SitesBLAST
Comparing H281DRAFT_03360 FitnessBrowser__Burk376:H281DRAFT_03360 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 96% coverage: 7:481/493 of query aligns to 2:474/476 of 5x5uA
- active site: N151 (= N156), K174 (≠ R179), E249 (= E254), C283 (= C288), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (≠ S20), A16 (= A21), A17 (≠ T22), G19 (≠ D24)
- binding nicotinamide-adenine-dinucleotide: P149 (= P154), P207 (≠ A212), A208 (≠ D213), S211 (≠ T216), G227 (= G232), S228 (= S233), V231 (≠ I236), R329 (≠ K334), R330 (= R335), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 96% coverage: 7:481/493 of query aligns to 2:474/476 of 5x5tA
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 97% coverage: 7:483/493 of query aligns to 8:481/481 of 3jz4A
- active site: N156 (= N156), K179 (≠ R179), E254 (= E254), C288 (= C288), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (≠ R179), A181 (≠ S181), S182 (≠ N182), A212 (= A212), G216 (≠ T216), G232 (= G232), S233 (= S233), I236 (= I236), C288 (= C288), K338 (≠ A338), E385 (= E387), F387 (= F389)
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, 97% coverage: 7:483/493 of query aligns to 9:482/482 of P25526
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)
38% identity, 95% coverage: 13:479/493 of query aligns to 64:530/535 of P51649
- C93 (≠ A44) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G127) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ E131) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ R133) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R164) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (≠ N174) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ RPSN 179:182) binding
- T233 (≠ A184) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ T188) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N206) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ T216) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVPIG 232:237) binding
- R334 (= R282) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N283) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C288) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S290) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D319) natural variant: N -> S
- P382 (= P329) to L: in SSADHD; 2% of activity
- V406 (= V353) to I: in dbSNP:rs143741652
- G409 (= G356) 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.
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)
38% identity, 95% coverage: 13:479/493 of query aligns to 14:480/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
38% identity, 95% coverage: 13:479/493 of query aligns to 14:480/485 of 2w8qA
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 94% coverage: 26:489/493 of query aligns to 38:503/503 of O14293
- S248 (= S233) modified: Phosphoserine
- S501 (≠ E487) modified: Phosphoserine
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
37% identity, 95% coverage: 13:481/493 of query aligns to 13:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F152), T153 (= T153), P154 (= P154), K179 (≠ R179), A212 (= A212), K213 (≠ D213), F230 (= F230), T231 (= T231), G232 (= G232), S233 (= S233), V236 (≠ I236), W239 (≠ Q239), G256 (= G256)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
34% identity, 96% coverage: 9:480/493 of query aligns to 1:476/477 of 6j76A
- active site: N148 (= N156), E246 (= E254), C280 (= C288), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ F152), T145 (= T153), A146 (≠ P154), W147 (= W155), N148 (= N156), K171 (≠ R179), T173 (≠ S181), S174 (≠ N182), G204 (≠ A212), G208 (≠ T216), T223 (= T231), G224 (= G232), S225 (= S233), A228 (≠ I236), S231 (≠ Q239), I232 (= I240), E246 (= E254), L247 (= L255), C280 (= C288), E381 (= E387), F383 (= F389), H447 (≠ F453)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
33% identity, 96% coverage: 12:484/493 of query aligns to 5:478/494 of 5izdA
- active site: N149 (= N156), K172 (≠ R179), E247 (= E254), C281 (= C288), E381 (= E387), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ F152), T146 (= T153), W148 (= W155), K172 (≠ R179), P173 (= P180), S174 (= S181), S175 (≠ N182), R204 (≠ K211), G205 (≠ A212), G209 (≠ T216), D210 (≠ P217), G225 (= G232), S226 (= S233), T229 (≠ I236)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 97% coverage: 6:485/493 of query aligns to 2:484/489 of 4cazA
- active site: N152 (= N156), K175 (≠ R179), E251 (= E254), C285 (= C288), 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 (≠ F152), G149 (≠ T153), W151 (= W155), N152 (= N156), K175 (≠ R179), E178 (≠ N182), G208 (≠ A212), G212 (≠ T216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (≠ I236), V236 (≠ I240), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E387), F388 (= F389)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 97% coverage: 6:485/493 of query aligns to 2:484/489 of 2woxA
