SitesBLAST
Comparing WP_057506719.1 NCBI__GCF_001431535.1:WP_057506719.1 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)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
57% identity, 99% coverage: 6:508/510 of query aligns to 13:509/509 of 2jg7A
- active site: N166 (= N163), K189 (= K186), E267 (= E264), C301 (= C298), E398 (= E397), E478 (= E477)
- binding nicotinamide-adenine-dinucleotide: I162 (= I159), T163 (≠ S160), A164 (= A161), F165 (= F162), N166 (= N163), K189 (= K186), P192 (≠ N189), A226 (≠ T223), G229 (≠ S226), T230 (≠ E227), F243 (= F240), T244 (= T241), G245 (= G242), S246 (= S243), V249 (= V246), E267 (= E264), L268 (= L265), C301 (= C298), E398 (= E397), F400 (= F399)
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)
56% identity, 99% coverage: 6:509/510 of query aligns to 42:539/539 of P49419
- 110:539 (vs. 78:509, 58% identical) natural variant: Missing (in EPEO4; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 160:162) binding NAD(+)
- A199 (= A167) to V: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K186) binding NAD(+)
- GT 258:259 (≠ SE 226:227) binding NAD(+)
- GS 274:275 (= GS 242:243) binding NAD(+)
- EL 296:297 (= EL 264:265) binding NAD(+)
- C330 (= C298) active site, Nucleophile
- E427 (= E397) binding NAD(+); to Q: in EPEO4; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ S409) to Q: in dbSNP:rs12514417
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
56% identity, 99% coverage: 6:509/510 of query aligns to 12:509/509 of 4zulA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E397), E477 (= E477)
- binding 2-aminohexanedioic acid: E119 (= E117), F166 (= F164), R299 (= R297), C300 (= C298), T301 (= T299), G459 (= G459), A460 (= A460), F466 (= F466)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
56% identity, 99% coverage: 6:509/510 of query aligns to 12:509/509 of 4x0tA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E397), E477 (= E477)
- binding 4-(diethylamino)benzaldehyde: F166 (= F164), V170 (= V168), W173 (= W171), C300 (= C298), F466 (= F466)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S160), A163 (= A161), F164 (= F162), N165 (= N163), K188 (= K186), G189 (≠ P187), A190 (≠ S188), A225 (≠ T223), G228 (≠ S226), T229 (≠ E227), F242 (= F240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (= V246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E397), F399 (= F399)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
56% identity, 99% coverage: 6:509/510 of query aligns to 13:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
56% identity, 96% coverage: 6:497/510 of query aligns to 12:497/497 of 2j6lA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E397), E477 (= E477)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I159), T162 (≠ S160), A163 (= A161), F164 (= F162), N165 (= N163), K188 (= K186), A225 (≠ T223), G228 (≠ S226), T229 (≠ E227), F242 (= F240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (= V246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E397), F399 (= F399)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
55% identity, 94% coverage: 31:510/510 of query aligns to 20:504/504 of 6dbbA
- active site: N152 (= N163), E259 (= E264), C293 (= C298), E471 (= E477)
