SitesBLAST
Comparing RR42_RS21375 FitnessBrowser__Cup4G11:RR42_RS21375 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)
67% identity, 99% coverage: 1:484/488 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
67% identity, 99% coverage: 2:484/488 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E258), C288 (= C292), E385 (= E389), E462 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (≠ E183), A212 (= A213), G216 (= G220), G232 (= G236), S233 (= S237), I236 (≠ V240), C288 (= C292), K338 (= K342), E385 (= E389), F387 (= F391)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
64% identity, 99% coverage: 3:486/488 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ A214), F230 (= F234), T231 (= T235), G232 (= G236), S233 (= S237), V236 (= V240), W239 (≠ I243), G256 (= G260)
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)
57% identity, 98% coverage: 8:486/488 of query aligns to 58:535/535 of P51649
- C93 (≠ M45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ A132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P134) 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 (≠ S207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G220) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 236:241) binding
- R334 (= R286) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N287) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C292) modified: Disulfide link with 342, In inhibited form
- C342 (= C294) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ H323) natural variant: N -> S
- P382 (= P333) to L: in SSADHD; 2% of activity
- V406 (≠ L357) to I: in dbSNP:rs143741652
- G409 (= G360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S449) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G484) 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)
57% identity, 98% coverage: 8:486/488 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
57% identity, 98% coverage: 8:486/488 of query aligns to 8:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
40% identity, 96% coverage: 10:479/488 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N157), E246 (= E258), C280 (= C292), E458 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (≠ E183), G204 (≠ A213), G208 (= G220), T223 (= T235), G224 (= G236), S225 (= S237), A228 (≠ V240), S231 (≠ I243), I232 (≠ L244), E246 (= E258), L247 (= L259), C280 (= C292), E381 (= E389), F383 (= F391), H447 (≠ F455)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 98% coverage: 7:483/488 of query aligns to 1:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E258), C283 (= C292), E380 (= E389), E457 (= E466)
- binding glycerol: D15 (≠ S21), A16 (= A22), A17 (≠ D23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (= A214), S211 (≠ G220), G227 (= G236), S228 (= S237), V231 (= V240), R329 (≠ D338), R330 (≠ A339), E380 (= E389), F382 (= F391)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 98% coverage: 7:483/488 of query aligns to 1:474/476 of 5x5tA
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 96% coverage: 10:479/488 of query aligns to 9:485/505 of O24174
- N164 (= N157) 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 (≠ R165) 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.
7radA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 5:483/488 of query aligns to 7:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I153), I159 (≠ T154), P160 (= P155), W161 (= W156), N162 (= N157), M167 (= M162), K185 (= K180), E188 (= E183), G218 (≠ A213), G222 (= G220), A223 (= A221), T237 (= T235), G238 (= G236), S239 (= S237), V242 (= V240), E261 (= E258), L262 (= L259), C295 (= C292), E392 (= E389), F394 (= F391)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ A113), E117 (= E117), F163 (= F158), E285 (≠ A282), F289 (≠ R286), N450 (≠ L447), V452 (≠ S449)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 5:483/488 of query aligns to 7:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I153), I159 (≠ T154), P160 (= P155), W161 (= W156), N162 (= N157), M167 (= M162), K185 (= K180), E188 (= E183), G218 (≠ A213), G222 (= G220), F236 (= F234), T237 (= T235), G238 (= G236), S239 (= S237), V242 (= V240), E261 (= E258), L262 (= L259), C295 (= C292), E392 (= E389), F394 (= F391)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (= E117), E285 (≠ A282), F289 (≠ R286), N450 (≠ L447), V452 (≠ S449)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 98% coverage: 5:483/488 of query aligns to 7:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I153), I159 (≠ T154), P160 (= P155), W161 (= W156), N162 (= N157), K185 (= K180), E188 (= E183), G218 (≠ A213), G222 (= G220), T237 (= T235), G238 (= G236), S239 (= S237), V242 (= V240), E261 (= E258), L262 (= L259), C295 (= C292), E392 (= E389), F394 (= F391)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
