SitesBLAST
Comparing HSERO_RS20590 FitnessBrowser__HerbieS:HSERO_RS20590 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)
59% identity, 99% coverage: 8:683/686 of query aligns to 4:675/681 of P77455
- E256 (= E259) 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)
59% identity, 99% coverage: 8:683/686 of query aligns to 3:674/678 of 6jqoA
- active site: N157 (= N161), E255 (= E259), C294 (= C298), L483 (= L492)
- binding crotonyl coenzyme a: V97 (≠ I101), F107 (= F111), S111 (= S115), F158 (= F162), W161 (= W165), R638 (≠ K647)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N158), F156 (= F160), N157 (= N161), T183 (= T187), T230 (= T234), G231 (= G235), S232 (= S236), T235 (= T239), A256 (= A260), D257 (= D261), C294 (= C298)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
59% identity, 99% coverage: 8:683/686 of query aligns to 3:674/678 of 6jqnA
- active site: N157 (= N161), E255 (= E259), C294 (= C298), L483 (= L492)
- binding octanoyl-coenzyme a: F562 (= F571), H565 (= H574), F576 (= F585), G583 (= G592), V595 (= V604), A604 (= A613), N605 (= N614), Y606 (= Y615), F613 (= F622), I614 (≠ V623)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q23), I153 (= I157), N154 (= N158), A155 (= A159), F156 (= F160), K180 (= K184), A182 (= A186), T183 (= T187), T230 (= T234), G231 (= G235), S232 (= S236), T235 (= T239), L239 (= L243), E255 (= E259), A256 (= A260), D257 (= D261), C294 (= C298), F396 (= F405), H471 (= H480)
6jqmA Structure of paaz with NADPH (see paper)
59% identity, 99% coverage: 8:683/686 of query aligns to 3:674/678 of 6jqmA
- active site: N157 (= N161), E255 (= E259), C294 (= C298), L483 (= L492)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q23), I153 (= I157), N154 (= N158), A155 (= A159), F156 (= F160), N157 (= N161), K180 (= K184), A182 (= A186), T183 (= T187), G231 (= G235), S232 (= S236), T235 (= T239), A256 (= A260), D257 (= D261), C294 (= C298), E394 (= E403), F396 (= F405)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
44% identity, 69% coverage: 7:480/686 of query aligns to 5:484/521 of 2vroA
- active site: N160 (= N161), K183 (= K184), E258 (= E259), C297 (= C298), E401 (= E403)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I157), K183 (= K184), S217 (≠ T218), S235 (= S236), T238 (= T239), L242 (= L243), F403 (= F405)
Sites not aligning to the query:
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
44% identity, 69% coverage: 7:480/686 of query aligns to 5:483/529 of 2y53A
- active site: N160 (= N161), K183 (= K184), Q258 (≠ E259), C297 (= C298), E401 (= E403)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I157), N157 (= N158), F159 (= F160), N160 (= N161), K183 (= K184), A185 (= A186), T186 (= T187), S217 (≠ T218), F232 (= F233), G234 (= G235), S235 (= S236), A236 (= A237), T238 (= T239), A259 (= A260), D260 (= D261), C297 (= C298), F403 (= F405)
Sites not aligning to the query:
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
29% identity, 56% coverage: 65:447/686 of query aligns to 72:436/494 of 4pz2B
- active site: N159 (= N161), K182 (= K184), E258 (≠ P255), C292 (= C298), E392 (= E403)
- binding nicotinamide-adenine-dinucleotide: I155 (= I157), I156 (≠ N158), P157 (≠ A159), W158 (≠ F160), N159 (= N161), M164 (≠ G166), K182 (= K184), A184 (= A186), E185 (≠ T187), G215 (vs. gap), G219 (= G219), F233 (= F233), T234 (= T234), G235 (= G235), S236 (= S236), V239 (≠ T239), E258 (≠ P255), L259 (≠ F256), C292 (= C298), E392 (= E403), F394 (= F405)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
27% identity, 63% coverage: 9:438/686 of query aligns to 11:420/481 of 3jz4A
- active site: N156 (= N161), K179 (= K184), E254 (≠ N264), C288 (= C298), E385 (= E403)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A159), W155 (≠ F160), K179 (= K184), A181 (= A186), S182 (≠ T187), A212 (≠ T218), G216 (≠ L222), G232 (= G235), S233 (= S236), I236 (≠ T239), C288 (= C298), K338 (≠ D348), E385 (= E403), F387 (= F405)
Sites not aligning to the query:
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)
27% identity, 63% coverage: 9:438/686 of query aligns to 12:421/482 of P25526
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
30% identity, 43% coverage: 152:447/686 of query aligns to 142:425/477 of 2opxA
- active site: N151 (= N161), K174 (= K184), E249 (≠ I267), C283 (= C298), E381 (= E403)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F152 (= F162), N284 (≠ T299), F312 (≠ V327), G313 (= G328), R318 (≠ E333), D320 (vs. gap), I321 (≠ V335), A322 (≠ R336), Y362 (≠ F382)
Sites not aligning to the query:
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
30% identity, 43% coverage: 152:447/686 of query aligns to 142:425/477 of 2impA
