SitesBLAST
Comparing BPHYT_RS13360 FitnessBrowser__BFirm:BPHYT_RS13360 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)
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
93% identity, 100% coverage: 1:529/531 of query aligns to 2:527/529 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)
93% identity, 98% coverage: 1:522/531 of query aligns to 2:521/521 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)
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
44% identity, 98% coverage: 5:524/531 of query aligns to 3:510/678 of 6jqoA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding crotonyl coenzyme a: V97 (= V100), F107 (≠ S110), S111 (≠ K114), 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: 5:524/531 of query aligns to 3:510/678 of 6jqnA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ V21), 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: 5:524/531 of query aligns to 3:510/678 of 6jqmA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L497)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ V21), 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)
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: 5:524/531 of query aligns to 4:511/681 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.
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: 63:516/531 of query aligns to 69:487/497 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 (≠ SAQT 234:237) binding
- V251 (≠ Q249) 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:
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
25% identity, 82% coverage: 64:498/531 of query aligns to 71:469/493 of 6vr6D
- active site: N156 (= N159), E253 (= E257), 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)
25% 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: 63:516/531 of query aligns to 67:485/495 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 (≠ A217), A218 (≠ G218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (= T237), E255 (≠ N255), L256 (≠ V256), A289 (≠ C296), E388 (= E400), F390 (= F402)
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 (vs. gap), 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
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
27% identity, 96% coverage: 3:513/531 of query aligns to 4:479/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E496)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I155), G149 (≠ N156), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (≠ T185), G208 (≠ S216), G212 (vs. gap), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ L241), E251 (= E257), L252 (≠ A258), C285 (= C296), E386 (= E400), F388 (= F402)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
27% identity, 96% coverage: 3:513/531 of query aligns to 4:479/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E496)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ N156), W151 (≠ F158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (≠ T185), G208 (≠ S216), G212 (vs. gap), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ L241), E251 (= E257), L252 (≠ A258), C285 (= C296), E386 (= E400), F388 (= F402)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
27% identity, 96% coverage: 3:513/531 of query aligns to 4:479/489 of 2wmeA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E496)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ N156), W151 (≠ F158), K175 (= K182), S177 (≠ A184), E178 (≠ T185), G208 (≠ S216), G212 (vs. gap), F226 (= F231), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ L241)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
27% identity, 96% coverage: 3:513/531 of query aligns to 5:480/490 of Q9HTJ1
- GAWN 150:153 (≠ NAFN 156:159) binding
- K162 (= K168) active site, Charge relay system
- KPSE 176:179 (≠ KPAT 182:185) binding
- G209 (≠ S216) binding
- GTST 230:233 (≠ SAQT 234:237) binding
- E252 (= E257) active site, Proton acceptor
- C286 (= C296) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E400) binding
- E464 (= E496) active site, Charge relay system
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
27% identity, 95% coverage: 3:506/531 of query aligns to 2:474/485 of 4u3wA
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 (≠ A217), E214 (≠ G218), 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 (≠ A217), 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
>BPHYT_RS13360 FitnessBrowser__BFirm:BPHYT_RS13360
MTELLKNHVAGQWIAGSGTGVTLTDPVTGVALVRVSSEGLDLAHAFGFARDTGGAALRAL
TYAQRAARLADIVKLLQAKRDDYYAIATANSGTTRNDSAVDIDGGIFTLSYYAKLGASLG
DVHALRDGESVSLSKDQSFSVQHVLTPTRGVALFINAFNFPSWGLWEKAAPALLSGVPVI
VKPATATAWLTQRMVADVVDAGILPPGALSVICGSSAGLLDQIQSFDVVSFTGSAQTAAT
LRAHPAFVQRGARLNVEADSLNSAILCADAAPGTPAFDLFIKEVVREMTVKSGQKCTAIR
RAFVPEGALEAVLEALNAKLAKITVGDPRNDTVRMGSLVSREQYENVLAGIAALREEAVL
AFDGSAVPLIDADSNIAACIAPHLFVVNDPDNATLLHDVEVFGPVASVAPYRVATDAATL
PEAHAVALARRGQGSLVASIYSNDEAHLGRLALELADSHGRVHAISPSVQQSQTGHGNVM
PMSLHGGPGRAGGGEELGGLRALGFYHRRSAIQAASAAIGSLTQATHLPKT
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