SitesBLAST
Comparing WP_086510137.1 NCBI__GCF_002151265.1:WP_086510137.1 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
51% identity, 96% coverage: 11:489/497 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N165), K179 (= K188), E254 (= E263), C288 (= C297), E385 (= E394), E462 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P163), W155 (= W164), K179 (= K188), A181 (= A190), S182 (≠ G191), A212 (≠ P221), G216 (≠ S225), G232 (= G241), S233 (= S242), I236 (≠ V245), C288 (= C297), K338 (= K347), E385 (= E394), F387 (= F396)
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)
51% identity, 96% coverage: 11:489/497 of query aligns to 3:481/482 of P25526
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
45% identity, 97% coverage: 11:491/497 of query aligns to 20:500/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I161), A171 (≠ T162), P172 (= P163), W173 (= W164), K197 (= K188), A230 (≠ P221), F248 (= F239), G250 (= G241), S251 (= S242), V254 (= V245), M257 (≠ L248), L273 (= L264), C306 (= C297), K356 (= K347), E403 (= E394), F405 (= F396)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
48% identity, 97% coverage: 11:491/497 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I161), T153 (= T162), P154 (= P163), K179 (= K188), A212 (≠ P221), K213 (≠ A222), F230 (= F239), T231 (= T240), G232 (= G241), S233 (= S242), V236 (= V245), W239 (≠ L248), G256 (= G265)
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)
49% identity, 96% coverage: 16:491/497 of query aligns to 58:535/535 of P51649
- C93 (≠ L53) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G136) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P140) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H142) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R173) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C183) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAG 188:191) binding
- T233 (= T193) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A197) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N215) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S225) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTRVG 241:246) binding
- R334 (≠ Q291) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ T292) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C297) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A299) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N328) natural variant: N -> S
- P382 (= P338) to L: in SSADHD; 2% of activity
- V406 (≠ L362) to I: in dbSNP:rs143741652
- G409 (= G365) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ T454) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G489) 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)
48% identity, 96% coverage: 16:491/497 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
48% identity, 96% coverage: 16:491/497 of query aligns to 8:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
39% identity, 93% coverage: 23:484/497 of query aligns to 9:470/476 of 5x5uA
- active site: N151 (= N165), K174 (= K188), E249 (= E263), C283 (= C297), E380 (= E394), E457 (= E471)
- binding glycerol: D15 (≠ H29), A16 (≠ G30), A17 (≠ D31), G19 (= G33)
- binding nicotinamide-adenine-dinucleotide: P149 (= P163), P207 (= P221), A208 (= A222), S211 (= S225), G227 (= G241), S228 (= S242), V231 (= V245), R329 (≠ Q343), R330 (≠ A344), E380 (= E394), F382 (= F396)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
39% identity, 93% coverage: 23:484/497 of query aligns to 9:470/476 of 5x5tA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 96% coverage: 10:484/497 of query aligns to 2:482/494 of 4pz2B
- active site: N159 (= N165), K182 (= K188), E258 (= E263), C292 (= C297), E392 (= E394), D469 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I155 (= I161), I156 (≠ T162), P157 (= P163), W158 (= W164), N159 (= N165), M164 (= M170), K182 (= K188), A184 (= A190), E185 (≠ G191), G215 (≠ P221), G219 (≠ S225), F233 (= F239), T234 (= T240), G235 (= G241), S236 (= S242), V239 (= V245), E258 (= E263), L259 (= L264), C292 (= C297), E392 (= E394), F394 (= F396)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
37% identity, 93% coverage: 22:484/497 of query aligns to 21:492/498 of 4go2A
- active site: N170 (= N165), K193 (= K188), E269 (= E263), C303 (= C297), E400 (= E394), D479 (≠ E471)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (≠ T162), P168 (= P163), W169 (= W164), K193 (= K188), A195 (= A190), Q196 (≠ G191), S225 (≠ E220), G226 (≠ P221), G230 (≠ S225), Q231 (≠ K226), F244 (= F239), G246 (= G241), S247 (= S242), V250 (= V245), I254 (≠ L249), E269 (= E263), G271 (= G265), C303 (= C297), E400 (= E394), F402 (= F396)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
37% identity, 93% coverage: 22:484/497 of query aligns to 21:492/498 of 2o2rA