- binding nicotinamide-adenine-dinucleotide: I148 (= I159), S149 (= S160), A150 (= A161), F151 (= F162), N152 (= N163), K175 (= K186), S177 (= S188), R218 (≠ N219), T236 (= T241), G237 (= G242), S238 (= S243), M241 (≠ V246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E397), F393 (= F399)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I159), S149 (= S160), A150 (= A161), F151 (= F162), N152 (= N163), K175 (= K186), S177 (= S188), R218 (≠ N219), T236 (= T241), G237 (= G242), S238 (= S243), M241 (≠ V246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E397), F393 (= F399)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
54% identity, 96% coverage: 6:497/510 of query aligns to 12:487/487 of 4x0uD
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E397), E467 (= E477)
- binding 4-(diethylamino)benzaldehyde: F166 (= F164), A169 (= A167), V170 (= V168), C300 (= C298), F456 (= F466), H461 (≠ D471)
- binding magnesium ion: E119 (= E117), D122 (= D120)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
51% identity, 98% coverage: 4:503/510 of query aligns to 5:498/498 of 4pxnA
- active site: N161 (= N163), K184 (= K186), E262 (= E264), C296 (= C298), E392 (= E397), E472 (= E477)
- binding nicotinamide-adenine-dinucleotide: I157 (= I159), T158 (≠ S160), A159 (= A161), F160 (= F162), N161 (= N163), K184 (= K186), T221 (= T223), G224 (≠ S226), Q225 (≠ E227), F238 (= F240), T239 (= T241), G240 (= G242), S241 (= S243), A244 (≠ V246), V248 (= V250), E262 (= E264), L263 (= L265), S264 (≠ G266), C296 (= C298), E392 (= E397), F394 (= F399), F461 (= F466)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
55% identity, 95% coverage: 27:508/510 of query aligns to 25:507/508 of 6rttA
- active site: N161 (= N163), E262 (= E264), C296 (= C298), E476 (= E477)
- binding pyridine-2-carboxylic acid: A159 (= A161), F162 (= F164), V166 (= V168), W169 (= W171), G240 (= G242), S241 (= S243), R295 (= R297), C296 (= C298), T297 (= T299), E396 (= E397), F398 (= F399), P421 (= P422), K469 (= K470), E470 (≠ D471)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
55% identity, 95% coverage: 27:508/510 of query aligns to 26:508/509 of 6rtsA
- active site: N162 (= N163), E263 (= E264), C297 (= C298), E477 (= E477)
- binding nicotinamide-adenine-dinucleotide: I158 (= I159), S159 (= S160), A160 (= A161), F161 (= F162), N162 (= N163), K185 (= K186), S187 (= S188), E188 (≠ N189), A222 (≠ T223), G225 (≠ S226), T240 (= T241), G241 (= G242), S242 (= S243), M245 (≠ V246), E263 (= E264), L264 (= L265), C297 (= C298), E397 (= E397), F399 (= F399)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
54% identity, 95% coverage: 27:508/510 of query aligns to 25:504/505 of 6rtuA
- active site: N161 (= N163), E259 (= E264), C293 (= C298), E473 (= E477)
- binding 2-aminohexanedioic acid: E115 (= E117), F162 (= F164), R292 (= R297), C293 (= C298), T294 (= T299), S454 (= S458), G455 (= G459), A456 (= A460), F462 (= F466)
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, 96% coverage: 16:504/510 of query aligns to 5:510/511 of 6fkuA
- active site: N159 (= N163), E261 (= E264), C295 (= C298), E483 (= E477)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I159), T156 (≠ S160), N159 (= N163), K182 (= K186), S184 (= S188), E185 (≠ N189), G214 (≠ I218), G215 (≠ N219), K216 (≠ D220), G220 (≠ A224), Q221 (≠ L225), F237 (= F240), T238 (= T241), G239 (= G242), S240 (= S243), V243 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), R342 (≠ G346), F343 (≠ A347), E404 (= E397), F406 (= F399)
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)
31% identity, 95% coverage: 14:498/510 of query aligns to 5:488/497 of P17202
- I28 (≠ V37) binding K(+)
- D96 (≠ E103) binding K(+)
- SPW 156:158 (≠ SAF 160:162) binding NAD(+)
