SitesBLAST
Comparing H281DRAFT_00370 FitnessBrowser__Burk376:H281DRAFT_00370 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)
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
86% identity, 100% coverage: 1:531/531 of query aligns to 2:529/529 of 2y53A
- active site: N160 (= N159), K183 (= K182), Q258 (≠ E257), C297 (= C296), E401 (= E400), L495 (= L497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I155), N157 (= N156), F159 (= F158), N160 (= N159), K183 (= K182), A185 (= A184), T186 (= T185), S217 (= S216), F232 (= F231), G234 (= G233), S235 (= S234), A236 (= A235), T238 (= T237), A259 (= A258), D260 (= D259), C297 (= C296), F403 (= F402)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
87% identity, 96% coverage: 1:509/531 of query aligns to 2:508/521 of 2vroA
- active site: N160 (= N159), K183 (= K182), E258 (= E257), C297 (= C296), E401 (= E400), L496 (= L497)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I155), K183 (= K182), S217 (= S216), S235 (= S234), T238 (= T237), L242 (= L241), F403 (= F402)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
44% identity, 98% coverage: 2:524/531 of query aligns to 1:511/681 of P77455
- E256 (= E257) 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)
44% identity, 98% coverage: 3:524/531 of query aligns to 1:510/678 of 6jqoA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding crotonyl coenzyme a: V97 (= V100), F107 (≠ S110), S111 (≠ R114), F158 (= F160), W161 (= W163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N156), F156 (= F158), N157 (= N159), T183 (= T185), T230 (= T232), G231 (= G233), S232 (= S234), T235 (= T237), A256 (= A258), D257 (= D259), C294 (= C296)
Sites not aligning to the query:
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
44% identity, 98% coverage: 3:524/531 of query aligns to 1:510/678 of 6jqnA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ H21), I153 (= I155), N154 (= N156), A155 (= A157), F156 (= F158), K180 (= K182), A182 (= A184), T183 (= T185), T230 (= T232), G231 (= G233), S232 (= S234), T235 (= T237), L239 (= L241), E255 (= E257), A256 (= A258), D257 (= D259), C294 (= C296), F396 (= F402), H471 (= H485)
Sites not aligning to the query:
6jqmA Structure of paaz with NADPH (see paper)
44% identity, 98% coverage: 3:524/531 of query aligns to 1:510/678 of 6jqmA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ H21), I153 (= I155), N154 (= N156), A155 (= A157), F156 (= F158), N157 (= N159), K180 (= K182), A182 (= A184), T183 (= T185), G231 (= G233), S232 (= S234), T235 (= T237), A256 (= A258), D257 (= D259), C294 (= C296), E394 (= E400), F396 (= F402)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
26% identity, 77% coverage: 1:411/531 of query aligns to 2:391/454 of 3ty7B
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
25% identity, 76% coverage: 64:467/531 of query aligns to 81:461/503 of 1bpwA
- active site: N166 (= N159), K189 (= K182), E263 (≠ N255), C297 (= C296), E400 (= E400)
- binding nicotinamide-adenine-dinucleotide: I162 (= I155), L163 (≠ N156), W165 (≠ F158), N166 (= N159), K189 (= K182), G221 (= G215), G225 (≠ A217), T240 (= T232), G241 (= G233), S242 (= S234), T245 (= T237), E263 (≠ N255), L264 (≠ V256), C297 (= C296), E400 (= E400), F402 (= F402)
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)
25% identity, 76% coverage: 64:467/531 of query aligns to 81:461/503 of P56533
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)
25% identity, 85% coverage: 63:513/531 of query aligns to 69:484/497 of P17202
- D96 (≠ N90) binding
- SPW 156:158 (≠ NAF 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAT 182:185) binding
- L186 (≠ A186) binding
- SSAT 236:239 (≠ SAET 234:237) binding
- V251 (= V249) binding in other chain
- L258 (≠ V256) binding
- W285 (vs. gap) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E400) binding
- A441 (≠ H459) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S468) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H485) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G489) binding
Sites not aligning to the query:
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, 85% coverage: 4:455/531 of query aligns to 9:438/487 of Q9H2A2
- R109 (≠ G104) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N159) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
24% identity, 82% coverage: 64:498/531 of query aligns to 71:469/493 of 6vr6D
- active site: N156 (= N159), E253 (≠ N255), C287 (= C296), E467 (= E496)
- binding nicotinamide-adenine-dinucleotide: I152 (= I155), G153 (≠ N156), W155 (≠ F158), K179 (= K182), A212 (≠ S216), G215 (≠ L219), Q216 (≠ L220), F229 (= F231), G231 (= G233), S232 (= S234), T235 (= T237), I239 (≠ L241)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
24% identity, 82% coverage: 64:498/531 of query aligns to 72:470/494 of P49189
