SitesBLAST
Comparing Pf6N2E2_1919 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1919 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
47% identity, 95% coverage: 20:483/490 of query aligns to 7:472/476 of 5x5uA
- active site: N151 (= N162), K174 (= K185), E249 (= E260), C283 (= C294), E380 (= E391), E457 (= E468)
- binding glycerol: D15 (= D29), A16 (≠ R30), A17 (≠ P31), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P160), P207 (= P218), A208 (= A219), S211 (= S222), G227 (= G238), S228 (= S239), V231 (= V242), R329 (= R340), R330 (= R341), E380 (= E391), F382 (= F393)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
47% identity, 95% coverage: 20:483/490 of query aligns to 7:472/476 of 5x5tA
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)
33% identity, 97% coverage: 10:483/490 of query aligns to 3:478/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 97% coverage: 10:483/490 of query aligns to 2:477/481 of 3jz4A
- active site: N156 (= N162), K179 (= K185), E254 (= E260), C288 (= C294), E385 (= E391), E462 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P160), W155 (= W161), K179 (= K185), A181 (≠ P187), S182 (≠ E188), A212 (≠ P218), G216 (≠ S222), G232 (= G238), S233 (= S239), I236 (≠ V242), C288 (= C294), K338 (≠ A344), E385 (= E391), F387 (= F393)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
34% identity, 94% coverage: 20:482/490 of query aligns to 4:472/477 of 6j76A
- active site: N148 (= N162), E246 (= E260), C280 (= C294), E458 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ F158), T145 (= T159), A146 (≠ P160), W147 (= W161), N148 (= N162), K171 (= K185), T173 (≠ P187), S174 (≠ E188), G204 (≠ P218), G208 (≠ S222), T223 (= T237), G224 (= G238), S225 (= S239), A228 (≠ V242), S231 (≠ H245), I232 (≠ L246), E246 (= E260), L247 (= L261), C280 (= C294), E381 (= E391), F383 (= F393), H447 (≠ F457)
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
34% identity, 95% coverage: 17:483/490 of query aligns to 60:530/535 of P51649
- C93 (≠ A51) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G134) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P138) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ E140) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R170) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C180) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KAPE 185:188) binding
- T233 (= T190) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A194) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N212) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S222) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVAVG 238:243) binding
- R334 (= R288) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ I289) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C294) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A296) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D325) natural variant: N -> S
- P382 (= P335) to L: in SSADHD; 2% of activity
- V406 (= V359) to I: in dbSNP:rs143741652
- G409 (= G362) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ P451) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
34% identity, 95% coverage: 17:483/490 of query aligns to 10:480/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
34% identity, 95% coverage: 17:483/490 of query aligns to 10:480/485 of 2w8qA
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)
34% identity, 96% coverage: 16:485/490 of query aligns to 6:484/497 of P17202
- I28 (≠ L37) binding
- D96 (≠ E103) binding
- SPW 156:158 (≠ TPW 159:161) binding
- Y160 (≠ V163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R170) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KAPE 185:188) binding
- L186 (≠ V195) binding
- SSAT 236:239 (≠ SVAV 239:242) binding
- V251 (≠ M254) binding in other chain
- L258 (= L261) binding
- W285 (≠ R288) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E391) binding
- A441 (≠ V442) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ P451) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F457) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K461) binding
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
32% identity, 96% coverage: 15:483/490 of query aligns to 14:486/491 of 5gtlA
- active site: N165 (= N162), K188 (= K185), E263 (= E260), C297 (= C294), E394 (= E391), E471 (= E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ F158), P163 (= P160), K188 (= K185), A190 (≠ P187), E191 (= E188), Q192 (≠ E189), G221 (≠ P218), G225 (≠ S222), G241 (= G238), S242 (= S239), T245 (≠ V242), L264 (= L261), C297 (= C294), E394 (= E391), F396 (= F393)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
32% identity, 96% coverage: 15:483/490 of query aligns to 14:486/491 of 5gtkA
- active site: N165 (= N162), K188 (= K185), E263 (= E260), C297 (= C294), E394 (= E391), E471 (= E468)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ F158), I162 (≠ T159), P163 (= P160), W164 (= W161), K188 (= K185), E191 (= E188), G221 (≠ P218), G225 (≠ S222), A226 (≠ S223), F239 (≠ L236), G241 (= G238), S242 (= S239), T245 (≠ V242), Y248 (≠ H245), L264 (= L261), C297 (= C294), Q344 (≠ R341), R347 (≠ A344), E394 (= E391), F396 (= F393)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
