SitesBLAST
Comparing GFF2643 FitnessBrowser__Phaeo:GFF2643 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)
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
51% identity, 99% coverage: 5:675/676 of query aligns to 2:672/678 of 6jqoA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding crotonyl coenzyme a: V97 (≠ I100), F107 (= F110), S111 (= S114), F158 (= F161), W161 (= W164), R638 (≠ D647)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N157), F156 (= F159), N157 (= N160), T183 (= T186), T230 (= T233), G231 (= G234), S232 (= S235), T235 (= T238), A256 (≠ Q259), D257 (= D260), C294 (= C297)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
51% identity, 99% coverage: 5:675/676 of query aligns to 2:672/678 of 6jqnA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding octanoyl-coenzyme a: F562 (= F570), H565 (= H573), F576 (= F585), G583 (= G592), V595 (= V604), A604 (= A613), N605 (= N614), Y606 (≠ T615), F613 (= F622), I614 (≠ M623)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (= R22), I153 (= I156), N154 (= N157), A155 (= A158), F156 (= F159), K180 (= K183), A182 (= A185), T183 (= T186), T230 (= T233), G231 (= G234), S232 (= S235), T235 (= T238), L239 (= L242), E255 (= E258), A256 (≠ Q259), D257 (= D260), C294 (= C297), F396 (= F404), H471 (= H479)
6jqmA Structure of paaz with NADPH (see paper)
51% identity, 99% coverage: 5:675/676 of query aligns to 2:672/678 of 6jqmA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (= R22), I153 (= I156), N154 (= N157), A155 (= A158), F156 (= F159), N157 (= N160), K180 (= K183), A182 (= A185), T183 (= T186), G231 (= G234), S232 (= S235), T235 (= T238), A256 (≠ Q259), D257 (= D260), C294 (= C297), E394 (= E402), F396 (= F404)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
51% identity, 99% coverage: 6:675/676 of query aligns to 4:673/681 of P77455
- E256 (= E258) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
44% identity, 69% coverage: 11:479/676 of query aligns to 11:483/529 of 2y53A
- active site: N160 (= N160), K183 (= K183), Q258 (≠ E258), C297 (= C297), E401 (= E402)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I156), N157 (= N157), F159 (= F159), N160 (= N160), K183 (= K183), A185 (= A185), T186 (= T186), S217 (≠ L217), F232 (= F232), G234 (= G234), S235 (= S235), A236 (= A236), T238 (= T238), A259 (≠ Q259), D260 (= D260), C297 (= C297), F403 (= F404)
Sites not aligning to the query:
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
44% identity, 69% coverage: 11:479/676 of query aligns to 11:484/521 of 2vroA
- active site: N160 (= N160), K183 (= K183), E258 (= E258), C297 (= C297), E401 (= E402)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I156), K183 (= K183), S217 (≠ L217), S235 (= S235), T238 (= T238), L242 (= L242), F403 (= F404)
Sites not aligning to the query:
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
30% identity, 44% coverage: 151:446/676 of query aligns to 139:424/454 of 3ty7B
Sites not aligning to the query:
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
26% identity, 65% coverage: 62:501/676 of query aligns to 77:486/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (= E258), C298 (= C297), E399 (= E402), E476 (= E490)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A158), K189 (= K183), E192 (≠ T186), G222 (vs. gap), G226 (= G218), G242 (= G234), G243 (≠ S235), T246 (= T238), H249 (≠ K241), I250 (≠ L242), C298 (= C297), E399 (= E402), F401 (= F404)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
27% identity, 66% coverage: 64:506/676 of query aligns to 67:475/483 of 3b4wA
