SitesBLAST
Comparing GFF3676 FitnessBrowser__Phaeo:GFF3676 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)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
35% identity, 94% coverage: 11:675/710 of query aligns to 4:674/681 of P77455
- E256 (≠ C261) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
35% identity, 94% coverage: 11:675/710 of query aligns to 3:673/678 of 6jqoA
- active site: N157 (≠ D163), E255 (≠ C261), C294 (≠ R300), L483 (≠ E490)
- binding crotonyl coenzyme a: V97 (≠ L105), F107 (≠ S115), S111 (≠ G119), F158 (≠ N164), W161 (≠ S167), R638 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (≠ T160), F156 (≠ L162), N157 (≠ D163), T183 (≠ P189), T230 (≠ A236), G231 (= G237), S232 (≠ F238), T235 (= T241), A256 (≠ E262), D257 (≠ T263), C294 (≠ R300)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
35% identity, 94% coverage: 11:675/710 of query aligns to 3:673/678 of 6jqnA
- active site: N157 (≠ D163), E255 (≠ C261), C294 (≠ R300), L483 (≠ E490)
- binding octanoyl-coenzyme a: F562 (= F568), H565 (= H571), F576 (= F583), G583 (= G590), V595 (= V602), A604 (= A611), N605 (= N612), Y606 (≠ I613), F613 (= F620), I614 (≠ H621)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q27), I153 (≠ V159), N154 (≠ T160), A155 (= A161), F156 (≠ L162), K180 (≠ C186), A182 (≠ D188), T183 (≠ P189), T230 (≠ A236), G231 (= G237), S232 (≠ F238), T235 (= T241), L239 (= L245), E255 (≠ C261), A256 (≠ E262), D257 (≠ T263), C294 (≠ R300), F396 (≠ Q402), H471 (≠ F478)
6jqmA Structure of paaz with NADPH (see paper)
35% identity, 94% coverage: 11:675/710 of query aligns to 3:673/678 of 6jqmA
- active site: N157 (≠ D163), E255 (≠ C261), C294 (≠ R300), L483 (≠ E490)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q27), I153 (≠ V159), N154 (≠ T160), A155 (= A161), F156 (≠ L162), N157 (≠ D163), K180 (≠ C186), A182 (≠ D188), T183 (≠ P189), G231 (= G237), S232 (≠ F238), T235 (= T241), A256 (≠ E262), D257 (≠ T263), C294 (≠ R300), E394 (≠ F400), F396 (≠ Q402)
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
35% identity, 57% coverage: 47:454/710 of query aligns to 42:460/529 of 2y53A
- active site: N160 (≠ D163), K183 (≠ C186), Q258 (≠ C261), C297 (≠ R300), E401 (≠ F400)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (≠ V159), N157 (≠ T160), F159 (≠ L162), N160 (≠ D163), K183 (≠ C186), A185 (≠ D188), T186 (≠ P189), S217 (≠ P220), F232 (= F235), G234 (= G237), S235 (≠ F238), A236 (≠ R239), T238 (= T241), A259 (≠ E262), D260 (≠ T263), C297 (≠ R300), F403 (≠ Q402)
Sites not aligning to the query:
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
35% identity, 57% coverage: 47:454/710 of query aligns to 42:461/521 of 2vroA
- active site: N160 (≠ D163), K183 (≠ C186), E258 (≠ C261), C297 (≠ R300), E401 (≠ F400)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (≠ V159), K183 (≠ C186), S217 (≠ P220), S235 (≠ F238), T238 (= T241), L242 (= L245), F403 (≠ Q402)
Sites not aligning to the query:
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
25% identity, 41% coverage: 154:447/710 of query aligns to 140:425/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
25% identity, 41% coverage: 154:447/710 of query aligns to 140:425/474 of 1wndA
Sites not aligning to the query:
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