- active site: N151 (= N161), K174 (= K184), E249 (≠ I267), C283 (= C298), E381 (= E403)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I157), L148 (≠ N158), P149 (≠ A159), W150 (≠ F160), K174 (= K184), E177 (≠ T187), F178 (≠ A188), G207 (vs. gap), G211 (= G219), Q212 (≠ D220), S228 (= S236), A231 (≠ T239), K234 (= K242), R334 (≠ D348)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
30% identity, 43% coverage: 152:447/686 of query aligns to 142:425/477 of 2iluA
- active site: N151 (= N161), K174 (= K184), E249 (≠ I267), C283 (= C298), E381 (= E403)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I157), L148 (≠ N158), P149 (≠ A159), W150 (≠ F160), K174 (= K184), S176 (≠ A186), E177 (≠ T187), R206 (vs. gap), G207 (vs. gap), G211 (= G219), Q212 (≠ D220), S228 (= S236), A231 (≠ T239), K234 (= K242), I235 (≠ L243), N328 (≠ S342), R334 (≠ D348), F383 (= F405)
Sites not aligning to the query:
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 43% coverage: 152:447/686 of query aligns to 144:427/479 of P25553
- L150 (≠ N158) binding
- R161 (≠ E169) binding
- KPSE 176:179 (≠ KPAT 184:187) binding
- F180 (≠ A188) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D220) binding
- S230 (= S236) binding
- E251 (≠ I267) binding
- N286 (≠ T299) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ D348) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 73% coverage: 11:513/686 of query aligns to 23:501/501 of Q56YU0
- G152 (≠ A142) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A420) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
24% identity, 65% coverage: 65:508/686 of query aligns to 79:498/505 of 4neaA
- active site: N166 (= N161), K189 (= K184), E264 (vs. gap), C298 (= C298), E399 (= E403), E476 (≠ A486)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A159), K189 (= K184), E192 (≠ T187), G222 (vs. gap), G226 (= G219), G242 (= G235), G243 (≠ S236), T246 (= T239), H249 (≠ K242), I250 (≠ L243), C298 (= C298), E399 (= E403), F401 (= F405)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
27% identity, 64% coverage: 66:507/686 of query aligns to 68:475/483 of 3b4wA
- active site: N154 (= N161), K177 (= K184), E251 (= E259), C285 (= C298), E384 (= E403), E460 (≠ A486)
- binding nicotinamide-adenine-dinucleotide: I150 (= I157), V151 (≠ N158), W153 (≠ F160), N154 (= N161), K177 (= K184), I210 (vs. gap), G213 (= G219), T228 (= T234), G229 (= G235), S230 (= S236), V233 (≠ T239), E236 (≠ K242), E251 (= E259), L252 (≠ A260), C285 (= C298), E384 (= E403), F386 (= F405)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
27% identity, 42% coverage: 152:438/686 of query aligns to 139:415/454 of 3ty7B
Sites not aligning to the query:
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
27% identity, 64% coverage: 66:507/686 of query aligns to 68:476/486 of 4pxlA
- active site: N154 (= N161), K177 (= K184), E253 (≠ P255), C287 (= C298), E384 (= E403), D461 (≠ E491)
- binding nicotinamide-adenine-dinucleotide: I150 (= I157), V151 (≠ N158), P152 (≠ A159), W153 (≠ F160), K177 (= K184), E180 (≠ T187), G210 (vs. gap), G214 (= G219), A215 (≠ D220), F228 (= F233), G230 (= G235), S231 (= S236), V234 (≠ T239), E253 (≠ P255), G255 (≠ N257), C287 (= C298), Q334 (= Q345), K337 (≠ D348), E384 (= E403), F386 (= F405)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
29% identity, 50% coverage: 152:493/686 of query aligns to 141:462/489 of 4o6rA
- active site: N150 (= N161), K173 (= K184), E248 (≠ N264), C282 (= C298), E383 (= E403), E460 (= E491)
- binding adenosine monophosphate: I146 (= I157), V147 (≠ N158), K173 (= K184), G206 (vs. gap), G210 (= G219), Q211 (≠ D220), F224 (= F233), G226 (= G235), S227 (= S236), T230 (= T239), R233 (≠ K242)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
29% identity, 51% coverage: 152:499/686 of query aligns to 138:469/476 of 4yweA
Sites not aligning to the query:
Query Sequence
>HSERO_RS20590 FitnessBrowser__HerbieS:HSERO_RS20590
MTAHPPLLQSFIAGRWLGQRPSQALHSAVNGSAVASTHEESIDFGEALEHARKTGLPALM
ALDFQQRAAILKALAKYLMEHKEVLYAVSAHTGATRADSWIDIEGGSGTLFTYASIGANE
FPSSNLVHEGPAMRLGKQGRFAGTHILVPRGGVAVHINAFNFPVWGMLEKFAPTFLAGMP
CIVKPATATSYLAEAAVRLIQQSGLLPEGSLQLVIGSTGDLLERLQAQDVVTFTGSADTA
AKLRAHPNLIANSIPFNAEADSLNCAILGPDITADDEEFDLFVKEVAREMTTKAGQKCTA
IRRAIVPRRHVDAVAERLAARLSKIVVGDPALETVRMGPLASRAQQRDVEERVALLRHSA
DLILGAGSAFAPQGQGVGEGAFFAPTLLLARDTAAGSPVHEVEAFGPVSTLMPYDDLDEA
LALAARGRGSLVASLVTRTPAVAARAIPVAAAWHGRLLVLDREAAAESTGHGSPLPQLKH
GGPGRAGGGEELGGSRAVKHYLQRTAVQGSPTMLAAVVGEHVRGARVRESGIHPFRHYFE
DLQIGDSLTTHRRTVTEADIVNFGCLSGDHFYMHFDEIAARQSPFGKRIAHGYFVLSAAA
GLFVSPAPGPVLANYGLDTLRFVKPVGIGDTISARLTCKRKIDRNKKDANGQGQGVVAWD
VEVSNQEGELVASYDILTLVAKKPLE
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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