SitesBLAST
Comparing WP_068004977.1 NCBI__GCF_001623255.1:WP_068004977.1 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
65% identity, 97% coverage: 16:511/512 of query aligns to 6:504/504 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, 96% coverage: 16:509/512 of query aligns to 15:507/508 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, 96% coverage: 16:509/512 of query aligns to 16:508/509 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, 96% coverage: 16:509/512 of query aligns to 15:504/505 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)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
51% identity, 93% coverage: 30:504/512 of query aligns to 29:498/498 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)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
49% identity, 94% coverage: 30:509/512 of query aligns to 34:509/509 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)
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)
48% identity, 96% coverage: 19:510/512 of query aligns to 50:539/539 of P49419
- 110:539 (vs. 77:510, 51% identical) natural variant: Missing (in EPEO4; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 159:161) binding NAD(+)
- A199 (= A166) to V: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K185) binding NAD(+)
- GT 258:259 (≠ GE 227:228) binding NAD(+)
- GS 274:275 (= GS 243:244) binding NAD(+)
- EL 296:297 (= EL 265:266) binding NAD(+)
- C330 (= C299) active site, Nucleophile
- E427 (= E398) binding NAD(+); to Q: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ T410) to Q: in dbSNP:rs12514417
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
48% identity, 96% coverage: 19:510/512 of query aligns to 20:509/509 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)
48% identity, 96% coverage: 19:510/512 of query aligns to 20:509/509 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)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
48% identity, 96% coverage: 19:510/512 of query aligns to 21:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
48% identity, 94% coverage: 19:498/512 of query aligns to 20:497/497 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)
46% identity, 94% coverage: 19:498/512 of query aligns to 20:487/487 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)
32% identity, 93% coverage: 28:505/512 of query aligns to 24:510/511 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 (= G223), G215 (≠ R224), K216 (≠ D225), G220 (vs. gap), Q221 (vs. gap), F237 (≠ A241), T238 (= T242), G239 (= G243), S240 (= S244), V243 (≠ M247), E261 (= E265), L262 (= L266), C295 (= C299), R342 (≠ D345), F343 (≠ A346), E404 (= E398), F406 (= F400)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
30% identity, 91% coverage: 30:497/512 of query aligns to 16:477/477 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 (= G223), G208 (= G227), T223 (= T242), G224 (= G243), S225 (= S244), A228 (≠ M247), S231 (≠ Q250), I232 (≠ V251), E246 (= E265), L247 (= L266), C280 (= C299), E381 (= E398), F383 (= F400), H447 (≠ F467)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 90% coverage: 29:488/512 of query aligns to 23:472/481 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 (≠ N349), 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)
31% identity, 90% coverage: 29:488/512 of query aligns to 24:473/482 of P25526
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 93% coverage: 27:502/512 of query aligns to 15:484/489 of 4o6rA
- active site: N150 (= N162), K173 (= K185), E248 (= E265), C282 (= C299), E383 (= E398), E460 (= E478)
- binding adenosine monophosphate: I146 (= I158), V147 (≠ S159), K173 (= K185), G206 (= G223), G210 (= G227), Q211 (≠ E228), F224 (≠ A241), G226 (= G243), S227 (= S244), T230 (≠ M247), R233 (≠ Q250)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
29% identity, 94% coverage: 30:508/512 of query aligns to 22:490/490 of 5ekcE
- active site: N154 (= N162), K177 (= K185), E252 (= E265), C286 (= C299), E381 (= E398), E459 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I158), T151 (≠ S159), P152 (≠ A160), W153 (≠ F161), K177 (= K185), S180 (≠ E188), G210 (= G223), G214 (= G227), F228 (≠ A241), G230 (= G243), E231 (≠ S244), T234 (≠ M247), N331 (≠ D343), R333 (≠ D345), Q334 (≠ A346)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
29% identity, 91% coverage: 30:495/512 of query aligns to 15:471/482 of 5ek6A
- active site: N147 (= N162), K170 (= K185), E245 (= E265), C279 (= C299), E374 (= E398), E452 (= E478)
- binding 2-methylpropanal: I152 (≠ V167), K155 (≠ W170), T222 (= T242), E245 (= E265), F441 (= F467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I158), T144 (≠ S159), W146 (≠ F161), N147 (= N162), I152 (≠ V167), K170 (= K185), A172 (≠ S187), S173 (≠ E188), P202 (vs. gap), G203 (= G223), G207 (= G227), F221 (≠ A241), T222 (= T242), G223 (= G243), E224 (≠ S244), T227 (≠ M247), I231 (≠ V251), E245 (= E265), L246 (= L266), C279 (= C299), E374 (= E398)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
29% identity, 91% coverage: 30:495/512 of query aligns to 15:471/482 of 4h73A
- active site: N147 (= N162), K170 (= K185), E245 (= E265), C279 (= C299), E374 (= E398), E452 (= E478)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I158), T144 (≠ S159), P145 (≠ A160), W146 (≠ F161), K170 (= K185), A172 (≠ S187), S173 (≠ E188), G203 (= G223), G207 (= G227), F221 (≠ A241), G223 (= G243), E224 (≠ S244), T227 (≠ M247)
Query Sequence
>WP_068004977.1 NCBI__GCF_001623255.1:WP_068004977.1
MTVGLDTAQFTQETIELMERMGVTRASLEGGTLAATSPISGETLAMVKEDSVEETSVAIG
RAHDAFKQWRKLPSPRRGELVRLLGEELRTYKNDLGKLVSLEAGKITSEGLGEVQEMIDI
CDFAVGLSRQLYGLTIATERPGHRMMETWHSSGVVGVISAFNFPVAVWSWNAALAFVCGD
SVVWKPSEKTPLTALAVQALYKRAAAKFGEEAPAGLMEVIQGGRDVGETLVDDKRVPVIS
ATGSTRMGRQVGPRVAERFGKSILELGGNNAAIVTPSADLDLTLRGVAFSAMGTCGQRCT
TLRRLITHDSVYDALIPRLIKAYSSVKIGVPTEDDTLIGPLIDKDAFDNMQKALEAAKAA
GGKVHGGQRVLSKEFPEAYYVQPAIVEMPGQVGPVLEETFAPILYVVRYTDFDEAIEIQN
GVGAGLSSSIFTKDIGEAETFVSVVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGREAG
SDAWKAYMRRATNTINYSGALPLAQGVKFDVE
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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