SitesBLAST
Comparing GFF3462 FitnessBrowser__Marino:GFF3462 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)
45% identity, 97% coverage: 7:475/483 of query aligns to 8:474/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
45% identity, 97% coverage: 7:475/483 of query aligns to 7:473/481 of 3jz4A
- active site: N156 (= N156), K179 (= K179), E254 (= E255), C288 (= C289), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (= K179), A181 (= A181), S182 (= S182), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (≠ V237), C288 (= C289), K338 (= K339), E385 (= E387), F387 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
42% identity, 100% coverage: 2:482/483 of query aligns to 2:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I152), T153 (= T153), P154 (= P154), K179 (= K179), A212 (= A213), K213 (≠ S214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ K240), G256 (= G257)
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)
41% identity, 99% coverage: 4:482/483 of query aligns to 55:533/535 of P51649
- C93 (≠ M44) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (≠ A127) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P131) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ K133) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ K164) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C174) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 179:182) binding
- T233 (= T184) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ M188) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 233:238) binding
- R334 (= R283) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ G284) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C289) modified: Disulfide link with 342, In inhibited form
- C342 (= C291) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (≠ L354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ P447) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G482) 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)
41% identity, 99% coverage: 4:482/483 of query aligns to 5:483/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
41% identity, 99% coverage: 4:482/483 of query aligns to 5:483/485 of 2w8qA
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)
36% identity, 98% coverage: 6:479/483 of query aligns to 12:491/505 of 4neaA
- active site: N166 (= N156), K189 (= K179), E264 (= E255), C298 (= C289), E399 (= E387), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P154), K189 (= K179), E192 (≠ S182), G222 (≠ A213), G226 (= G217), G242 (= G233), G243 (≠ S234), T246 (≠ V237), H249 (≠ K240), I250 (≠ L241), C298 (= C289), E399 (= E387), F401 (= F389)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
34% identity, 97% coverage: 13:481/483 of query aligns to 13:489/505 of O24174
- N164 (= N156) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ K164) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
6popA Crystal structure of daua in complex with NADP+ (see paper)
34% identity, 98% coverage: 13:483/483 of query aligns to 7:473/475 of 6popA
- active site: N148 (= N156), E246 (= E255), C280 (= C289), D454 (≠ E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F144 (≠ I152), L145 (≠ T153), W147 (= W155), N148 (= N156), K171 (= K179), S173 (≠ A181), S174 (= S182), D204 (≠ A213), G208 (= G217), I223 (≠ T232), G224 (= G233), S225 (= S234), V228 (= V237), H231 (≠ K240), E246 (= E255), L247 (= L256), G248 (= G257), C280 (= C289), E378 (= E387), F380 (= F389), H443 (≠ F453)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
36% identity, 99% coverage: 1:479/483 of query aligns to 2:484/494 of 4pz2B
- active site: N159 (= N156), K182 (= K179), E258 (= E255), C292 (= C289), E392 (= E387), D469 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I155 (= I152), I156 (≠ T153), P157 (= P154), W158 (= W155), N159 (= N156), M164 (= M161), K182 (= K179), A184 (= A181), E185 (≠ S182), G215 (≠ A213), G219 (= G217), F233 (= F231), T234 (= T232), G235 (= G233), S236 (= S234), V239 (= V237), E258 (= E255), L259 (= L256), C292 (= C289), E392 (= E387), F394 (= F389)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
35% identity, 97% coverage: 13:479/483 of query aligns to 7:475/489 of 4o6rA
- active site: N150 (= N156), K173 (= K179), E248 (= E255), C282 (= C289), E383 (= E387), E460 (= E464)
- binding adenosine monophosphate: I146 (= I152), V147 (≠ T153), K173 (= K179), G206 (≠ A213), G210 (= G217), Q211 (≠ K218), F224 (= F231), G226 (= G233), S227 (= S234), T230 (≠ V237), R233 (≠ K240)
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, 97% coverage: 13:479/483 of query aligns to 11:482/497 of P17202
- I28 (≠ Y30) binding
- D96 (≠ E96) binding
- SPW 156:158 (≠ TPW 153:155) binding
