SitesBLAST
Comparing AZOBR_RS19635 AZOBR_RS19635 succinate-semialdehyde dehydrogenase 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)
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)
69% identity, 100% coverage: 1:483/485 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
69% identity, 99% coverage: 3:483/485 of query aligns to 2:481/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E256), C288 (= C290), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (≠ E183), A212 (≠ P214), G216 (= G218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (= K340), E385 (= E387), F387 (= F389)
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)
59% identity, 98% coverage: 7:482/485 of query aligns to 57:533/535 of P51649
- C93 (≠ V45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ F134) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R165) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C175) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 180:183) binding
- T233 (= T185) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A189) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 234:239) binding
- R334 (= R284) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N285) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C290) modified: Disulfide link with 342, In inhibited form
- C342 (= C292) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N321) natural variant: N -> S
- P382 (= P331) to L: in SSADHD; 2% of activity
- V406 (= V355) to I: in dbSNP:rs143741652
- G409 (= G358) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S447) 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)
58% identity, 98% coverage: 7:482/485 of query aligns to 7:483/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
58% identity, 98% coverage: 7:482/485 of query aligns to 7:483/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
59% identity, 99% coverage: 2:482/485 of query aligns to 1:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (≠ P214), K213 (≠ V215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ I241), G256 (= G258)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 97% coverage: 11:481/485 of query aligns to 5:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E256), C283 (= C290), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (= D21), A16 (= A22), A17 (≠ F23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (= P214), A208 (≠ V215), S211 (≠ G218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (≠ Q336), R330 (≠ A337), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 97% coverage: 11:481/485 of query aligns to 5:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
41% identity, 97% coverage: 10:481/485 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N157), E246 (= E256), C280 (= C290), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (≠ E183), G204 (≠ D213), G208 (= G218), T223 (= T233), G224 (= G234), S225 (= S235), A228 (≠ V238), S231 (≠ I241), I232 (≠ L242), E246 (= E256), L247 (= L257), C280 (= C290), E381 (= E387), F383 (= F389), H447 (≠ F453)
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
40% identity, 99% coverage: 3:483/485 of query aligns to 13:496/501 of P00352
- N121 (≠ G107) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPWN 154:157) binding
- I177 (≠ T164) to F: in dbSNP:rs8187929
- KPAE 193:196 (= KPAE 180:183) binding
- GP 226:227 (≠ DP 213:214) binding
- GS 246:247 (= GS 234:235) binding
- E269 (= E256) active site, Proton acceptor
- ELG 269:271 (= ELG 256:258) binding
- C302 (≠ T289) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C290) active site, Nucleophile
- EQYDK 349:353 (≠ QAVEK 336:340) binding
- EIF 400:402 (= EIF 387:389) binding
- G458 (= G444) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
4wb9A Human aldh1a1 complexed with nadh (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 5:488/493 of 4wb9A
- active site: N162 (= N157), K185 (= K180), E261 (= E256), C295 (= C290), E392 (= E387), E469 (= E464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I153), I159 (≠ T154), P160 (= P155), W161 (= W156), N162 (= N157), K185 (= K180), E188 (= E183), G218 (≠ D213), G222 (= G218), F236 (= F232), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), G263 (= G258), C295 (= C290), Q342 (≠ A337), K345 (= K340), E392 (= E387), F394 (= F389)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I153), I160 (≠ T154), P161 (= P155), W162 (= W156), N163 (= N157), K186 (= K180), E189 (= E183), G219 (≠ D213), G223 (= G218), F237 (= F232), T238 (= T233), G239 (= G234), S240 (= S235), V243 (= V238), E262 (= E256), G264 (= G258), Q343 (≠ A337), K346 (= K340), E393 (= E387), F395 (= F389)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ R165), H286 (≠ A280), Y290 (≠ R284), I297 (≠ V291), G451 (= G444)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 5l2nA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F158), M168 (= M162), W171 (≠ R165), H286 (≠ A280), G287 (≠ S281), Y290 (≠ R284), C295 (≠ T289), C296 (= C290), I297 (≠ V291), Y450 (≠ E443), G451 (= G444), V453 (≠ L446), F459 (= F453)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 5l2mA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F158), F283 (≠ G277), H286 (≠ A280), Y290 (≠ R284)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 4wpnA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (= F158), H286 (≠ A280), G287 (≠ S281), Y290 (≠ R284), C295 (≠ T289), I297 (≠ V291), G451 (= G444), V453 (≠ L446)
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 7jwwA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ Y111), T122 (≠ F115), F164 (= F158), M168 (= M162), Y290 (≠ R284), C295 (≠ T289), C296 (= C290), I297 (≠ V291), V453 (≠ L446), F459 (= F453)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 7jwvA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ Y111), T122 (≠ F115), F164 (= F158), M168 (= M162), Y290 (≠ R284), C295 (≠ T289), I297 (≠ V291), V453 (≠ L446), F459 (= F453)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 7jwuA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding nicotinamide-adenine-dinucleotide: I159 (= I153), I160 (≠ T154), P161 (= P155), W162 (= W156), N163 (= N157), K186 (= K180), E189 (= E183), G219 (≠ D213), G223 (= G218), A224 (≠ G219), F237 (= F232), T238 (= T233), G239 (= G234), S240 (= S235), V243 (= V238), L263 (= L257), C296 (= C290), Q343 (≠ A337), K346 (= K340), E393 (= E387), F395 (= F389)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-(pyridin-2-yl)ethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: T122 (≠ F115), F164 (= F158), W171 (≠ R165), Y290 (≠ R284), C295 (≠ T289), I297 (≠ V291), V453 (≠ L446), F459 (= F453)
7jwtA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
40% identity, 99% coverage: 3:483/485 of query aligns to 6:489/494 of 7jwtA
- active site: N163 (= N157), K186 (= K180), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E464)
- binding 6-{[(1R)-1-(3-hydroxyphenyl)ethyl]sulfanyl}-1-methyl-5-phenyl-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ Y111), T122 (≠ F115), F164 (= F158), M168 (= M162), W171 (≠ R165), Y290 (≠ R284), C295 (≠ T289), V453 (≠ L446), F459 (= F453)
Query Sequence
>AZOBR_RS19635 AZOBR_RS19635 succinate-semialdehyde dehydrogenase
LSLNDQSLLRTQAYVNGVWRDAFSGKTFAVTNPATGEELAQVADVGAEETRQAINAADAA
LPAWRAKTAKERAAILRRWFELIMAAQEDLAVLMTLEQGKPLAEARGEVAYGASFIEWFA
EEGKRVYGDVIPSFAGNKRIVVLKEPIGVVAAITPWNFPNAMITRKVGPALAAGCTIVVK
PAEDTPLSALALAELAERAGVPAGVFNIVTGSDPVAIGGELTASPIVRKLSFTGSTEVGK
ILMRQSADTVKKVSLELGGNAPFIVFDDADLDEAVKGALASKYRNSGQTCVCANRLLVQA
GVYDAFAAKLAEAVKQIRVGNGMEAGVTQGPMINGQAVEKVEELMGDALAKGAKVALGGK
RHGLGGTFFEPTILTGVTTEMRVAREEIFGPVAPLFKFETEADAIRMANDTEFGLAAYFY
SRDIGRVWRVAEQLEYGMVGINEGILSTEVAPFGGIKQSGIGREGSKYGVEDFLEIKYLC
VGLGA
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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