SitesBLAST
Comparing SM_b21539 FitnessBrowser__Smeli:SM_b21539 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)
Q92UV7 Phosphonoacetaldehyde dehydrogenase; EC 1.2.1.- from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
100% identity, 100% coverage: 1:485/485 of query aligns to 1:485/485 of Q92UV7
- R108 (= R108) binding ; mutation to A: Decreased catalytic activity and decreased affinity for phosphonoacetaldehyde.
- TPF 155:157 (= TPF 155:157) binding
- N158 (= N158) mutation to A: Strongly decreased catalytic activity.
- H159 (= H159) binding
- KPTE 181:184 (= KPTE 181:184) binding
- S235 (= S235) binding
- E254 (= E254) active site, Proton donor/acceptor; mutation to A: Loss of catalytic activity.
- R290 (= R290) mutation to A: Decreased catalytic activity and slightly decreased affinity for phosphonoacetaldehyde.
- RCT 290:292 (= RCT 290:292) binding
- C291 (= C291) active site, Nucleophile; mutation to A: Loss of catalytic activity.
- E385 (= E385) binding ; mutation to A: Decreased catalytic activity and decreased affinity for phosphonoacetaldehyde.
- R447 (= R447) binding ; mutation to A: Decreased catalytic activity and strongly decreased affinity for phosphonoacetaldehyde.
4i3xA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetate and cofactor NAD+ (see paper)
100% identity, 98% coverage: 10:485/485 of query aligns to 1:476/476 of 4i3xA
- active site: N149 (= N158), K172 (= K181), E245 (= E254), C282 (= C291), E376 (= E385), E456 (= E465)
- binding nicotinamide-adenine-dinucleotide: I145 (= I154), T146 (= T155), P147 (= P156), F148 (= F157), N149 (= N158), K172 (= K181), T174 (= T183), P205 (= P214), G209 (= G218), F223 (= F232), T224 (= T233), G225 (= G234), S226 (= S235), V229 (= V238), E245 (= E254), L246 (= L255), G247 (= G256), C282 (= C291), E376 (= E385), F378 (= F387), F444 (= F453)
- binding phosphonoacetic acid: R99 (= R108), H150 (= H159), R281 (= R290), C282 (= C291), R438 (= R447)
4i3tA Structure of phosphonoacetaldehyde dehydrogenase in the apo state (see paper)
100% identity, 98% coverage: 11:484/485 of query aligns to 1:474/474 of 4i3tA
4i3wA Structure of phosphonoacetaldehyde dehydrogenase in complex with gylceraldehyde-3-phosphate and cofactor NAD+ (see paper)
100% identity, 98% coverage: 12:484/485 of query aligns to 1:473/473 of 4i3wA
- active site: N147 (= N158), K170 (= K181), E243 (= E254), C280 (= C291), E374 (= E385), E454 (= E465)
- binding glyceraldehyde-3-phosphate: R97 (= R108), H148 (= H159), M152 (= M163), R279 (= R290), C280 (= C291), R436 (= R447)
- binding nicotinamide-adenine-dinucleotide: I143 (= I154), T144 (= T155), P145 (= P156), F146 (= F157), K170 (= K181), T172 (= T183), P203 (= P214), G207 (= G218), F221 (= F232), G223 (= G234), S224 (= S235), V227 (= V238)
4i3uA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetaldehyde (see paper)
100% identity, 98% coverage: 12:484/485 of query aligns to 1:473/473 of 4i3uA
- active site: N147 (= N158), K170 (= K181), E243 (= E254), C280 (= C291), E374 (= E385), E454 (= E465)
- binding phosphonoacetaldehyde: R97 (= R108), H148 (= H159), M152 (= M163), R279 (= R290), C280 (= C291), R436 (= R447)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
37% identity, 94% coverage: 28:482/485 of query aligns to 3:463/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I154), L137 (≠ T155), F139 (= F157), K163 (= K181), S165 (≠ T183), I166 (≠ E184), S196 (≠ P214), G200 (= G218), G216 (= G234), S217 (= S235), T220 (≠ V238), I224 (= I242)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