- Y160 (≠ F157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ K164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAS 179:182) binding
- L186 (≠ E183) binding
- SSAT 236:239 (≠ STEV 234:237) binding
- V251 (= V249) binding in other chain
- L258 (= L256) binding
- W285 (≠ R283) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E387) binding
- A441 (≠ H438) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ P447) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F453) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K457) 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)
33% identity, 99% coverage: 2:479/483 of query aligns to 12:491/501 of Q56YU0
- G152 (≠ W139) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V404) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
34% identity, 97% coverage: 13:479/483 of query aligns to 9:480/495 of 4v37A
- active site: N157 (= N156), K180 (= K179), E255 (= E255), A289 (≠ C289), E388 (= E387), E465 (= E464)
- binding 3-aminopropan-1-ol: C448 (≠ P447), W454 (≠ F453)
- binding nicotinamide-adenine-dinucleotide: I153 (= I152), S154 (≠ T153), P155 (= P154), W156 (= W155), N157 (= N156), M162 (= M161), K180 (= K179), S182 (≠ A181), E183 (≠ S182), G213 (≠ A213), G217 (= G217), A218 (≠ K218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (≠ V237), E255 (= E255), L256 (= L256), A289 (≠ C289), E388 (= E387), F390 (= F389)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
34% identity, 99% coverage: 2:479/483 of query aligns to 9:486/491 of 5gtlA
- active site: N165 (= N156), K188 (= K179), E263 (= E255), C297 (= C289), E394 (= E387), E471 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I152), P163 (= P154), K188 (= K179), A190 (= A181), E191 (≠ S182), Q192 (≠ E183), G221 (≠ A213), G225 (= G217), G241 (= G233), S242 (= S234), T245 (≠ V237), L264 (= L256), C297 (= C289), E394 (= E387), F396 (= F389)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
34% identity, 99% coverage: 2:479/483 of query aligns to 9:486/491 of 5gtkA
- active site: N165 (= N156), K188 (= K179), E263 (= E255), C297 (= C289), E394 (= E387), E471 (= E464)
- binding nicotinamide-adenine-dinucleotide: I161 (= I152), I162 (≠ T153), P163 (= P154), W164 (= W155), K188 (= K179), E191 (≠ S182), G221 (≠ A213), G225 (= G217), A226 (≠ K218), F239 (= F231), G241 (= G233), S242 (= S234), T245 (≠ V237), Y248 (≠ K240), L264 (= L256), C297 (= C289), Q344 (≠ G336), R347 (≠ K339), E394 (= E387), F396 (= F389)
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
35% identity, 97% coverage: 13:479/483 of query aligns to 11:485/503 of Q93YB2
- I28 (≠ Y30) binding
- D99 (≠ E96) binding
- W161 (= W155) binding
- K185 (= K179) binding
- L189 (≠ E183) binding
- S239 (= S234) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
35% identity, 97% coverage: 13:479/483 of query aligns to 8:482/500 of 3iwjA
- active site: N159 (= N156), K182 (= K179), E257 (= E255), C291 (= C289), E390 (= E387), E467 (= E464)
- binding glycerol: D110 (≠ Y110), Y160 (≠ F157), W167 (≠ K164), I290 (≠ T288), C291 (= C289), C450 (≠ P447), W456 (≠ F453)
- binding nicotinamide-adenine-dinucleotide: I155 (= I152), T156 (= T153), W158 (= W155), K182 (= K179), S184 (≠ A181), E185 (≠ S182), G215 (≠ A213), A220 (≠ K218), F233 (= F231), G235 (= G233), S236 (= S234), T239 (≠ V237), I243 (≠ L241)
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
35% identity, 97% coverage: 13:479/483 of query aligns to 13:487/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
35% identity, 97% coverage: 13:479/483 of query aligns to 8:482/500 of 4i8pA
- active site: N159 (= N156), K182 (= K179), E257 (= E255), C291 (= C289), E390 (= E387), E467 (= E464)
- binding nicotinamide-adenine-dinucleotide: I155 (= I152), T156 (= T153), P157 (= P154), W158 (= W155), N159 (= N156), M164 (= M161), K182 (= K179), S184 (≠ A181), E185 (≠ S182), G215 (≠ A213), G219 (= G217), A220 (≠ K218), T234 (= T232), G235 (= G233), S236 (= S234), T239 (≠ V237), E257 (= E255), L258 (= L256), C291 (= C289), E390 (= E387), F392 (= F389), W456 (≠ F453)
Query Sequence
>GFF3462 FitnessBrowser__Marino:GFF3462
MIESPLLEKLTGYIGGRWTDNEHGNTFDVYNPATGKVIAQVASMSEDEVNAAVASGKSAL
RLTSPYSIETRRKWLEDIRDALKANKEEVGRILCMEHGKPLQEAQGEVDYAAGFFDYCSK
HIQALDAHTIPEKPKDCTWTVHYRPIGVTGLITPWNFPIGMIAKKLSAALAAGCPSVIKP
ASETPLTMIALFSLMDKHTDIPDGMVNLVMGKASVIGKVLCESPDVPMLSFTGSTEVGRK
LIVDTADQVKKLALELGGNAPFIVFDDADLDAAADNLIANKFRGGGQTCVCANRIFVHEK
VADAFGEKLAERVNKMTVGDGINGDVDLGPLINQAGYDKVKRHVQDALEKGATLVAGKKP
EDLGNDLFFPPTVVHGVNRDMCCYQEETFGPLVPMALFRTEEEVIEAGNDTEFGLASYVF
TNDAERAQRVAAGLRFGHCGWNTGTGPTPEAPFGGMKASGIGREGGLEGLFEFVEAQTVP
RGF
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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