- active site: N152 (= N156), K175 (≠ R179), E251 (= E254), C285 (= C288), E386 (= E387), E463 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F152), G149 (≠ T153), W151 (= W155), N152 (= N156), K175 (≠ R179), S177 (= S181), E178 (≠ N182), G208 (≠ A212), G212 (≠ T216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (≠ I236), V236 (≠ I240), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E387), F388 (= F389)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 97% coverage: 6:485/493 of query aligns to 2:484/489 of 2wmeA
- active site: N152 (= N156), K175 (≠ R179), E251 (= E254), C285 (= C288), E386 (= E387), E463 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T153), W151 (= W155), K175 (≠ R179), S177 (= S181), E178 (≠ N182), G208 (≠ A212), G212 (≠ T216), F226 (= F230), G228 (= G232), G229 (≠ S233), T232 (≠ I236), V236 (≠ I240)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
34% identity, 97% coverage: 6:485/493 of query aligns to 3:485/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 153:156) binding
- K162 (= K165) active site, Charge relay system
- KPSE 176:179 (≠ RPSN 179:182) binding
- G209 (≠ A212) binding
- GTST 230:233 (≠ SVPI 233:236) binding
- E252 (= E254) active site, Proton acceptor
- C286 (= C288) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E387) binding
- E464 (= E464) active site, Charge relay system
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
35% identity, 96% coverage: 12:483/493 of query aligns to 14:487/492 of 6b5hA
- active site: N161 (= N156), E260 (= E254), C294 (= C288), E468 (= E464)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G106), G116 (≠ A110), F162 (= F157), W169 (≠ R164), Q284 (≠ L278), F288 (≠ R282), T295 (≠ A289), N449 (≠ V445), L451 (≠ S447), N452 (≠ T448), F457 (= F453)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ F152), I158 (≠ T153), W160 (= W155), N161 (= N156), K184 (≠ R179), G217 (≠ A212), G221 (≠ T216), F235 (= F230), T236 (= T231), G237 (= G232), S238 (= S233), V241 (≠ I236), E260 (= E254), L261 (= L255), C294 (= C288), F393 (= F389)
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)
35% identity, 96% coverage: 12:483/493 of query aligns to 14:487/492 of 6b5gA
- active site: N161 (= N156), E260 (= E254), C294 (= C288), E468 (= E464)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F157), L165 (= L160), W169 (≠ R164), F288 (≠ R282), C293 (≠ V287), C294 (= C288), T295 (≠ A289), N449 (≠ V445), L451 (≠ S447)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ F152), I158 (≠ T153), P159 (= P154), W160 (= W155), N161 (= N156), M166 (≠ L161), K184 (≠ R179), E187 (≠ N182), G217 (≠ A212), G221 (≠ T216), F235 (= F230), T236 (= T231), G237 (= G232), S238 (= S233), V241 (≠ I236), E260 (= E254), L261 (= L255), C294 (= C288), E391 (= E387), F393 (= F389)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
35% identity, 96% coverage: 12:483/493 of query aligns to 14:487/492 of 6aljA
- active site: N161 (= N156), E260 (= E254), C294 (= C288), E468 (= E464)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A110), F162 (= F157), L165 (= L160), M166 (≠ L161), W169 (≠ R164), E260 (= E254), C293 (≠ V287), C294 (= C288), L451 (≠ S447), N452 (≠ T448), A453 (= A449)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ F152), I158 (≠ T153), P159 (= P154), W160 (= W155), N161 (= N156), K184 (≠ R179), E187 (≠ N182), G217 (≠ A212), G221 (≠ T216), F235 (= F230), G237 (= G232), S238 (= S233), V241 (≠ I236), Q341 (≠ R335), K344 (≠ A338), E391 (= E387), F393 (= F389)
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)
35% identity, 96% coverage: 12:483/493 of query aligns to 40:513/518 of O94788
- E50 (≠ T22) to G: in dbSNP:rs34266719
- A110 (= A79) to V: in dbSNP:rs35365164
- Q182 (≠ A151) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 153:155) binding
- KPAE 210:213 (≠ RPSN 179:182) binding
- STE 264:266 (≠ SVP 233:235) binding
- C320 (= C288) active site, Nucleophile
- R347 (≠ L315) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R316) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ KRREA 334:338) binding
- A383 (= A351) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E387) binding
- E436 (≠ T406) to K: in dbSNP:rs34744827
- S461 (≠ T431) to Y: in DIH4; decreased retinoic acid biosynthetic process
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)
35% identity, 96% coverage: 12:483/493 of query aligns to 40:513/518 of Q63639
Query Sequence
>H281DRAFT_03360 FitnessBrowser__Burk376:H281DRAFT_03360
MELEGHYREHGMLIAGRWQSATADNGQVSINPATEERLGYMPLATPAQVTEAIDAATEAS
AAMRKLTPWERTALLRRAATLIRERAPQLARIVALETGKPIAQATGEANASAESIDWFAD
EARRVFGMSYESRVKGGRYLVHYEPLGVVAAFTPWNFPLLLLARKMGPALAAGNAIVIRP
SNEAAGATMGLVRCFVDAGFPEGAVNLVIGKADAITPTVMADPRVAKISFTGSVPIGRQI
VEMSAKTLKKVTMELGGHAPVIVHRDADIDAFAHLASLGKFRNAGQVCASPTRFYIHESI
FDKTVKALVERSTALRVGDPLQQNTDLGPLTTSKRREAIERLVDEAVSEGASVLCGGRRP
SQFGRGWFYEPTLISNPAPHIGLMNDEPFGPVGTLNRFTTMDEVITEANRLPFALAAYVF
TRSMRNTLETTERLQAGVVGVNTFVASTAETPFGGSKDSGFGREGGPNAIRDYLDTKFIN
LELANDEPLDATA
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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