37% identity, 94% coverage: 28:482/485 of query aligns to 3:463/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (= I154), L137 (≠ T155), F139 (= F157), K163 (= K181), S165 (≠ T183), I166 (≠ E184), S196 (≠ P214), G200 (= G218), G216 (= G234), S217 (= S235), T220 (≠ V238), I224 (= I242), L239 (= L255), C272 (= C291), E368 (= E385), F370 (= F387)
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
36% identity, 93% coverage: 28:480/485 of query aligns to 6:452/456 of 3rhdA
- active site: N133 (= N158), H156 (≠ K181), E233 (= E254), C267 (= C291), E360 (= E385), E437 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (= I154), T130 (= T155), F132 (= F157), H156 (≠ K181), S158 (≠ T183), S159 (≠ E184), K160 (≠ L185), G193 (≠ P214), E194 (≠ A215), G197 (= G218), D198 (≠ M219), F211 (= F232), S214 (= S235), V217 (= V238)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
37% identity, 93% coverage: 24:475/485 of query aligns to 17:466/480 of 3rhhD
- active site: N155 (= N158), K178 (= K181), E251 (= E254), C285 (= C291), E378 (= E385), Q456 (≠ E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (= I154), P153 (= P156), F154 (= F157), K178 (= K181), P179 (= P182), A180 (≠ T183), T181 (≠ E184), G211 (≠ P214), G215 (= G218), D216 (≠ M219), F229 (= F232), G231 (= G234), G232 (≠ S235), T235 (≠ V238)
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)
35% identity, 94% coverage: 24:479/485 of query aligns to 16:469/475 of Q59931
- R103 (= R108) binding
- S151 (≠ T155) binding
- K177 (= K181) binding
- T180 (≠ E184) binding
- D215 (≠ M219) binding
- 230:251 (vs. 234:255, 36% identical) binding
- E377 (= E385) binding
- R437 (≠ Y446) binding
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
34% identity, 94% coverage: 24:479/485 of query aligns to 15:468/474 of 2esdA
- active site: N153 (= N158), K176 (= K181), A249 (≠ E254), C283 (= C291), E376 (= E385), Q454 (≠ E465)
- binding glyceraldehyde-3-phosphate: R102 (= R108), Y154 (≠ H159), R282 (= R290), C283 (= C291), T284 (= T292), Q435 (≠ G445), R436 (≠ Y446)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (= F157), K176 (= K181), P178 (≠ T183), T179 (≠ E184), G209 (≠ P214), G213 (= G218), D214 (≠ M219), F227 (= F232), S230 (= S235), I233 (≠ V238), K328 (= K337), S329 (≠ A338), Y332 (≠ L341)
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
34% identity, 94% coverage: 24:479/485 of query aligns to 15:468/474 of 1qi1B
- active site: N153 (= N158), K176 (= K181), E249 (= E254), S283 (≠ C291), E376 (= E385), Q454 (≠ E465)
- binding sn-glycerol-3-phosphate: Y154 (≠ H159), R282 (= R290), S283 (≠ C291), T284 (= T292), R436 (≠ Y446)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (= P156), F152 (= F157), N153 (= N158), L158 (≠ M163), K176 (= K181), P178 (≠ T183), T179 (≠ E184), G209 (≠ P214), G213 (= G218), G229 (= G234), S230 (= S235), I233 (≠ V238), E249 (= E254), L250 (= L255), S283 (≠ C291)
5n5sB Crystal structure of aldehyde dehydrogenase 21 (aldh21) from physcomitrella patens in complex with NADP+ (see paper)
34% identity, 86% coverage: 67:482/485 of query aligns to 64:475/481 of 5n5sB
- active site: N155 (= N158), K178 (= K181), E251 (= E254), C286 (= C291), E380 (= E385), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V151 (≠ I154), S152 (≠ T155), P153 (= P156), W154 (≠ F157), N155 (= N158), L160 (≠ M163), K178 (= K181), A180 (≠ T183), S181 (≠ E184), R212 (≠ P214), A215 (≠ I217), T230 (= T233), G231 (= G234), S232 (= S235), I235 (≠ V238), E251 (= E254), L252 (= L255), C286 (= C291), E380 (= E385), F382 (= F387), Y447 (≠ F453)
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)
