SitesBLAST
Comparing PP_3270 FitnessBrowser__Putida:PP_3270 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: 7:682/684 of query aligns to 4:675/681 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.
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
59% identity, 99% coverage: 7:682/684 of query aligns to 3:674/678 of 6jqoA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding crotonyl coenzyme a: V97 (≠ I100), F107 (= F110), S111 (≠ G114), F158 (= F161), W161 (= W164), R638 (≠ T646)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N157), F156 (= F159), N157 (= N160), T183 (= T186), T230 (= T233), G231 (= G234), S232 (= S235), T235 (= T238), A256 (= A259), D257 (= D260), C294 (= C297)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
59% identity, 99% coverage: 7:682/684 of query aligns to 3:674/678 of 6jqnA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding octanoyl-coenzyme a: F562 (= F570), H565 (= H573), F576 (= F584), G583 (= G591), V595 (= V603), A604 (= A612), N605 (= N613), Y606 (= Y614), F613 (= F621), I614 (= I622)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q22), 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 (= A259), D257 (= D260), C294 (= C297), F396 (= F404), H471 (= H479)
6jqmA Structure of paaz with NADPH (see paper)
59% identity, 99% coverage: 7:682/684 of query aligns to 3:674/678 of 6jqmA
- active site: N157 (= N160), E255 (= E258), C294 (= C297), L483 (= L491)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ Q22), I153 (= I156), N154 (= N157), A155 (= A158), F156 (= F159), N157 (= N160), K180 (= K183), A182 (= A185), T183 (= T186), G231 (= G234), S232 (= S235), T235 (= T238), A256 (= A259), D257 (= D260), C294 (= C297), E394 (= E402), F396 (= F404)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
41% identity, 69% coverage: 7:479/684 of query aligns to 6:484/521 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 (≠ T217), S235 (= S235), T238 (= T238), L242 (= L242), F403 (= F404)
Sites not aligning to the query:
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
41% identity, 69% coverage: 7:479/684 of query aligns to 6:483/529 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 (≠ T217), F232 (= F232), G234 (= G234), S235 (= S235), A236 (= A236), T238 (= T238), A259 (= A259), D260 (= D260), C297 (= C297), F403 (= F404)
Sites not aligning to the query:
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
29% identity, 44% coverage: 142:444/684 of query aligns to 129:422/454 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)
24% identity, 65% coverage: 64:507/684 of query aligns to 79:498/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (= E258), C298 (= C297), E399 (= E402), E476 (≠ A485)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A158), K189 (= K183), E192 (≠ T186), G222 (≠ T217), G226 (≠ L221), G242 (= G234), G243 (≠ S235), T246 (= T238), H249 (≠ R243), I250 (≠ V244), C298 (= C297), E399 (= E402), F401 (= F404)
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)
28% identity, 47% coverage: 127:446/684 of query aligns to 120:425/477 of 2impA
- active site: N151 (= N160), K174 (= K183), E249 (≠ I266), C283 (= C297), E381 (= E402)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I156), L148 (≠ N157), P149 (≠ A158), W150 (≠ F159), K174 (= K183), E177 (≠ T186), F178 (≠ S187), G207 (≠ T217), G211 (≠ L221), Q212 (≠ D222), S228 (= S235), A231 (≠ T238), K234 (= K241), R334 (≠ D347)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
28% identity, 47% coverage: 127:446/684 of query aligns to 120:425/477 of 2iluA
- active site: N151 (= N160), K174 (= K183), E249 (≠ I266), C283 (= C297), E381 (= E402)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I156), L148 (≠ N157), P149 (≠ A158), W150 (≠ F159), K174 (= K183), S176 (≠ A185), E177 (≠ T186), R206 (≠ S216), G207 (≠ T217), G211 (≠ L221), Q212 (≠ D222), S228 (= S235), A231 (≠ T238), K234 (= K241), I235 (≠ L242), N328 (≠ S341), R334 (≠ D347), F383 (= F404)
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)
28% identity, 47% coverage: 127:446/684 of query aligns to 122:427/479 of P25553
- L150 (≠ N157) binding