25% identity, 41% coverage: 154:447/710 of query aligns to 140:425/474 of 1wnbB
- active site: N149 (≠ D163), K172 (≠ C186), E246 (= E262), C280 (≠ R300), E378 (≠ F400)
- binding betaine aldehyde: D279 (≠ R299)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ V159), A146 (≠ T160), W148 (≠ L162), K172 (≠ C186), G204 (≠ P220), G208 (≠ V224), D209 (= D225), T223 (≠ A236), G224 (= G237), S225 (≠ F238), T228 (= T241), H231 (≠ K244), G248 (= G264), E378 (≠ F400)
Sites not aligning to the query:
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
25% identity, 41% coverage: 154:447/710 of query aligns to 140:425/474 of 1wnbA
- active site: N149 (≠ D163), K172 (≠ C186), E246 (= E262), C280 (≠ R300), E378 (≠ F400)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ V159), A146 (≠ T160), W148 (≠ L162), K172 (≠ C186), G204 (≠ P220), G208 (≠ V224), D209 (= D225), G224 (= G237), S225 (≠ F238), T228 (= T241), H231 (≠ K244), G248 (= G264), F380 (≠ Q402)
Sites not aligning to the query:
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
27% identity, 40% coverage: 154:438/710 of query aligns to 145:422/483 of 3b4wA
- active site: N154 (≠ D163), K177 (≠ C186), E251 (= E262), C285 (≠ R300), E384 (≠ F400)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V159), V151 (≠ T160), W153 (≠ L162), N154 (≠ D163), K177 (≠ C186), I210 (≠ L223), G213 (≠ N226), T228 (≠ R239), G229 (≠ S240), S230 (≠ T241), V233 (≠ K244), E236 (≠ Q247), E251 (= E262), L252 (≠ T263), C285 (≠ R300), E384 (≠ F400), F386 (≠ Q402)
Sites not aligning to the query:
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
28% identity, 54% coverage: 61:445/710 of query aligns to 55:428/489 of 4o6rA
- active site: N150 (≠ D163), K173 (≠ C186), E248 (≠ C261), C282 (≠ R300), E383 (≠ F400)
- binding adenosine monophosphate: I146 (≠ V159), V147 (≠ T160), K173 (≠ C186), G206 (≠ N218), G210 (= G222), Q211 (vs. gap), F224 (= F235), G226 (= G237), S227 (= S240), T230 (≠ Q243), R233 (= R246)
Sites not aligning to the query:
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
24% identity, 60% coverage: 23:447/710 of query aligns to 34:447/503 of 1bpwA
- active site: N166 (≠ D163), K189 (≠ C186), E263 (≠ Q259), C297 (≠ R300), E400 (≠ Q398)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V159), L163 (≠ T160), W165 (≠ L162), N166 (≠ D163), K189 (≠ C186), G221 (= G230), G225 (vs. gap), T240 (≠ A236), G241 (= G237), S242 (≠ F238), T245 (= T241), E263 (≠ Q259), L264 (≠ S260), C297 (≠ R300), E400 (≠ Q398), F402 (= F400)
Sites not aligning to the query:
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)
24% identity, 60% coverage: 23:447/710 of query aligns to 34:447/503 of P56533
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
24% identity, 43% coverage: 154:458/710 of query aligns to 139:438/454 of 3ty7B
Sites not aligning to the query:
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
25% identity, 38% coverage: 154:422/710 of query aligns to 160:420/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (= V159), L166 (≠ T160), P167 (≠ A161), W168 (≠ L162), K192 (≠ C186), G225 (vs. gap), G229 (≠ N218), F243 (= F235), G245 (= G237), S246 (≠ F238), T249 (= T241), L252 (≠ K244), F253 (≠ L245), Y256 (≠ H248), C269 (≠ E262), G270 (≠ T263), C303 (≠ R300), H350 (= H347), K353 (≠ T350), F400 (= F400)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