31% identity, 96% coverage: 17:482/485 of query aligns to 15:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 96% coverage: 17:482/485 of query aligns to 14:479/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E254), C288 (= C291), E385 (= E385), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (≠ F157), K179 (= K181), A181 (≠ T183), S182 (≠ E184), A212 (≠ P214), G216 (= G218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C291), K338 (≠ L341), E385 (= E385), F387 (= F387)
5kf0A Crystal structure of an aldedhyde dehydrogenase from burkholderia vietnamiensis
35% identity, 85% coverage: 63:476/485 of query aligns to 62:471/480 of 5kf0A
- active site: N157 (= N158), K180 (= K181), E252 (= E254), C288 (= C291), E382 (= E385), E460 (= E465)
- binding magnesium ion: E88 (≠ D89)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I153 (= I154), S154 (≠ T155), P155 (= P156), F156 (= F157), N157 (= N158), L162 (≠ M163), K180 (= K181), S183 (≠ E184), R184 (≠ L185), R213 (vs. gap), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), E252 (= E254), L253 (= L255), C288 (= C291), E382 (= E385), F384 (= F387)
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)
34% identity, 90% coverage: 6:440/485 of query aligns to 1:437/479 of P25553
- M1 (≠ V6) modified: Initiator methionine, Removed
- L150 (≠ T155) binding
- R161 (≠ H166) binding
- KPSE 176:179 (≠ KPTE 181:184) binding
- F180 (≠ L185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ M219) binding
- S230 (= S235) binding
- E251 (= E254) binding
- N286 (≠ T292) 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 (≠ L341) binding
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)
34% identity, 89% coverage: 8:440/485 of query aligns to 1:435/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (= E254), C283 (= C291), E381 (= E385)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (≠ F157), K174 (= K181), E177 (= E184), F178 (≠ L185), G207 (≠ P214), G211 (= G218), Q212 (≠ M219), S228 (= S235), A231 (≠ V238), K234 (≠ L241), R334 (≠ L341)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
34% identity, 89% coverage: 8:440/485 of query aligns to 1:435/477 of 2iluA
- active site: N151 (= N158), K174 (= K181), E249 (= E254), C283 (= C291), E381 (= E385)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (≠ F157), K174 (= K181), S176 (≠ T183), E177 (= E184), R206 (≠ W213), G207 (≠ P214), G211 (= G218), Q212 (≠ M219), S228 (= S235), A231 (≠ V238), K234 (≠ L241), I235 (= I242), N328 (≠ H335), R334 (≠ L341), F383 (= F387)
Sites not aligning to the query:
Q3SY69 Mitochondrial 10-formyltetrahydrofolate dehydrogenase; Mitochondrial 10-FTHFDH; mtFDH; Aldehyde dehydrogenase family 1 member L2; EC 1.5.1.6 from Homo sapiens (Human) (see paper)
32% identity, 87% coverage: 63:484/485 of query aligns to 500:923/923 of Q3SY69
Sites not aligning to the query:
- 374 S→A: No effect on phosphopantetheinylation.
- 375 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation.
Query Sequence
>SM_b21539 FitnessBrowser__Smeli:SM_b21539
MTNAEVTIAVRHEPMRIAGRLVDTDDRVEVRYPWNDTVVGTVPAGRAEHAREAFAIAAAY
QPKLTRYERQKILLATAEALAARKEEISDVITLELGISKADSLYEVGRAFDVFTLAGQMC
IRDDGEIFSCDLTPHGKARKIFTMREPLTAISAITPFNHPLNMVAHKVAPAIATNNCVVV
KPTELTPMTALLLADILYEAGLPPEMLSVVTGWPADIGMEMITNPHVDLVTFTGSVPVGK
LIAANAHYKRQVLELGGNDPLIILNDLSDDDLARAADLAVAGATKNSGQRCTAVKRILCQ
ESVADRFVPLVLERAKRLRFGDPMDRSTDLGTVIHEKAAALFEERVMRAAEEGADILYHP
GRSGALLPPIVVDRVPHQSDLVLEETFGPIIPIVRVPDDDDATITLSNSTAFGLSSGVCT
NDYRRMQKYIAGLKVGTVNIWEVPGYRIEMSPFGGIKDSGNGYKEGVIEAMKSFTNVKTF
SLPWP
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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