- R161 (≠ E168) binding
- KPSE 176:179 (≠ KPAT 183:186) binding
- F180 (≠ S187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D222) binding
- S230 (= S235) binding
- E251 (≠ I266) binding
- N286 (≠ T298) 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 (≠ D347) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
28% identity, 47% coverage: 127:446/684 of query aligns to 120:425/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (≠ I266), C283 (= C297), E381 (= E402)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F152 (= F161), N284 (≠ T298), F312 (≠ V326), G313 (= G327), R318 (≠ E332), D320 (vs. gap), I321 (≠ V334), A322 (≠ R335), Y362 (≠ F381)
Sites not aligning to the query:
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
33% identity, 40% coverage: 151:423/684 of query aligns to 160:419/496 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 (vs. gap), F253 (vs. gap), Y256 (≠ L242), C269 (≠ A259), G270 (≠ D260), C303 (= C297), H350 (≠ Q344), K353 (≠ R351), F400 (= F404)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
27% identity, 54% coverage: 136:506/684 of query aligns to 130:475/483 of 3b4wA
- active site: N154 (= N160), K177 (= K183), E251 (= E258), C285 (= C297), E384 (≠ D400), E460 (≠ A485)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), V151 (≠ N157), W153 (≠ F159), N154 (= N160), K177 (= K183), I210 (vs. gap), G213 (= G218), T228 (= T233), G229 (= G234), S230 (= S235), V233 (≠ T238), E236 (≠ K241), E251 (= E258), L252 (≠ A259), C285 (= C297), E384 (≠ D400), F386 (= F404)
6mvtA Structure of a bacterial aldh16 complexed with nadh (see paper)
25% identity, 64% coverage: 151:588/684 of query aligns to 142:569/751 of 6mvtA
- active site: N151 (= N160), E247 (≠ N263), C281 (= C297), E450 (≠ A485)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I156), I148 (≠ N157), K174 (= K183), E177 (≠ T186), G207 (vs. gap), G210 (= G218), E211 (≠ D219), F223 (= F232), S226 (= S235), V229 (≠ A240), D327 (= D343), R331 (= R351)
6mvsA Structure of a bacterial aldh16 complexed with NAD (see paper)
25% identity, 64% coverage: 151:588/684 of query aligns to 142:569/751 of 6mvsA
- active site: N151 (= N160), E247 (≠ N263), C281 (= C297), E450 (≠ A485)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I156), I148 (≠ N157), W150 (≠ F159), K174 (= K183), E177 (≠ T186), G207 (vs. gap), G210 (= G218), E211 (≠ D219), F223 (= F232), S226 (= S235), V229 (≠ A240)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
25% identity, 74% coverage: 1:507/684 of query aligns to 8:487/497 of 8skfA
- binding calcium ion: T33 (≠ S26), I34 (≠ A27), D100 (≠ H90), V187 (≠ S187)
- binding nicotinamide-adenine-dinucleotide: I156 (= I156), G157 (≠ N157), A158 (= A158), W159 (≠ F159), K183 (= K183), E186 (≠ T186), G216 (vs. gap), G220 (= G218), T235 (= T233), G236 (= G234), G237 (≠ S235), S240 (≠ T238), K243 (= K241), E259 (≠ N263), C293 (= C297), F396 (= F404)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
25% identity, 73% coverage: 8:507/684 of query aligns to 6:478/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
25% identity, 73% coverage: 8:507/684 of query aligns to 6:478/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
25% identity, 73% coverage: 8:507/684 of query aligns to 6:478/488 of 8vqzA
Query Sequence
>PP_3270 FitnessBrowser__Putida:PP_3270
MSAAPTLQSFIAGRWLGQHGAQALRSALDGHVLAYSHEERPDFAEAVDYARARGLASLMG
MDFQQRAQRLKALALYLAECKEQLYALSHHSGATRADSWIDIEGGNATLFSYAGIGSREL
PSGNLVHEGPAIPLGKQGHFAGSHILVPRAGVAVHINAFNFPIWGMLEKFAPTFLAGMPC
IVKPATSTSYLTEAVVRLMNASGLLPEGSLQLVIGSTGDLLDRLQGQDVVTFTGSADTAA
KLRVTPNLIRNSVPFTAEADSLNCAILGPDVSPDSEEFDLYIKEVVREMTTKAGQKCTAI
RRAIVPARHLDAVATRLRERLSKVVVGDPSLEGVRMGALASHDQQRDVGERVRSLLQSCD
QLFGASDGFAPRGEGVAEGAFFAPTLLQARDPHAEGGAHDIEAFGPVSTLMAYDDLDEAL
ALAARGKGSLVATLVTADRSVAAKAIPVAAAWHGRLLVLDSQAAKESTGHGSPLPQLKHG
GPGRAGGGEELGGLRAVKHYLQRAAVQGSPSMLTAVTGEYVRGGEVIETEVHPFRRYFEQ
LRVGESLLTHRRTVTEADLVNFGCLSGDHFYMHFDEIAAKASQFGKRIAHGYFVLSAAAG
LFVSPGAGPVLANYGLDTLRFINPVGIGDTIQARLTCKRKIDQGKTSPLGQPQGVVAWDV
EVTNQLGELVASYDILTLVLKKPA
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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