27% identity, 33% coverage: 237:468/710 of query aligns to 216:456/504 of 6dbbA
- active site: E259 (vs. gap), C293 (≠ R300)
- binding nicotinamide-adenine-dinucleotide: R218 (= R239), T236 (= T253), G237 (= G254), S238 (≠ L255), M241 (≠ L258), E259 (vs. gap), L260 (vs. gap), G261 (vs. gap), C293 (≠ R300), E391 (≠ Q398), F393 (= F400)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: R218 (= R239), T236 (= T253), G237 (= G254), S238 (≠ L255), M241 (≠ L258), E259 (vs. gap), L260 (vs. gap), G261 (vs. gap), C293 (≠ R300), E391 (≠ Q398), F393 (= F400)
Sites not aligning to the query:
- active site: 152, 471
- binding nicotinamide-adenine-dinucleotide: 148, 149, 150, 151, 152, 175, 177
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: 148, 149, 150, 151, 152, 175, 177
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
24% identity, 58% coverage: 10:422/710 of query aligns to 9:413/487 of Q9H2A2
- R109 (≠ G109) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (≠ D163) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
24% identity, 52% coverage: 71:436/710 of query aligns to 69:424/495 of 4v37A
- active site: N157 (≠ D163), K180 (≠ C186), E255 (= E262), A289 (≠ R300), E388 (≠ F400)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V159), S154 (≠ T160), P155 (≠ A161), W156 (≠ L162), N157 (≠ D163), M162 (≠ G168), K180 (≠ C186), S182 (≠ D188), E183 (≠ P189), G213 (≠ N218), G217 (= G222), A218 (vs. gap), T232 (≠ A236), G233 (= G237), S234 (≠ F238), T237 (= T241), E255 (= E262), L256 (≠ T263), A289 (≠ R300), E388 (≠ F400), F390 (≠ Q402)
Sites not aligning to the query:
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)
24% identity, 52% coverage: 71:436/710 of query aligns to 71:426/497 of P17202
- D96 (≠ T95) binding
- SPW 156:158 (≠ TAL 160:162) binding
- Y160 (≠ N164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ E171) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ CPDP 186:189) binding
- L186 (≠ V190) binding
- SSAT 236:239 (≠ FRST 238:241) binding
- V251 (= V256) binding in other chain
- L258 (≠ T263) binding
- W285 (≠ L294) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (≠ F400) binding
Sites not aligning to the query:
- 28 binding
- 441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- 450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
Query Sequence
>GFF3676 FitnessBrowser__Phaeo:GFF3676
MTDHVKRPRFLQSLIAERWDHCGAQTQVFADAATNQPNAVLAYGSDDGIQAVDFARAVGG
PALRALGFQDRAQQLRAVARILKDNRAALYRESLTIGATRHDCALDVDGGIARLSALAGQ
ALKSLPNAPVLHLEDGIGPGSTTGRQQILAPLSGVALHVTALDNPVSGLLEQIAPALIAG
VPCIVCPDPVTACVSERLVKMIHDGQILPTGALQLIYNPPLGLVDNLSAGDAISFAGFRS
TAQKLRQHPAVATGLVRLQSCETGLSAAILGSDVAPGSQEYQFFLREIRSELILRAGQRR
HAVRRILLPRHREAEVLADLSVTLADTIVGVPDDAATQMGALVSRGHLETVQKALDELRH
GAEFVSDPIITPVETGGAFLSPVLLHCAKPANTPDVHQTFVQGPVATAMAYDSLCDAIAL
ANLAPCSRYSNVFTNDSPLAQEAAACLTSAEGQIRICGSEMARQASELSPDPSVPRLFAA
THHAQVCGAEDIRHAVAAYMMRTEIHAPPQLLTALTGRWVEGAETRHNGHPFRKSLETLR
IGDQLITETRQITEQDVEQFAHFTGDVFYAHMDREAARSHPFFDDRVAHGQLVVSFANGL
LVDPAPGPVLANIGSDNLRFHAPVYFGDCLHVRVTCKEITPRASAPFGDVRWDCCVLNAC
GVVVARFDLLTLVMKSWPPVPQDNVSEHKAAPHTAATPHRAQDPVQQPAE
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