SitesBLAST
Comparing SM_b20378 FitnessBrowser__Smeli:SM_b20378 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
48% identity, 97% coverage: 10:480/487 of query aligns to 2:473/476 of 5x5uA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (≠ Y23), A16 (≠ E24), A17 (= A25), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P156), P207 (= P214), A208 (= A215), S211 (= S218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (= R336), R330 (= R337), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
48% identity, 97% coverage: 10:480/487 of query aligns to 2:473/476 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)
39% identity, 95% coverage: 16:479/487 of query aligns to 14:478/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 95% coverage: 16:479/487 of query aligns to 13:477/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C290), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (= W157), K179 (= K181), A181 (≠ P183), S182 (≠ G184), A212 (≠ P214), G216 (≠ S218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (≠ A340), E385 (= E387), F387 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
40% identity, 95% coverage: 16:479/487 of query aligns to 13:477/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F154), T153 (= T155), P154 (= P156), K179 (= K181), A212 (≠ P214), K213 (≠ A215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ H241), G256 (= G258)
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)
39% identity, 96% coverage: 12:480/487 of query aligns to 60:531/535 of P51649
- C93 (≠ A46) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G129) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (vs. gap) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P133) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R166) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C176) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGPG 181:184) binding
- T233 (≠ S186) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ T190) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N208) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVEVG 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 (≠ S292) 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 (≠ I355) to I: in dbSNP:rs143741652
- G409 (= G358) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A447) 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)
39% identity, 96% coverage: 12:480/487 of query aligns to 10:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
39% identity, 96% coverage: 12:480/487 of query aligns to 10:481/485 of 2w8qA
7radA Crystal structure analysis of aldh1b1
36% identity, 100% coverage: 1:487/487 of query aligns to 6:490/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ F154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (≠ Q163), K185 (= K181), E188 (≠ G184), G218 (≠ P214), G222 (≠ S218), A223 (≠ E219), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (= E105), F163 (= F159), E285 (≠ G280), F289 (≠ R284), N450 (≠ G445), V452 (≠ A447)
7mjdA Crystal structure analysis of aldh1b1
36% identity, 100% coverage: 1:487/487 of query aligns to 6:490/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ F154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (≠ Q163), K185 (= K181), E188 (≠ G184), G218 (≠ P214), G222 (≠ S218), F236 (= F232), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (= E105), E285 (≠ G280), F289 (≠ R284), N450 (≠ G445), V452 (≠ A447)
7mjcA Crystal structure analysis of aldh1b1
36% identity, 100% coverage: 1:487/487 of query aligns to 6:490/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ F154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), K185 (= K181), E188 (≠ G184), G218 (≠ P214), G222 (≠ S218), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
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)
33% identity, 95% coverage: 17:479/487 of query aligns to 22:491/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (= E256), C298 (= C290), E399 (= E387), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P156), K189 (= K181), E192 (≠ G184), G222 (≠ P214), G226 (≠ S218), G242 (= G234), G243 (≠ S235), T246 (≠ V238), H249 (= H241), I250 (≠ L242), C298 (= C290), E399 (= E387), F401 (= F389)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
33% identity, 99% coverage: 1:480/487 of query aligns to 9:495/498 of 4go2A
