SitesBLAST
Comparing 3607155 FitnessBrowser__Dino:3607155 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)
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)
36% identity, 97% coverage: 6:473/483 of query aligns to 9:480/497 of P17202
- I28 (≠ R23) binding
- D96 (≠ E90) binding
- SPW 156:158 (= SPW 147:149) binding
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAN 173:176) binding
- L186 (≠ V177) binding
- SSAT 236:239 (≠ SVPV 227:230) binding
- V251 (≠ M242) binding in other chain
- L258 (≠ M249) binding
- W285 (≠ G276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ C432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ T442) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F448) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G452) binding
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 98% coverage: 4:477/483 of query aligns to 3:477/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E248), C282 (= C282), E383 (= E381), E460 (= E460)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ S147), K173 (= K173), G206 (= G206), G210 (= G210), Q211 (= Q211), F224 (= F224), G226 (= G226), S227 (= S227), T230 (≠ V230), R233 (≠ G233)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
36% identity, 97% coverage: 6:473/483 of query aligns to 7:478/495 of 4v37A
- active site: N157 (= N150), K180 (= K173), E255 (= E248), A289 (≠ C282), E388 (= E381), E465 (= E460)
- binding 3-aminopropan-1-ol: C448 (≠ T442), W454 (≠ F448)
- binding nicotinamide-adenine-dinucleotide: I153 (= I146), S154 (= S147), P155 (= P148), W156 (= W149), N157 (= N150), M162 (≠ T155), K180 (= K173), S182 (≠ A175), E183 (≠ N176), G213 (= G206), G217 (= G210), A218 (≠ Q211), T232 (= T225), G233 (= G226), S234 (= S227), T237 (≠ V230), E255 (= E248), L256 (≠ M249), A289 (≠ C282), E388 (= E381), F390 (= F383)
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)
36% identity, 97% coverage: 4:473/483 of query aligns to 10:476/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 97% coverage: 4:473/483 of query aligns to 9:475/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E248), C288 (= C282), E385 (= E381), E462 (= E460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P148), W155 (= W149), K179 (= K173), A181 (= A175), S182 (≠ N176), A212 (≠ G206), G216 (= G210), G232 (= G226), S233 (= S227), I236 (≠ V230), C288 (= C282), K338 (≠ Q332), E385 (= E381), F387 (= F383)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
37% identity, 97% coverage: 6:473/483 of query aligns to 9:483/503 of Q8VWZ1
- N27 (= N22) binding
- I28 (≠ R23) binding
- D99 (≠ E90) binding
- L189 (≠ V177) binding
- 238:245 (vs. 226:233, 38% identical) binding
- C294 (= C282) binding
- E393 (= E381) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
37% identity, 97% coverage: 6:473/483 of query aligns to 4:478/497 of 3iwkH
- active site: N157 (= N150), K180 (= K173), E255 (= E248), C289 (= C282), E388 (= E381), E465 (= E460)
- binding nicotinamide-adenine-dinucleotide: W156 (= W149), G213 (= G206), G217 (= G210), A218 (≠ Q211), G233 (= G226), S234 (= S227), T237 (≠ V230), K240 (≠ G233), C289 (= C282), Q336 (= Q329), E388 (= E381), F390 (= F383)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
39% identity, 98% coverage: 6:480/483 of query aligns to 7:482/489 of 6wsbA
- active site: N152 (= N150), E250 (= E248), C284 (= C282), E462 (= E460)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), G149 (≠ S147), A150 (≠ P148), W151 (= W149), N152 (= N150), K175 (= K173), E178 (≠ N176), G208 (= G206), G211 (= G210), A212 (≠ Q211), F225 (= F224), T226 (= T225), G227 (= G226), G228 (≠ S227), T231 (≠ V230), V235 (≠ I234), E250 (= E248), L251 (≠ M249), G252 (= G250), C284 (= C282), E385 (= E381), F387 (= F383)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
37% identity, 98% coverage: 4:477/483 of query aligns to 2:475/487 of 4go4A
- active site: N149 (= N150), K172 (= K173), E247 (= E248), C281 (= C282), E381 (= E381), E458 (= E460)
- binding nicotinamide-adenine-dinucleotide: I145 (= I146), V146 (≠ S147), W148 (= W149), N149 (= N150), F154 (≠ T155), K172 (= K173), G205 (= G206), G209 (= G210), Q210 (= Q211), F223 (= F224), T224 (= T225), G225 (= G226), S226 (= S227), T229 (≠ V230), E247 (= E248), G249 (= G250), C281 (= C282), E381 (= E381), F383 (= F383)
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)
36% identity, 99% coverage: 3:480/483 of query aligns to 5:484/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 147:150) binding
- K162 (= K159) active site, Charge relay system
- KPSE 176:179 (≠ KPAN 173:176) binding
- G209 (= G206) binding
- GTST 230:233 (≠ SVPV 227:230) binding
- E252 (= E248) active site, Proton acceptor
- C286 (= C282) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E381) binding
- E464 (= E460) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