- active site: N154 (= N160), K177 (= K183), E251 (= E250), C285 (= C297), E384 (= E402), E460 (≠ A485)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), V151 (≠ N157), W153 (≠ F159), N154 (= N160), K177 (= K183), I210 (≠ L217), G213 (= G218), T228 (= T233), G229 (= G234), S230 (= S235), V233 (≠ T238), E236 (≠ K241), E251 (= E250), L252 (vs. gap), C285 (= C297), E384 (= E402), F386 (= F404)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
31% identity, 53% coverage: 151:508/676 of query aligns to 145:479/485 of 6x9lA
- active site: N154 (= N160), E252 (= E258), A286 (≠ C297), E462 (= E490)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), T151 (≠ N157), W153 (≠ F159), N154 (= N160), Q159 (≠ G165), K177 (= K183), E180 (≠ T186), G210 (≠ L217), P211 (vs. gap), G214 (vs. gap), T229 (= T233), G230 (= G234), S231 (= S235), E252 (= E258), L253 (≠ Q259), A286 (≠ C297), E386 (= E402), F388 (= F404), F451 (≠ H479)
- binding octanal: W155 (≠ F161), S285 (≠ K296)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
25% identity, 60% coverage: 42:449/676 of query aligns to 24:419/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I156), L137 (≠ N157), F139 (= F159), K163 (= K183), S165 (≠ A185), I166 (≠ T186), S196 (vs. gap), G200 (= G218), G216 (= G234), S217 (= S235), T220 (= T238), I224 (≠ L242)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
25% identity, 60% coverage: 42:449/676 of query aligns to 24:419/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (= I156), L137 (≠ N157), F139 (= F159), K163 (= K183), S165 (≠ A185), I166 (≠ T186), S196 (vs. gap), G200 (= G218), G216 (= G234), S217 (= S235), T220 (= T238), I224 (≠ L242), L239 (≠ Q259), C272 (= C297), E368 (= E402), F370 (= F404)
P37685 Aldehyde dehydrogenase B; Acetaldehyde dehydrogenase; EC 1.2.1.4 from Escherichia coli (strain K12) (see paper)
26% identity, 74% coverage: 8:506/676 of query aligns to 27:500/512 of P37685
- R197 (≠ T186) mutation to E: Less than 10% of wild-type acetaldehyde dehydrogenase activity.
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
25% identity, 69% coverage: 39:502/676 of query aligns to 73:505/518 of Q63639
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
31% identity, 44% coverage: 151:448/676 of query aligns to 160:448/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I156), L166 (≠ N157), P167 (≠ A158), W168 (≠ F159), K192 (= K183), G225 (vs. gap), G229 (= G218), F243 (= F232), G245 (= G234), S246 (= S235), T249 (= T238), L252 (= L242), F253 (≠ R243), Y256 (≠ P246), C269 (≠ Q259), G270 (≠ D260), C303 (= C297), H350 (≠ Q344), K353 (≠ D347), F400 (= F404)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
24% identity, 69% coverage: 39:502/676 of query aligns to 47:479/492 of 6b5hA
- active site: N161 (= N160), E260 (= E258), C294 (= C297), E468 (= E490)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ I100), G116 (= G104), F162 (= F161), W169 (≠ E168), Q284 (≠ R287), F288 (≠ T291), T295 (= T298), N449 (≠ D462), L451 (≠ M464), N452 (≠ K465), F457 (≠ L474)
- binding nicotinamide-adenine-dinucleotide: I157 (= I156), I158 (≠ N157), W160 (≠ F159), N161 (= N160), K184 (= K183), G217 (vs. gap), G221 (≠ L217), F235 (= F232), T236 (= T233), G237 (= G234), S238 (= S235), V241 (≠ T238), E260 (= E258), L261 (≠ Q259), C294 (= C297), F393 (= F404)
1ky8A Crystal structure of the non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase (see paper)
25% identity, 67% coverage: 8:460/676 of query aligns to 19:449/499 of 1ky8A
