SitesBLAST
Comparing GFF2064 FitnessBrowser__Marino:GFF2064 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
63% identity, 99% coverage: 3:486/489 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
63% identity, 99% coverage: 4:486/489 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (= E260), C288 (= C294), E385 (= E391), E462 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P157), W155 (= W158), K179 (= K182), A181 (= A184), S182 (≠ E185), A212 (= A218), G216 (= G222), G232 (= G238), S233 (= S239), I236 (≠ V242), C288 (= C294), K338 (= K344), E385 (= E391), F387 (= F393)
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)
58% identity, 98% coverage: 10:488/489 of query aligns to 58:535/535 of P51649
- C93 (≠ M47) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G130) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P134) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H136) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C177) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 182:185) binding
- T233 (= T187) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A191) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N209) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G222) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 238:243) binding
- R334 (= R288) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N289) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C294) modified: Disulfide link with 342, In inhibited form
- C342 (= C296) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P325) 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 (= S451) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G486) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
58% identity, 98% coverage: 10:488/489 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
58% identity, 98% coverage: 10:488/489 of query aligns to 8:485/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
56% identity, 99% coverage: 5:488/489 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I155), T153 (= T156), P154 (= P157), K179 (= K182), A212 (≠ S214), K213 (= K215), F230 (= F236), T231 (= T237), G232 (= G238), S233 (= S239), V236 (= V242), W239 (≠ L245), G256 (= G262)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
42% identity, 96% coverage: 14:481/489 of query aligns to 3:471/477 of 6j76A
- active site: N148 (= N159), E246 (= E260), C280 (= C294), E458 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I155), T145 (= T156), A146 (≠ P157), W147 (= W158), N148 (= N159), K171 (= K182), T173 (≠ A184), S174 (≠ E185), G204 (≠ A218), G208 (= G222), T223 (= T237), G224 (= G238), S225 (= S239), A228 (≠ V242), S231 (≠ L245), I232 (≠ L246), E246 (= E260), L247 (= L261), C280 (= C294), E381 (= E391), F383 (= F393), H447 (≠ F457)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 96% coverage: 16:485/489 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y113), F152 (= F160), N284 (≠ V295), F312 (≠ V323), G313 (= G324), R318 (≠ E328), D320 (≠ E330), I321 (≠ T331), A322 (≠ Q332), Y362 (≠ F372), F440 (≠ I450), F440 (≠ I450), E441 (≠ S451)
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)
39% identity, 96% coverage: 16:485/489 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I155), L148 (≠ T156), P149 (= P157), W150 (= W158), K174 (= K182), E177 (= E185), F178 (≠ D186), G207 (≠ A218), G211 (= G222), Q212 (≠ S223), S228 (= S239), A231 (≠ V242), K234 (≠ L245), R334 (≠ K344)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 96% coverage: 16:485/489 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I155), L148 (≠ T156), P149 (= P157), W150 (= W158), K174 (= K182), S176 (≠ A184), E177 (= E185), R206 (≠ N217), G207 (≠ A218), G211 (= G222), Q212 (≠ S223), S228 (= S239), A231 (≠ V242), K234 (≠ L245), I235 (≠ L246), N328 (= N338), R334 (≠ K344), F383 (= F393)
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)
39% identity, 96% coverage: 16:485/489 of query aligns to 10:477/479 of P25553
- L150 (≠ T156) binding
- R161 (= R167) binding
- KPSE 176:179 (≠ KPAE 182:185) binding
- F180 (≠ D186) 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 (≠ V295) 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 (≠ K344) binding
- E443 (≠ S451) binding
- H449 (≠ F457) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 97% coverage: 9:481/489 of query aligns to 2:474/486 of 4pxlA
- active site: N154 (= N159), K177 (= K182), E253 (= E260), C287 (= C294), E384 (= E391), D461 (≠ E468)