- C116 (≠ T108) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
25% identity, 85% coverage: 63:513/531 of query aligns to 67:482/495 of 4v37A
- active site: N157 (= N159), K180 (= K182), E255 (≠ N255), A289 (≠ C296), E388 (= E400), E465 (= E496)
- binding 3-aminopropan-1-ol: C448 (≠ S468), W454 (≠ H485)
- binding nicotinamide-adenine-dinucleotide: I153 (= I155), S154 (≠ N156), P155 (≠ A157), W156 (≠ F158), N157 (= N159), M162 (vs. gap), K180 (= K182), S182 (≠ A184), E183 (≠ T185), G213 (vs. gap), G217 (≠ S216), A218 (= A217), T232 (= T232), G233 (= G233), S234 (= S234), T237 (= T237), E255 (≠ N255), L256 (≠ V256), A289 (≠ C296), E388 (= E400), F390 (= F402)
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
26% identity, 84% coverage: 1:444/531 of query aligns to 1:413/475 of Q59931
- R103 (≠ G104) binding
- S151 (≠ N156) binding
- K177 (= K182) binding
- T180 (= T185) binding
- D215 (= D221) binding
- 230:251 (vs. 233:258, 19% identical) binding
- E377 (= E400) binding
Sites not aligning to the query:
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
26% identity, 83% coverage: 6:444/531 of query aligns to 5:412/474 of 2esdA
- active site: N153 (= N159), K176 (= K182), A249 (≠ V249), C283 (= C296), E376 (= E400)
- binding glyceraldehyde-3-phosphate: R102 (≠ G104), Y154 (≠ F160), R282 (≠ K295), C283 (= C296), T284 (= T297)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (= F158), K176 (= K182), P178 (≠ A184), T179 (= T185), G209 (≠ S216), G213 (≠ L220), D214 (= D221), F227 (= F231), S230 (= S234), I233 (≠ T237), K328 (≠ A342), S329 (≠ Q343), Y332 (≠ N346)
Sites not aligning to the query:
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
27% identity, 83% coverage: 6:444/531 of query aligns to 5:412/474 of 1qi1B
- active site: N153 (= N159), K176 (= K182), E249 (= E257), S283 (≠ C296), E376 (= E400)
- binding sn-glycerol-3-phosphate: Y154 (≠ F160), R282 (≠ K295), S283 (≠ C296), T284 (= T297)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (≠ A157), F152 (= F158), N153 (= N159), L158 (≠ G164), K176 (= K182), P178 (≠ A184), T179 (= T185), G209 (≠ S216), G213 (≠ L220), G229 (= G233), S230 (= S234), I233 (≠ T237), E249 (= E257), L250 (≠ A258), S283 (≠ C296)
Sites not aligning to the query:
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 77% coverage: 5:411/531 of query aligns to 3:398/483 of 4npiA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E387 (= E400)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (≠ G104), L157 (≠ G164), W160 (≠ E167), E251 (= E257), C285 (= C296)
- binding nicotinamide-adenine-dinucleotide: I148 (= I155), S149 (≠ N156), P150 (≠ A157), W151 (≠ F158), K175 (= K182), E178 (≠ T185), G208 (vs. gap), G213 (= G218), E214 (vs. gap), F227 (= F231), G229 (= G233), E230 (≠ S234), T233 (= T237), G253 (≠ D259), C285 (= C296), K335 (≠ N346), E387 (= E400), F389 (= F402)
Sites not aligning to the query:
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 77% coverage: 5:411/531 of query aligns to 3:398/483 of 4i2rA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E387 (= E400)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (≠ G104), L157 (≠ G164), C285 (= C296)
- binding nicotinamide-adenine-dinucleotide: I148 (= I155), S149 (≠ N156), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (≠ T185), G208 (vs. gap), F227 (= F231), T228 (= T232), G229 (= G233), E230 (≠ S234), T233 (= T237), E251 (= E257), L252 (≠ A258), G253 (≠ D259), C285 (= C296), E387 (= E400), F389 (= F402)
Sites not aligning to the query:
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
25% identity, 77% coverage: 5:411/531 of query aligns to 3:398/483 of 4i25A
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E387 (= E400)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (≠ G104), L157 (≠ G164), C285 (= C296)
- binding nicotinamide-adenine-dinucleotide: I148 (= I155), S149 (≠ N156), P150 (≠ A157), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (≠ T185), G208 (vs. gap), G213 (= G218), F227 (= F231), T228 (= T232), G229 (= G233), E230 (≠ S234), T233 (= T237), E251 (= E257), L252 (≠ A258), C285 (= C296), E387 (= E400), F389 (= F402)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_00370 FitnessBrowser__Burk376:H281DRAFT_00370
MIELLKNHVAGEWVAGTGDGHTLTDPVTGEALVRVSSEGLDLSHAFRFARDEAGPSLRAL
TYAERAARLADVVKLLQSKRDDYYAIALANSGTTRNDSAVDIDGGIFTLSYYARLGASLG
NVHALRDGNASALSKDQSFSVQHVLTPTRGVALFINAFNFPSWGLWEKAAPALLSGLPVI
VKPATATAWLTQRMIADVVDAGILPRGALSVICGGSAGLLDQVQAFDVVSFTGSAETAAS
LRAHPAFVVRGARLNVEADSLNSAILCADATPDTPAFDLFIKEVVREMTVKSGQKCTAIR
RAFVPDTALDAVVDALKTKLAKITVGNPRNDAVRMGSLVSRAQYENVLAGIAALRQEAVL
AYDGSAAPLIDADAAVAACIAPHLFVVNDPDNATLLHDVEVFGPVASVAPYCVANGAGEL
REAHAVDLARRGQGSLVASIYSNDDAHLGRLALELADSHGRVHAVSPSVEQSQTGHGNVM
PMSLHGGPGRAGGGEELGGLRALGFYHRRSAIQASAAAIDAVAQLTHLPTA
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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