- active site: N170 (= N165), K193 (= K188), E269 (= E263), C303 (= C297), E400 (= E394), D479 (≠ E471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I161), I167 (≠ T162), W169 (= W164), K193 (= K188), A195 (= A190), Q196 (≠ G191), S225 (≠ E220), G226 (≠ P221), G230 (≠ S225), Q231 (≠ K226), F244 (= F239), S247 (= S242), V250 (= V245), I254 (≠ L249)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
37% identity, 93% coverage: 22:484/497 of query aligns to 106:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K188), S310 (≠ E220), G311 (≠ P221), G315 (≠ S225), G331 (= G241), S332 (= S242), V335 (= V245)
- binding 4'-phosphopantetheine: K201 (≠ R114), F382 (≠ Q291), N387 (≠ D296), C388 (= C297), N545 (≠ K452)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
37% identity, 93% coverage: 22:484/497 of query aligns to 425:896/902 of P28037
- IPW 571:573 (≠ TPW 162:164) binding
- KPAQ 597:600 (≠ KPAG 188:191) binding
- GSLVGQ 630:635 (≠ PAEVSK 221:226) binding
- GS 650:651 (= GS 241:242) binding
- E673 (= E263) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 263:264) binding
- C707 (= C297) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K347) binding
- ESF 804:806 (≠ ENF 394:396) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
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)
37% identity, 94% coverage: 20:488/497 of query aligns to 444:921/923 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.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 93% coverage: 22:484/497 of query aligns to 20:484/491 of 5gtlA
- active site: N165 (= N165), K188 (= K188), E263 (= E263), C297 (= C297), E394 (= E394), E471 (= E471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I161), P163 (= P163), K188 (= K188), A190 (= A190), E191 (≠ G191), Q192 (≠ E192), G221 (≠ P221), G225 (≠ S225), G241 (= G241), S242 (= S242), T245 (≠ V245), L264 (= L264), C297 (= C297), E394 (= E394), F396 (= F396)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 93% coverage: 22:484/497 of query aligns to 20:484/491 of 5gtkA
- active site: N165 (= N165), K188 (= K188), E263 (= E263), C297 (= C297), E394 (= E394), E471 (= E471)
- binding nicotinamide-adenine-dinucleotide: I161 (= I161), I162 (≠ T162), P163 (= P163), W164 (= W164), K188 (= K188), E191 (≠ G191), G221 (≠ P221), G225 (≠ S225), A226 (≠ K226), F239 (= F239), G241 (= G241), S242 (= S242), T245 (≠ V245), Y248 (≠ L248), L264 (= L264), C297 (= C297), Q344 (≠ A344), R347 (≠ K347), E394 (= E394), F396 (= F396)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 93% coverage: 13:473/497 of query aligns to 2:461/490 of 5ekcE
- active site: N154 (= N165), K177 (= K188), E252 (= E263), C286 (= C297), E381 (= E394), E459 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I161), T151 (= T162), P152 (= P163), W153 (= W164), K177 (= K188), S180 (≠ G191), G210 (≠ P221), G214 (≠ S225), F228 (= F239), G230 (= G241), E231 (≠ S242), T234 (≠ V245), N331 (≠ H341), R333 (≠ Q343), Q334 (≠ A344)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
36% identity, 91% coverage: 22:473/497 of query aligns to 4:454/482 of 5ek6A
- active site: N147 (= N165), K170 (= K188), E245 (= E263), C279 (= C297), E374 (= E394), E452 (= E471)
- binding 2-methylpropanal: I152 (≠ M170), K155 (≠ R173), T222 (= T240), E245 (= E263), F441 (= F460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I161), T144 (= T162), W146 (= W164), N147 (= N165), I152 (≠ M170), K170 (= K188), A172 (= A190), S173 (≠ G191), P202 (≠ E220), G203 (≠ P221), G207 (≠ S225), F221 (= F239), T222 (= T240), G223 (= G241), E224 (≠ S242), T227 (≠ V245), I231 (≠ L249), E245 (= E263), L246 (= L264), C279 (= C297), E374 (= E394)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
36% identity, 91% coverage: 22:473/497 of query aligns to 4:454/482 of 4h73A
- active site: N147 (= N165), K170 (= K188), E245 (= E263), C279 (= C297), E374 (= E394), E452 (= E471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I161), T144 (= T162), P145 (= P163), W146 (= W164), K170 (= K188), A172 (= A190), S173 (≠ G191), G203 (≠ P221), G207 (≠ S225), F221 (= F239), G223 (= G241), E224 (≠ S242), T227 (≠ V245)
Query Sequence
>WP_086510137.1 NCBI__GCF_002151265.1:WP_086510137.1
MKLTNTLSTMLDDPRLFRQHAYVNGKWTHGDGGREETVFDPATGEVIGYIPWLEAHQIRE
AVDSADAAFVHWRALRADERAERLMAWHDLLQAHREDLAIIMTLEQGKPLPDARGEVEYG
ASFVRWFAEEGKRTFGETIPSHIPNAALGTLKEPVGIAALITPWNFPLAMITRKAAAALA
AGCTVVVKPAGETPFSALALAELAERAGIPAGVFNVVLGEPAEVSKILCAEERVKALSFT
GSTRVGRLLLEQSAQTVKRVSLELGGNAPFIVGPDMDPKEAAFAAVAAKFQTAGQDCLAA
NRILVHESIHDEFVEHFAERMAALTVGNGMESEVDLGPLIHRQAVDKAAAIVDDAISRGA
TLVAGDQTRAPGENFFMPTLLTGVTPQMKVWREENFAPVAGVTAYRDDDEVIEMANDTEY
GLAAYVYTHDIRRIWKLLRALEYGMVSVNSVKMTGPPVPFGGVKQSGLGREGGITGIDEY
LETKYYCLGALGSVSGS
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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