34% identity, 96% coverage: 16:485/490 of query aligns to 4:482/495 of 4v37A
- active site: N157 (= N162), K180 (= K185), E255 (= E260), A289 (≠ C294), E388 (= E391), E465 (= E468)
- binding 3-aminopropan-1-ol: C448 (≠ P451), W454 (≠ F457)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F158), S154 (≠ T159), P155 (= P160), W156 (= W161), N157 (= N162), M162 (≠ A167), K180 (= K185), S182 (≠ P187), E183 (= E188), G213 (≠ P218), G217 (≠ S222), A218 (≠ S223), T232 (= T237), G233 (= G238), S234 (= S239), T237 (≠ V242), E255 (= E260), L256 (= L261), A289 (≠ C294), E388 (= E391), F390 (= F393)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 96% coverage: 15:483/490 of query aligns to 1:475/489 of 4o6rA
- active site: N150 (= N162), K173 (= K185), E248 (= E260), C282 (= C294), E383 (= E391), E460 (= E468)
- binding adenosine monophosphate: I146 (≠ F158), V147 (≠ T159), K173 (= K185), G206 (≠ P218), G210 (≠ S222), Q211 (≠ S223), F224 (≠ L236), G226 (= G238), S227 (= S239), T230 (≠ V242), R233 (≠ H245)
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)
31% identity, 95% coverage: 21:487/490 of query aligns to 21:495/505 of 4neaA
- active site: N166 (= N162), K189 (= K185), E264 (= E260), C298 (= C294), E399 (= E391), E476 (= E468)
- binding nicotinamide-adenine-dinucleotide: P164 (= P160), K189 (= K185), E192 (= E188), G222 (≠ P218), G226 (≠ S222), G242 (= G238), G243 (≠ S239), T246 (≠ V242), H249 (= H245), I250 (≠ L246), C298 (= C294), E399 (= E391), F401 (= F393)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
32% identity, 94% coverage: 21:483/490 of query aligns to 13:477/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F158), T153 (= T159), P154 (= P160), K179 (= K185), A212 (≠ P218), K213 (≠ A219), F230 (≠ L236), T231 (= T237), G232 (= G238), S233 (= S239), V236 (= V242), W239 (≠ H245), G256 (= G262)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
31% identity, 98% coverage: 12:489/490 of query aligns to 2:482/490 of 5ekcE
- active site: N154 (= N162), K177 (= K185), E252 (= E260), C286 (= C294), E381 (= E391), E459 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ F158), T151 (= T159), P152 (= P160), W153 (= W161), K177 (= K185), S180 (≠ E188), G210 (≠ P218), G214 (≠ S222), F228 (≠ L236), G230 (= G238), E231 (≠ S239), T234 (≠ V242), N331 (≠ S338), R333 (= R340), Q334 (≠ R341)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
32% identity, 97% coverage: 15:487/490 of query aligns to 5:477/477 of 2opxA
- active site: N151 (= N162), K174 (= K185), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ R117), F152 (≠ V163), N284 (≠ A295), F312 (≠ V323), G313 (≠ A324), R318 (≠ K330), D320 (= D332), I321 (= I333), A322 (vs. gap), Y362 (= Y372), F440 (≠ A450), F440 (≠ A450), E441 (≠ P451)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
31% identity, 96% coverage: 18:489/490 of query aligns to 1:475/482 of 5ek6A
- active site: N147 (= N162), K170 (= K185), E245 (= E260), C279 (= C294), E374 (= E391), E452 (= E468)
- binding 2-methylpropanal: I152 (≠ A167), K155 (≠ R170), T222 (= T237), E245 (= E260), F441 (= F457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F158), T144 (= T159), W146 (= W161), N147 (= N162), I152 (≠ A167), K170 (= K185), A172 (≠ P187), S173 (≠ E188), P202 (≠ N217), G203 (≠ P218), G207 (≠ S222), F221 (≠ L236), T222 (= T237), G223 (= G238), E224 (≠ S239), T227 (≠ V242), I231 (≠ L246), E245 (= E260), L246 (= L261), C279 (= C294), E374 (= E391)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
31% identity, 96% coverage: 18:489/490 of query aligns to 1:475/482 of 4h73A
- active site: N147 (= N162), K170 (= K185), E245 (= E260), C279 (= C294), E374 (= E391), E452 (= E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F158), T144 (= T159), P145 (= P160), W146 (= W161), K170 (= K185), A172 (≠ P187), S173 (≠ E188), G203 (≠ P218), G207 (≠ S222), F221 (≠ L236), G223 (= G238), E224 (≠ S239), T227 (≠ V242)
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)
32% identity, 97% coverage: 15:487/490 of query aligns to 7:479/479 of P25553
- L150 (≠ T159) binding
- R161 (= R170) binding
- KPSE 176:179 (≠ KAPE 185:188) binding
- F180 (≠ E189) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ S223) binding
- S230 (= S239) binding
- E251 (= E260) binding
- N286 (≠ A295) 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 (≠ A344) binding
- E443 (≠ P451) binding
- H449 (≠ F457) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>Pf6N2E2_1919 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1919
MSIETNNNVIADADHPRVGLFIDGEWIFDRPSCFEVLDPSTEASLTSVPGATTADLKRVL
AAAERGFKIWRDTPPAERNIIISRAIAGVRSRSEEIAQIITRENGKLIADARAEVERSAS
FFDWDMAQALRAYGTIVPGEAQMQKSILRQPIGPVAAFTPWNVPLSAPSRKISGALCAGC
SIILKAPEETPGAAVAMVQCFERAGLPKGVLNLVFGNPALVSSTLIESPVTRMVTLTGSV
AVGKHLSQLAGAAMKPVLMELGGHAPVIVCEGVNAAEIGKMALKSKIRINAQWCAAPGRF
LVHESIYDEFVAAFVATADQVRVADGMDTKADIGPVTSVRRLAAMQHFVDDALARGGKVA
VGGHRVGERGYYFAPTLLVDTPLDCAIMTDEPFGPVAVAVRFSTLDEAIEISNSLSVGLA
AFAFTNSLEQAERLSRELDVGVLSINHFGAPDPDTPFGGVKDSGIGREGGPWSLDSYMVS
KTVLQKTARV
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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