39% identity, 96% coverage: 11:479/488 of query aligns to 38:507/518 of Q63639
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 96% coverage: 11:479/488 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N157), K177 (= K180), E253 (= E258), C287 (= C292), E384 (= E389), D461 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I150 (= I153), V151 (≠ T154), P152 (= P155), W153 (= W156), K177 (= K180), E180 (= E183), G210 (≠ A213), G214 (= G220), A215 (= A221), F228 (= F234), G230 (= G236), S231 (= S237), V234 (= V240), E253 (= E258), G255 (= G260), C287 (= C292), Q334 (≠ A339), K337 (= K342), E384 (= E389), F386 (= F391)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
38% identity, 96% coverage: 11:479/488 of query aligns to 12:481/492 of 6b5hA
- active site: N161 (= N157), E260 (= E258), C294 (= C292), E468 (= E466)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ E108), G116 (≠ A112), F162 (= F158), W169 (≠ R165), Q284 (≠ A282), F288 (≠ R286), T295 (≠ V293), N449 (≠ L447), L451 (≠ S449), N452 (= N450), F457 (= F455)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), W160 (= W156), N161 (= N157), K184 (= K180), G217 (≠ A213), G221 (= G220), F235 (= F234), T236 (= T235), G237 (= G236), S238 (= S237), V241 (= V240), E260 (= E258), L261 (= L259), C294 (= C292), F393 (= F391)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
38% identity, 96% coverage: 11:479/488 of query aligns to 12:481/492 of 6b5gA
- active site: N161 (= N157), E260 (= E258), C294 (= C292), E468 (= E466)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F158), L165 (≠ A161), W169 (≠ R165), F288 (≠ R286), C293 (≠ T291), C294 (= C292), T295 (≠ V293), N449 (≠ L447), L451 (≠ S449)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), P159 (= P155), W160 (= W156), N161 (= N157), M166 (= M162), K184 (= K180), E187 (= E183), G217 (≠ A213), G221 (= G220), F235 (= F234), T236 (= T235), G237 (= G236), S238 (= S237), V241 (= V240), E260 (= E258), L261 (= L259), C294 (= C292), E391 (= E389), F393 (= F391)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
38% identity, 96% coverage: 11:479/488 of query aligns to 12:481/492 of 6aljA
- active site: N161 (= N157), E260 (= E258), C294 (= C292), E468 (= E466)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A112), F162 (= F158), L165 (≠ A161), M166 (= M162), W169 (≠ R165), E260 (= E258), C293 (≠ T291), C294 (= C292), L451 (≠ S449), N452 (= N450), A453 (≠ E451)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), P159 (= P155), W160 (= W156), N161 (= N157), K184 (= K180), E187 (= E183), G217 (≠ A213), G221 (= G220), F235 (= F234), G237 (= G236), S238 (= S237), V241 (= V240), Q341 (≠ A339), K344 (= K342), E391 (= E389), F393 (= F391)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
38% identity, 96% coverage: 11:479/488 of query aligns to 38:507/518 of O94788
- E50 (≠ D23) to G: in dbSNP:rs34266719
- A110 (≠ Y80) to V: in dbSNP:rs35365164
- Q182 (≠ A152) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 154:156) binding
- KPAE 210:213 (= KPAE 180:183) binding
- STE 264:266 (= STE 237:239) binding
- C320 (= C292) active site, Nucleophile
- R347 (≠ L319) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K320) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ DAVAK 338:342) binding
- A383 (= A355) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E389) binding
- E436 (≠ N408) to K: in dbSNP:rs34744827
- S461 (≠ A433) to Y: in DIH4; decreased retinoic acid biosynthetic process
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 97% coverage: 6:479/488 of query aligns to 6:482/494 of 4pz2B
- active site: N159 (= N157), K182 (= K180), E258 (= E258), C292 (= C292), E392 (= E389), D469 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I155 (= I153), I156 (≠ T154), P157 (= P155), W158 (= W156), N159 (= N157), M164 (= M162), K182 (= K180), A184 (= A182), E185 (= E183), G215 (≠ A213), G219 (= G220), F233 (= F234), T234 (= T235), G235 (= G236), S236 (= S237), V239 (= V240), E258 (= E258), L259 (= L259), C292 (= C292), E392 (= E389), F394 (= F391)
Query Sequence
>RR42_RS21375 FitnessBrowser__Cup4G11:RR42_RS21375
MQLKDPTLLRSQAFIGGQWQSADSGATFPVTNPADGSLIGTVPLMGAAETTRAIEAARVA
QAAWRRKTARERAQVLRAWYDLMLANADDLAVLMTTEQGKPLAEARGEAVYAASFLEWFA
EQAKRVHGDVLATPASDKRLLVVKEPVGVCAAITPWNFPLAMITRKAGPALAAGCAMVLK
PAEDTPLSALALALLAERAGLPAGLLSVVTGDAASSIEIGAELTGSPVVRKLSFTGSTEV
GRILMRQSAPTIKKLSLELGGNAPFIVFDDADLDAAVEGAMASKYRNAGQTCVCANRLYV
HDKVYDAFAQKLVAAVKTLKVGHGLEPGVQQGPLINEDAVAKVEQHIADALGKGARLLTG
GKRHDLGGTFFEPTVLANVTPDMVVAKQETFGPLAPLFRFTSDEEVVNMANDTEFGLASY
FFSRDIGRIWRVAEALEYGMVGINTGLISNEVAPFGGVKQSGLGREGASYGIEEYLEVKY
LCMGGVDR
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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