- binding nicotinamide-adenine-dinucleotide: I150 (= I155), V151 (≠ T156), P152 (= P157), W153 (= W158), K177 (= K182), E180 (= E185), G210 (≠ K215), G214 (= G222), A215 (≠ S223), F228 (= F236), G230 (= G238), S231 (= S239), V234 (= V242), E253 (= E260), G255 (= G262), C287 (= C294), Q334 (≠ A341), K337 (= K344), E384 (= E391), F386 (= F393)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 97% coverage: 14:485/489 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E380 (= E391), E457 (= E468)
- binding glycerol: D15 (≠ T23), A16 (= A24), A17 (≠ K25), G19 (= G27)
- binding nicotinamide-adenine-dinucleotide: P149 (= P157), P207 (≠ A218), A208 (≠ V219), S211 (≠ G222), G227 (= G238), S228 (= S239), V231 (= V242), R329 (≠ A340), R330 (≠ A341), E380 (= E391), F382 (= F393)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 97% coverage: 14:485/489 of query aligns to 6:474/476 of 5x5tA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
41% identity, 97% coverage: 9:481/489 of query aligns to 7:482/494 of 4pz2B
- active site: N159 (= N159), K182 (= K182), E258 (= E260), C292 (= C294), E392 (= E391), D469 (≠ E468)
- binding nicotinamide-adenine-dinucleotide: I155 (= I155), I156 (≠ T156), P157 (= P157), W158 (= W158), N159 (= N159), M164 (= M164), K182 (= K182), A184 (= A184), E185 (= E185), G215 (≠ K215), G219 (= G222), F233 (= F236), T234 (= T237), G235 (= G238), S236 (= S239), V239 (= V242), E258 (= E260), L259 (= L261), C292 (= C294), E392 (= E391), F394 (= F393)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 98% coverage: 5:481/489 of query aligns to 6:483/489 of 7a6qB
- active site: N163 (= N159), E262 (= E260), C296 (= C294), E470 (= E468)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), W162 (= W158), K186 (= K182), E189 (= E185), G219 (≠ K215), G223 (= G222), S240 (= S239), V243 (= V242), K342 (≠ A340)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A31), T33 (≠ V32), C34 (≠ N33), P36 (= P35), D103 (≠ E99), E189 (= E185), Q190 (≠ D186), F218 (≠ S214), I339 (= I337), D340 (≠ N338)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ Y113), D141 (= D139), N143 (≠ R141), N451 (≠ I449), L453 (≠ S451), A455 (≠ E453)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 98% coverage: 5:481/489 of query aligns to 6:483/489 of 7a6qA
- active site: N163 (= N159), E262 (= E260), C296 (= C294), E470 (= E468)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), T160 (= T156), W162 (= W158), K186 (= K182), A188 (= A184), E189 (= E185), G219 (≠ K215), G223 (= G222), S240 (= S239), V243 (= V242), K342 (≠ A340), K346 (= K344)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ Y113), D141 (= D139), N143 (≠ R141), N451 (≠ I449), L453 (≠ S451), Y454 (≠ T452)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
39% identity, 98% coverage: 5:481/489 of query aligns to 6:483/489 of 5fhzA
- active site: N163 (= N159), K186 (= K182), E262 (= E260), C296 (= C294), E393 (= E391), E470 (= E468)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), T160 (= T156), W162 (= W158), K186 (= K182), E189 (= E185), G219 (≠ K215), G223 (= G222), F237 (= F236), G239 (= G238), S240 (= S239), T241 (= T240), V243 (= V242), G264 (= G262), Q343 (≠ A341), E393 (= E391)
- binding retinoic acid: G118 (≠ Y113), R121 (≠ S116), F164 (= F160), M168 (= M164), W171 (≠ R167), C295 (≠ T293), C296 (= C294), L453 (≠ S451)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
39% identity, 98% coverage: 5:481/489 of query aligns to 24:501/512 of P47895
- R89 (= R67) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K182) binding
- E207 (= E185) binding
- GSTEVG 257:262 (≠ GSTPVG 238:243) binding
- Q361 (≠ A341) binding
- E411 (= E391) binding
- A493 (≠ G473) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
39% identity, 98% coverage: 5:481/489 of query aligns to 5:482/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I155), T159 (= T156), P160 (= P157), W161 (= W158), K185 (= K182), E188 (= E185), G218 (≠ K215), G222 (= G222), F236 (= F236), S239 (= S239), V242 (= V242)
Query Sequence
>GFF2064 FitnessBrowser__Marino:GFF2064
MSLELKNRELLREQAYINGQWITAKSGKTFAVNDPANGEQLATVPDMDDTDARAAIEAAS
AAWPAWRSTPAKERANILRKWFNLLMANQEDLARLMTAEQGKPLAESRGEVGYGASFIEW
FAEEAKRAYGDVIPGHGKDKRIVVIKQPVGVVAAITPWNFPIAMITRKVAPALAAGCPVV
VKPAEDTPLSALAITALAEEAGVPAGLINIITCSKPNAVSVGSELTGNPIVRKVSFTGST
PVGKLLMRQASDTVKKVSLELGGNAPFIVFDDADLDAAVAGLMASKYRNTGQTCVCANRV
YVQAGVYDAFAEKLKAAVSKMVVGPGLEGETQQGPLINDAALAKVKRHIEDATSKGAKVA
LGGRAHSLGGTFFEPTILTHATQEMLIAREETFGPVAPLFKFETDDEAIAMANDSEFGLS
AYFYSRNIHRVWRVAEELESGMIGVNEGIISTEVAPFGGVKESGLGREGSHYGLDEYMEL
KYLCLGGMK
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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