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E387), D479 (≠ E464)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ F154), I167 (≠ T155), P168 (= P156), W169 (= W157), K193 (= K181), A195 (≠ P183), Q196 (≠ G184), S225 (≠ D213), G226 (≠ P214), G230 (≠ S218), Q231 (≠ E219), F244 (= F232), G246 (= G234), S247 (= S235), V250 (= V238), I254 (vs. gap), E269 (= E256), G271 (= G258), C303 (= C290), E400 (= E387), F402 (= F389)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
33% identity, 99% coverage: 1:480/487 of query aligns to 9:495/498 of 2o2rA
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E387), D479 (≠ E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ F154), I167 (≠ T155), W169 (= W157), K193 (= K181), A195 (≠ P183), Q196 (≠ G184), S225 (≠ D213), G226 (≠ P214), G230 (≠ S218), Q231 (≠ E219), F244 (= F232), S247 (= S235), V250 (= V238), I254 (vs. gap)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
33% identity, 99% coverage: 1:480/487 of query aligns to 94:580/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K181), S310 (≠ D213), G311 (≠ P214), G315 (≠ S218), G331 (= G234), S332 (= S235), V335 (= V238)
- binding 4'-phosphopantetheine: K201 (≠ G108), F382 (≠ R284), N387 (≠ V289), C388 (= C290), N545 (≠ G445)
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)
33% identity, 99% coverage: 1:480/487 of query aligns to 413:899/902 of P28037
- IPW 571:573 (≠ TPW 155:157) binding
- KPAQ 597:600 (≠ KGPG 181:184) binding
- GSLVGQ 630:635 (≠ PAHLSE 214:219) binding
- GS 650:651 (= GS 234:235) binding
- E673 (= E256) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 256:257) binding
- C707 (= C290) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ A340) binding
- ESF 804:806 (≠ EPF 387:389) 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.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 98% coverage: 1:479/487 of query aligns to 5:486/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E387), E471 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ F154), P163 (= P156), K188 (= K181), A190 (≠ P183), E191 (≠ G184), Q192 (≠ E185), G221 (≠ P214), G225 (≠ S218), G241 (= G234), S242 (= S235), T245 (≠ V238), L264 (= L257), C297 (= C290), E394 (= E387), F396 (= F389)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 98% coverage: 1:479/487 of query aligns to 5:486/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E387), E471 (= E464)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ F154), I162 (≠ T155), P163 (= P156), W164 (= W157), K188 (= K181), E191 (≠ G184), G221 (≠ P214), G225 (≠ S218), A226 (≠ E219), F239 (= F232), G241 (= G234), S242 (= S235), T245 (≠ V238), Y248 (≠ H241), L264 (= L257), C297 (= C290), Q344 (≠ R337), R347 (≠ A340), E394 (= E387), F396 (= F389)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
34% identity, 96% coverage: 15:480/487 of query aligns to 8:477/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E256), C287 (= C290), E384 (= E387), D461 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ F154), V151 (≠ T155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (≠ G184), G210 (≠ P214), G214 (≠ S218), A215 (≠ E219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (= V238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (≠ R337), K337 (≠ A340), E384 (= E387), F386 (= F389)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
35% identity, 97% coverage: 10:479/487 of query aligns to 3:478/489 of 4cazA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C290), E386 (= E387), E463 (= E464)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (≠ F154), G149 (≠ T155), W151 (= W157), N152 (= N158), K175 (= K181), E178 (≠ G184), G208 (≠ P214), G212 (≠ S218), F226 (= F232), T227 (= T233), G228 (= G234), G229 (≠ S235), T232 (≠ V238), V236 (vs. gap), E251 (= E256), L252 (= L257), C285 (= C290), E386 (= E387), F388 (= F389)
Query Sequence
>SM_b20378 FitnessBrowser__Smeli:SM_b20378
MNPETTAVPYERLGILIDGRWIYEAERSTEVVDPATGQTIARLPFAADGEIAEAVASSQR
AFESWKDRSPLERGRILRRFADLARKHADEIARNMTRDQGKPLSEAIGEIRFAADHADWH
AEEARRIYGRVIPARDPRVQQMVLREPVGVCIAFTPWNFPFSQALRKVVAALASGCTIIL
KGPGESPSSTVAIGRLMQEAGLPDGCLNILWGDPAHLSETLLAAPEVRKISFTGSVEVGK
HLASLAGRHMKRSTMELGGHAPVILFDDADIEAAADALAGQKVRNAGQVCISPTRFYVQA
KGHDRFLARFAEKIASTRVGNGFQESVQMGPLCHGRRVAAMEGFIQDAREQGAEIVTGGE
RVGNAGFFYAPTVVAAGTDELRLMKEEPFGPIAVVTPFGDFDEVIRRANSLPFGLASYVF
TGSSSRAQNAARALAAGMVSVNHFGLALPETPFGGINDSGYGSEGGSETFDGYLNTKFVT
RFDQIPQ
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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