SitesBLAST
Comparing RR42_RS24555 FitnessBrowser__Cup4G11:RR42_RS24555 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)
61% identity, 97% coverage: 14:491/494 of query aligns to 2:479/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
60% identity, 97% coverage: 14:491/494 of query aligns to 1:478/481 of 3jz4A
- active site: N156 (= N169), K179 (≠ R192), E254 (= E267), C288 (= C301), E385 (= E398), E462 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P167), W155 (= W168), K179 (≠ R192), A181 (= A194), S182 (≠ D195), A212 (≠ S225), G216 (= G229), G232 (= G245), S233 (= S246), I236 (≠ V249), C288 (= C301), K338 (≠ H351), E385 (= E398), F387 (= F400)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
60% identity, 96% coverage: 15:490/494 of query aligns to 2:477/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I165), T153 (= T166), P154 (= P167), K179 (≠ R192), A212 (≠ S225), K213 (≠ R226), F230 (= F243), T231 (= T244), G232 (= G245), S233 (= S246), V236 (= V249), W239 (≠ V252), G256 (= G269)
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)
55% identity, 96% coverage: 19:491/494 of query aligns to 57:531/535 of P51649
- C93 (≠ L57) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G140) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P144) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P146) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R177) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C187) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ RPAD 192:195) binding
- T233 (= T197) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A201) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ Q219) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G229) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 245:250) binding
- R334 (= R295) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N296) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C301) modified: Disulfide link with 342, In inhibited form
- C342 (= C303) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N332) natural variant: N -> S
- P382 (= P342) to L: in SSADHD; 2% of activity
- V406 (= V366) to I: in dbSNP:rs143741652
- G409 (= G369) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S458) 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)
55% identity, 96% coverage: 19:491/494 of query aligns to 7:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 96% coverage: 19:491/494 of query aligns to 7:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 19:491/494 of query aligns to 1:473/476 of 5x5uA
- active site: N151 (= N169), K174 (≠ R192), E249 (= E267), C283 (= C301), E380 (= E398), E457 (= E475)
- binding glycerol: D15 (≠ E33), A16 (= A34), A17 (≠ S35), G19 (= G37)
- binding nicotinamide-adenine-dinucleotide: P149 (= P167), P207 (≠ S225), A208 (≠ R226), S211 (≠ G229), G227 (= G245), S228 (= S246), V231 (= V249), R329 (≠ S347), R330 (≠ A348), E380 (= E398), F382 (= F400)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 19:491/494 of query aligns to 1:473/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 95% coverage: 22:488/494 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N169), E246 (= E267), C280 (= C301), E458 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I165), T145 (= T166), A146 (≠ P167), W147 (= W168), N148 (= N169), K171 (≠ R192), T173 (≠ A194), S174 (≠ D195), G204 (≠ S225), G208 (= G229), T223 (= T244), G224 (= G245), S225 (= S246), A228 (≠ V249), S231 (≠ V252), I232 (≠ L253), E246 (= E267), L247 (= L268), C280 (= C301), E381 (= E398), F383 (= F400), H447 (≠ F464)
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)
37% identity, 96% coverage: 23:494/494 of query aligns to 38:513/518 of Q63639
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 95% coverage: 18:488/494 of query aligns to 4:485/505 of O24174
- N164 (= N169) 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 (≠ R177) 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.
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)
37% identity, 96% coverage: 23:494/494 of query aligns to 38:513/518 of O94788
- E50 (≠ S35) to G: in dbSNP:rs34266719
- A110 (≠ F92) to V: in dbSNP:rs35365164
- Q182 (≠ A164) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 166:168) binding
- KPAE 210:213 (≠ RPAD 192:195) binding
- STE 264:266 (= STE 246:248) binding
- C320 (= C301) active site, Nucleophile
- R347 (≠ L328) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K329) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ SACEH 347:351) binding
- A383 (= A364) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E398) binding
- E436 (≠ A417) to K: in dbSNP:rs34744827
- S461 (≠ G442) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
37% identity, 96% coverage: 23:494/494 of query aligns to 12:487/492 of 6b5hA
- active site: N161 (= N169), E260 (= E267), C294 (= C301), E468 (= E475)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G119), G116 (≠ Y123), F162 (= F170), W169 (≠ R177), Q284 (≠ A291), F288 (≠ R295), T295 (≠ V302), N449 (≠ L456), L451 (≠ S458), N452 (= N459), F457 (= F464)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ T166), W160 (= W168), N161 (= N169), K184 (≠ R192), G217 (≠ S225), G221 (= G229), F235 (= F243), T236 (= T244), G237 (= G245), S238 (= S246), V241 (= V249), E260 (= E267), L261 (= L268), C294 (= C301), F393 (= F400)