- active site: N166 (= N160), K189 (= K183), E261 (= E258), C295 (= C297), E393 (= E402)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I156), T163 (≠ N157), F165 (= F159), N166 (= N160), K189 (= K183), S191 (≠ A185), I192 (≠ T186), P221 (≠ S214), G222 (= G215), A225 (≠ G218), E226 (≠ D219), F239 (= F232), T240 (= T233), G241 (= G234), S242 (= S235), V245 (≠ T238), E261 (= E258), L262 (≠ Q259), G263 (≠ D260), C295 (= C297), E393 (= E402), F395 (= F404)
Sites not aligning to the query:
O57693 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde phosphate dehydrogenase (NAD(P)); GAPN; EC 1.2.1.90 from Thermoproteus tenax (see 2 papers)
25% identity, 67% coverage: 8:460/676 of query aligns to 21:451/501 of O57693
- R72 (= R59) binding ; binding ; binding
- R79 (= R66) binding ; binding ; binding
- G134 (= G116) binding
- RR 154:155 (≠ RN 136:137) binding ; binding
- T165 (≠ N157) binding ; binding
- N168 (= N160) binding
- Y184 (≠ A176) binding
- K191 (= K183) binding
- KPSI 191:194 (≠ KPAT 183:186) binding
- G224 (= G215) binding
- E228 (≠ D219) binding ; binding
- S244 (= S235) binding ; binding
- G265 (≠ D260) binding ; binding
- RCD 296:298 (≠ KCT 296:298) binding
- E395 (= E402) binding ; binding
Sites not aligning to the query:
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
28% identity, 52% coverage: 151:503/676 of query aligns to 143:483/504 of 6dbbA
- active site: N152 (= N160), E259 (= E258), C293 (= C297), E471 (= E490)
- binding nicotinamide-adenine-dinucleotide: I148 (= I156), S149 (≠ N157), A150 (= A158), F151 (= F159), N152 (= N160), K175 (= K183), S177 (≠ A185), R218 (vs. gap), T236 (= T233), G237 (= G234), S238 (= S235), M241 (≠ T238), E259 (= E258), L260 (≠ Q259), G261 (≠ D260), C293 (= C297), E391 (= E402), F393 (= F404)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I156), S149 (≠ N157), A150 (= A158), F151 (= F159), N152 (= N160), K175 (= K183), S177 (≠ A185), R218 (vs. gap), T236 (= T233), G237 (= G234), S238 (= S235), M241 (≠ T238), E259 (= E258), L260 (≠ Q259), G261 (≠ D260), C293 (= C297), E391 (= E402), F393 (= F404)
1uxuA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 67% coverage: 8:460/676 of query aligns to 19:449/499 of 1uxuA
- active site: N166 (= N160), K189 (= K183), E261 (= E258), C295 (= C297), E393 (= E402)
- binding adenosine monophosphate: R70 (= R59), R77 (= R66), I131 (≠ K115), G132 (= G116), R152 (= R136), R153 (≠ N137)
- binding glyceraldehyde-3-phosphate: N166 (= N160), Y167 (≠ F161), R294 (≠ K296), C295 (= C297), D296 (≠ T298)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I156), T163 (≠ N157), P164 (≠ A158), F165 (= F159), K189 (= K183), S191 (≠ A185), I192 (≠ T186), P221 (≠ S214), G222 (= G215), E226 (≠ D219), G241 (= G234), S242 (= S235), V245 (≠ T238), E393 (= E402), F395 (= F404)
Sites not aligning to the query:
Query Sequence
>GFF2643 FitnessBrowser__Phaeo:GFF2643
MSLLDVSSFAAGQWIAPGAGARSIASAITGAPLAQAGNDALDVQGMLDYARTVGGPSLRK
LTFHDRARMLKALAGHLNQHKQALYDLSFNTGATQSDHMIDIDGGIGTMFVFASKGRREM
PDAHVYLDGDIEQLSRNGTFLGQHICTPLQGVAVHINAFNFPVWGMLEKLAPTLLAGVPA
IVKPATATCYVTELAVRLMLESGILPEGALQLVSGGLGDMLDHLTMQDVVSFTGSAQTAL
KLRANPVILENSIRFVAEQDSLNASILGPDAGPGTPEFDLFVKEVSREMTTKAGQKCTAI
RRIIAPDAQVEAVIEALSARLAKTRIGDPRLETTRMGALVSNSQKRDVLEKAAIIGQEAE
RVFGDPENFSVDGADAEKGAFVPPMLFHCADPDKAQRVHDTEAFGPVSTIMGYHDLDHAI
TLANRGEGSLVASVITHDTEVAREVALGAGAYHGRLYFNNRDSMKESTGHGSPLPHMVHG
GPGRAGGGEELGGVRGVKHYMQRTAIQGSPDILSAIGEQWVPGGTEIAAKVHPFTRKFGD
LELGETLHSAARQITLEDIETFAHFTGDTFYAHMDDEAAARNPFFPGRVAHGYLLISFAA
GLFVQPDEGPVLANTGLDNLRFMKPVSAGDSIKVRLTVKKKTPRNEDYGQVRWHVTLTNQ
DDEIAAEYELLTMNAF
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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