36% identity, 99% coverage: 3:480/483 of query aligns to 4:483/489 of 4cazA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- 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 (= I146), G149 (≠ S147), W151 (= W149), N152 (= N150), K175 (= K173), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234), E251 (= E248), L252 (≠ M249), C285 (= C282), E386 (= E381), F388 (= F383)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
36% identity, 99% coverage: 3:480/483 of query aligns to 4:483/489 of 2woxA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I146), G149 (≠ S147), W151 (= W149), N152 (= N150), K175 (= K173), S177 (≠ A175), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234), E251 (= E248), L252 (≠ M249), C285 (= C282), E386 (= E381), F388 (= F383)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
36% identity, 99% coverage: 3:480/483 of query aligns to 4:483/489 of 2wmeA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S147), W151 (= W149), K175 (= K173), S177 (≠ A175), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234)
7radA Crystal structure analysis of aldh1b1
36% identity, 98% coverage: 5:477/483 of query aligns to 13:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ T155), K185 (= K173), E188 (≠ N176), G218 (= G206), G222 (= G210), A223 (≠ Q211), T237 (= T225), G238 (= G226), S239 (= S227), V242 (= V230), E261 (= E248), L262 (≠ M249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ R104), F163 (= F151), E285 (≠ S272), F289 (≠ G276), N450 (≠ T439), V452 (≠ G441)
7mjdA Crystal structure analysis of aldh1b1
36% identity, 98% coverage: 5:477/483 of query aligns to 13:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (= P148), W161 (= W149), N162 (= N150), M167 (≠ T155), K185 (= K173), E188 (≠ N176), G218 (= G206), G222 (= G210), F236 (= F224), T237 (= T225), G238 (= G226), S239 (= S227), V242 (= V230), E261 (= E248), L262 (≠ M249), C295 (= C282), E392 (= E381), F394 (= F383)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R104), E285 (≠ S272), F289 (≠ G276), N450 (≠ T439), V452 (≠ G441)
7mjcA Crystal structure analysis of aldh1b1
36% identity, 98% coverage: 5:477/483 of query aligns to 13:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ S147), P160 (= P148), W161 (= W149), N162 (= N150), K185 (= K173), E188 (≠ N176), G218 (= G206), G222 (= G210), T237 (= T225), G238 (= G226), S239 (= S227), V242 (= V230), E261 (= E248), L262 (≠ M249), C295 (= C282), E392 (= E381), F394 (= F383)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
37% identity, 98% coverage: 7:480/483 of query aligns to 13:485/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W149), K180 (= K173), A182 (= A175), T212 (≠ P205), G213 (= G206), G217 (= G210), F231 (= F224), G233 (= G226), S234 (= S227), V237 (= V230), Q337 (= Q329), E388 (= E381), F390 (= F383)
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)
33% identity, 96% coverage: 8:473/483 of query aligns to 21:489/505 of 4neaA
- active site: N166 (= N150), K189 (= K173), E264 (= E248), C298 (= C282), E399 (= E381), E476 (= E460)
- binding nicotinamide-adenine-dinucleotide: P164 (= P148), K189 (= K173), E192 (≠ N176), G222 (= G206), G226 (= G210), G242 (= G226), G243 (≠ S227), T246 (≠ V230), H249 (≠ G233), I250 (= I234), C298 (= C282), E399 (= E381), F401 (= F383)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
36% identity, 98% coverage: 7:480/483 of query aligns to 12:484/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I146), T153 (≠ S147), P154 (= P148), W155 (= W149), N156 (= N150), I161 (≠ T155), K179 (= K173), A181 (= A175), E182 (≠ N176), T211 (≠ P205), G212 (= G206), G216 (= G210), Q217 (= Q211), F230 (= F224), T231 (= T225), G232 (= G226), S233 (= S227), V236 (= V230), E255 (= E248), L256 (≠ M249), G257 (= G250), A289 (≠ C282), E387 (= E381), F389 (= F383)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
36% identity, 86% coverage: 65:478/483 of query aligns to 71:487/500 of 4i8pA
- active site: N159 (= N150), K182 (= K173), E257 (= E248), C291 (= C282), E390 (= E381), E467 (= E460)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (≠ S147), P157 (= P148), W158 (= W149), N159 (= N150), M164 (≠ T155), K182 (= K173), S184 (≠ A175), E185 (≠ N176), G215 (= G206), G219 (= G210), A220 (≠ Q211), T234 (= T225), G235 (= G226), S236 (= S227), T239 (≠ V230), E257 (= E248), L258 (≠ M249), C291 (= C282), E390 (= E381), F392 (= F383), W456 (≠ F448)
Query Sequence
>3607155 FitnessBrowser__Dino:3607155
MTDRTQLYIDGAWTEGTAQIENRNPSDTTDLIGMYAQADAGQLDTALAAARRAQPAWWAA
GIQKRHDVLMAIGTELMARSDEIGRLLSREEGKPLAEGKGEVYRAGQFFTYFAAEALRQH
GDLAESVRPGIEIDVRREAVGVVAIISPWNFPVATPAWKIAPALAFGNAVVWKPANVTPA
SAIALTEIIARQDIPKGLFNLVAGPGRDVGQRLVESAEVDAISFTGSVPVGRGIAAAAVQ
NMTKVQMEMGSKNPLIVMDDCDLDLAVAHAASSAFGGTGQKCTAASRLIVHSAVHDAFVE
KLVAAARAMKVGHALEDGTQLGPVVSESQLNQNMEYIGVGKDEGAELLCGGDRLEMATDG
YFMAPAVFAGTANDMRINREEMFAPITAVQRVDSYDEALARANDTQFGLTAGIMTTSLAR
ASHFRAHMRAGCVMVNLPTAGTDYHVPFGGRGASSFGPREQGSYAAEFYTTVKTAYVAAG
APA
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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