- Y160 (≠ F164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W171) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSN 186:189) binding NAD(+)
- L186 (≠ K190) binding K(+)
- SSAT 236:239 (≠ STQV 243:246) binding NAD(+)
- V251 (≠ L258) binding in other chain
- L258 (= L265) binding NAD(+)
- W285 (≠ G292) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E397) binding NAD(+)
- A441 (≠ I450) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A460) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F466) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K470) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 95% coverage: 14:498/510 of query aligns to 3:486/495 of 4v37A
- active site: N157 (= N163), K180 (= K186), E255 (= E264), A289 (≠ C298), E388 (= E397), E465 (= E477)
- binding 3-aminopropan-1-ol: C448 (≠ A460), W454 (≠ F466)
- binding nicotinamide-adenine-dinucleotide: I153 (= I159), S154 (= S160), P155 (≠ A161), W156 (≠ F162), N157 (= N163), M162 (≠ V168), K180 (= K186), S182 (= S188), E183 (≠ N189), G213 (≠ I218), G217 (= G222), A218 (≠ T223), T232 (= T241), G233 (= G242), S234 (= S243), T237 (≠ V246), E255 (= E264), L256 (= L265), A289 (≠ C298), E388 (= E397), F390 (= F399)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
30% identity, 94% coverage: 19:496/510 of query aligns to 5:477/477 of 6j76A
- active site: N148 (= N163), E246 (= E264), C280 (= C298), E458 (= E477)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I159), T145 (≠ S160), A146 (= A161), W147 (≠ F162), N148 (= N163), K171 (= K186), T173 (≠ S188), S174 (≠ N189), G204 (= G222), G208 (≠ S226), T223 (= T241), G224 (= G242), S225 (= S243), A228 (≠ V246), S231 (≠ T249), I232 (≠ V250), E246 (= E264), L247 (= L265), C280 (= C298), E381 (= E397), F383 (= F399), H447 (≠ F466)
P54115 Magnesium-activated aldehyde dehydrogenase, cytosolic; Mg(2+)-activated acetaldehyde dehydrogenase; Mg(2+)-ACDH; EC 1.2.1.-; EC 1.2.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
29% identity, 91% coverage: 22:486/510 of query aligns to 31:490/500 of P54115
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 3 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8rwkA Cryoem structure of the central ald4 filament determined by filamentid (see paper)
29% identity, 89% coverage: 37:488/510 of query aligns to 41:485/495 of 8rwkA
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
30% identity, 92% coverage: 20:487/510 of query aligns to 13:472/481 of 3jz4A
- active site: N156 (= N163), K179 (= K186), E254 (= E264), C288 (= C298), E385 (= E397), E462 (= E477)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A161), W155 (≠ F162), K179 (= K186), A181 (≠ S188), S182 (≠ N189), A212 (≠ G222), G216 (≠ S226), G232 (= G242), S233 (= S243), I236 (≠ V246), C288 (= C298), K338 (≠ Q350), E385 (= E397), F387 (= F399)
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)
30% identity, 92% coverage: 20:487/510 of query aligns to 14:473/482 of P25526
Query Sequence
>WP_057506719.1 NCBI__GCF_001431535.1:WP_057506719.1
MSAKLLKALGLDAINAGTYLGNGEWSTATGGELITPVNPTTGEAIAQVRATTADEYETVI
ARAQEAFKIWRTTPAPRRGEAVRLCGEALRANKDALGSLVALEMGKSKPEGDGEVQEMID
IADFAVGQSRMLYGYTMHSERPGHRMYEQYQPLGLVGIISAFNFPVAVWAWNAFLATVCG
DICLWKPSNKTPLTAIASMRICNEALRDAGFPDLFFLINDAGTALSETMVADKRVPLISF
TGSTQVGRTVAEKVAHRLGRCLLELGGNNAIILDETADLKLAIPGIVFGAVGTAGQRCTT
TRRLIVHESIHDDVLATLVKAYKQVEGKIGDPTDPANLMGPLNSDGAVQQFLASIEKAKA
SGGTVQTGGTRIDRAGNFVLPAIVTGLKNSDEVVQHETFAPILYVMKYSTLDEAIDMQNG
VPQGLSSSIFTTNLKTAERFLSAAGSDCGIANVNIGTSGAEIGGAFGGEKDTGGGRESGS
DAWKVYMRRQTNTINYSDSLPLAQGIKFDL
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