173), E255 (= E253), A289 (≠ C287), E388 (= E385), E465 (= E465)
- binding 3-aminopropan-1-ol: C448 (≠ A448), W454 (≠ F454)
- binding nicotinamide-adenine-dinucleotide: I153 (= I146), S154 (≠ T147), P155 (≠ A148), W156 (≠ F149), N157 (= N150), M162 (≠ P155), K180 (= K173), S182 (= S175), E183 (= E176), G213 (≠ R212), G217 (= G215), A218 (≠ E216), T232 (= T230), G233 (= G231), S234 (= S232), T237 (≠ M235), E255 (= E253), L256 (= L254), A289 (≠ C287), E388 (= E385), F390 (= F387)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
30% identity, 93% coverage: 23:484/497 of query aligns to 21:477/477 of 6j76A
- active site: N148 (= N150), E246 (= E253), C280 (= C287), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I146), T145 (= T147), A146 (= A148), W147 (≠ F149), N148 (= N150), K171 (= K173), T173 (≠ S175), S174 (≠ E176), G204 (≠ E211), G208 (= G215), T223 (= T230), G224 (= G231), S225 (= S232), A228 (≠ M235), S231 (≠ E238), I232 (≠ V239), E246 (= E253), L247 (= L254), C280 (= C287), E381 (= E385), F383 (= F387), H447 (≠ F454)
Query Sequence
>WP_086509630.1 NCBI__GCF_002151265.1:WP_086509630.1
MIDSLMQRLGVALEQYRNGDIAVVTPIDGSEIGRVRTATPAEVDTAIANAQRAFEAWRQV
PAPRRGELVRLFGDQLRRHKEDLGALVTWECGKILQEGLGEVQEMIDICDLAVGQSRQLY
GLTIASERPGHHMRESWHPLGPVGLITAFNFPVAPWAWNAALALVCGDSLLWKPSEKTPL
TALACQALLERAMAEFGDDAPQHLSQVIIGERAAGEQLTDDPRIPLISATGSTRMGREVG
PRVAARFGRSILELGGNNAMILTPSADLDMAVRAILFSAVGTAGQRCTTLRRLIVHRSIQ
AEVVARLKQSYAGISIGDPLVGNLIGPLIDRQAYDTMQTVLTQAREQGAEVYGGQRQLAE
RYPEGYYVAPAIVEIAGQNDLVRHETFAPILYVIGYETLDEAIALNNDVPQGLSSCIFTT
DVREAETFVSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDVWKSYMRRQTN
TVNYSRELPLAQGIKFD
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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