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)
37% identity, 96% coverage: 23:494/494 of query aligns to 12:487/492 of 6b5gA
- active site: N161 (= N169), E260 (= E267), C294 (= C301), E468 (= E475)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F170), L165 (≠ A173), W169 (≠ R177), F288 (≠ R295), C293 (≠ T300), C294 (= C301), T295 (≠ V302), N449 (≠ L456), L451 (≠ S458)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ T166), P159 (= P167), W160 (= W168), N161 (= N169), M166 (= M174), K184 (≠ R192), E187 (≠ D195), G217 (≠ S225), G221 (= G229), F235 (= F243), T236 (= T244), G237 (= G245), S238 (= S246), V241 (= V249), E260 (= E267), L261 (= L268), C294 (= C301), E391 (= E398), F393 (= F400)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
37% identity, 96% coverage: 23:494/494 of query aligns to 12:487/492 of 6aljA
- active site: N161 (= N169), E260 (= E267), C294 (= C301), E468 (= E475)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ Y123), F162 (= F170), L165 (≠ A173), M166 (= M174), W169 (≠ R177), E260 (= E267), C293 (≠ T300), C294 (= C301), L451 (≠ S458), N452 (= N459), A453 (≠ E460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ T166), P159 (= P167), W160 (= W168), N161 (= N169), K184 (≠ R192), E187 (≠ D195), G217 (≠ S225), G221 (= G229), F235 (= F243), G237 (= G245), S238 (= S246), V241 (= V249), Q341 (≠ A348), K344 (≠ H351), E391 (= E398), F393 (= F400)
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)
35% identity, 96% coverage: 21:494/494 of query aligns to 16:495/505 of 4neaA
- active site: N166 (= N169), K189 (≠ R192), E264 (= E267), C298 (= C301), E399 (= E398), E476 (= E475)
- binding nicotinamide-adenine-dinucleotide: P164 (= P167), K189 (≠ R192), E192 (≠ D195), G222 (≠ S225), G226 (= G229), G242 (= G245), G243 (≠ S246), T246 (≠ V249), H249 (≠ V252), I250 (≠ L253), C298 (= C301), E399 (= E398), F401 (= F400)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 95% coverage: 18:488/494 of query aligns to 6:482/494 of 4pz2B
- active site: N159 (= N169), K182 (≠ R192), E258 (= E267), C292 (= C301), E392 (= E398), D469 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I155 (= I165), I156 (≠ T166), P157 (= P167), W158 (= W168), N159 (= N169), M164 (= M174), K182 (≠ R192), A184 (= A194), E185 (≠ D195), G215 (≠ S225), G219 (= G229), F233 (= F243), T234 (= T244), G235 (= G245), S236 (= S246), V239 (= V249), E258 (= E267), L259 (= L268), C292 (= C301), E392 (= E398), F394 (= F400)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 94% coverage: 23:488/494 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N169), K177 (≠ R192), E253 (= E267), C287 (= C301), E384 (= E398), D461 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I150 (= I165), V151 (≠ T166), P152 (= P167), W153 (= W168), K177 (≠ R192), E180 (≠ D195), G210 (≠ S225), G214 (= G229), A215 (= A230), F228 (= F243), G230 (= G245), S231 (= S246), V234 (= V249), E253 (= E267), G255 (= G269), C287 (= C301), Q334 (≠ A348), K337 (≠ H351), E384 (= E398), F386 (= F400)
7radA Crystal structure analysis of aldh1b1
37% identity, 98% coverage: 11:494/494 of query aligns to 1:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ T166), P160 (= P167), W161 (= W168), N162 (= N169), M167 (= M174), K185 (≠ R192), E188 (≠ D195), G218 (≠ S225), G222 (= G229), A223 (= A230), T237 (= T244), G238 (= G245), S239 (= S246), V242 (= V249), E261 (= E267), L262 (= L268), C295 (= C301), E392 (= E398), F394 (= F400)
- 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 (≠ Y123), F163 (= F170), E285 (≠ A291), F289 (≠ R295), N450 (≠ L456), V452 (≠ S458)
7mjdA Crystal structure analysis of aldh1b1
37% identity, 98% coverage: 11:494/494 of query aligns to 1:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ T166), P160 (= P167), W161 (= W168), N162 (= N169), M167 (= M174), K185 (≠ R192), E188 (≠ D195), G218 (≠ S225), G222 (= G229), F236 (= F243), T237 (= T244), G238 (= G245), S239 (= S246), V242 (= V249), E261 (= E267), L262 (= L268), C295 (= C301), E392 (= E398), F394 (= F400)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ Y123), E285 (≠ A291), F289 (≠ R295), N450 (≠ L456), V452 (≠ S458)
Query Sequence
>RR42_RS24555 FitnessBrowser__Cup4G11:RR42_RS24555
MNHDTQVTTALQARLRDPSLLETRAWLASGWQEASGGRSFAVTNPATGEILARVASLSGA
EVESAITASAQAQAVWQRRSSHERAKLLRAWFDLMIANADDLALIMTSEQGKPLAEARGE
ILYAASFVEWFAEEAKRIYGDVAPHPQTDKRILVIRQPVGVCAAITPWNFPAAMITRKVA
PALAAGCSIIVRPADLTPLTALALAVLAERAGIPAGVLQMVCGPSREIGAVLTASPVVRK
LSFTGSTEVGRVLMSQSSPTIKRLSLELGGNAPFIVFDDADLDAAIEGAMASKYRNSGQT
CVCANRFLVQDGIYDRFVEALVRRVAELKVGNGVEPGVQQGPLIQKSACEHLQAMIDDAV
GKGAKVVVGGKGHALGGTFFEPTVIAGATPDMRVAREELFGPVAPVFRFRDEAEAIALAN
DTEYGLAAYLYTRDNARIWRVGEALEYGMVGLNTGLISNEVAPFGGVKQSGLGREGSRYG
IDEYLEIKYLCAQV
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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