SitesBLAST
Comparing RR42_RS21760 FitnessBrowser__Cup4G11:RR42_RS21760 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)
71% identity, 99% coverage: 2:479/482 of query aligns to 1:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
71% identity, 99% coverage: 3:479/482 of query aligns to 1:479/481 of 3jz4A
- active site: N156 (= N156), K179 (= K179), E254 (= E254), C288 (= C288), E385 (= E385), E462 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (= K179), A181 (= A181), S182 (= S182), A212 (= A212), G216 (= G216), G232 (= G232), S233 (= S233), I236 (≠ V236), C288 (= C288), K338 (= K338), E385 (= E385), F387 (= F387)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
62% identity, 99% coverage: 4:482/482 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I152), T153 (= T153), P154 (= P154), K179 (= K179), A212 (= A212), K213 (≠ A213), F230 (= F230), T231 (= T231), G232 (= G232), S233 (= S233), V236 (= V236), W239 (≠ T239), G256 (= G256)
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)
56% identity, 99% coverage: 8:482/482 of query aligns to 57:535/535 of P51649
- C93 (≠ L44) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G127) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P131) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P133) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R164) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C174) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 179:182) binding
- T233 (= T184) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A188) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S206) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G216) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 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 (= C290) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N319) 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 (= S445) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (≠ A480) 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)
55% identity, 99% coverage: 8:482/482 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 99% coverage: 8:482/482 of query aligns to 7:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
44% identity, 97% coverage: 13:480/482 of query aligns to 6:476/476 of 5x5uA
- active site: N151 (= N156), K174 (= K179), E249 (= E254), C283 (= C288), E380 (= E385), E457 (= E462)
- binding glycerol: D15 (= D22), A16 (= A23), A17 (≠ Q24), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P154), P207 (≠ A212), A208 (= A213), S211 (≠ G216), G227 (= G232), S228 (= S233), V231 (= V236), R329 (≠ K334), R330 (≠ A335), E380 (= E385), F382 (= F387)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
44% identity, 97% coverage: 13:480/482 of query aligns to 6:476/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 96% coverage: 11:472/482 of query aligns to 1:468/477 of 6j76A
- active site: N148 (= N156), E246 (= E254), C280 (= C288), E458 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I152), T145 (= T153), A146 (≠ P154), W147 (= W155), N148 (= N156), K171 (= K179), T173 (≠ A181), S174 (= S182), G204 (≠ A212), G208 (= G216), T223 (= T231), G224 (= G232), S225 (= S233), A228 (≠ V236), S231 (≠ T239), I232 (≠ L240), E246 (= E254), L247 (= L255), C280 (= C288), E381 (= E385), F383 (= F387), H447 (≠ F451)
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
38% identity, 96% coverage: 12:475/482 of query aligns to 8:480/497 of P17202
- I28 (≠ T30) binding
- D96 (≠ E96) binding
- SPW 156:158 (≠ TPW 153:155) binding
- Y160 (≠ F157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAS 179:182) binding
- L186 (≠ Q183) binding
- SSAT 236:239 (≠ STEV 233:236) binding
- V251 (≠ I248) binding in other chain
- L258 (= L255) binding
- W285 (≠ R282) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding
- A441 (≠ M436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S445) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F451) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K455) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 96% coverage: 12:475/482 of query aligns to 6:478/495 of 4v37A
- active site: N157 (= N156), K180 (= K179), E255 (= E254), A289 (≠ C288), E388 (= E385), E465 (= E462)
- binding 3-aminopropan-1-ol: C448 (≠ S445), W454 (≠ F451)
- binding nicotinamide-adenine-dinucleotide: I153 (= I152), S154 (≠ T153), P155 (= P154), W156 (= W155), N157 (= N156), M162 (= M161), K180 (= K179), S182 (≠ A181), E183 (≠ S182), G213 (≠ A212), G217 (= G216), A218 (≠ G217), T232 (= T231), G233 (= G232), S234 (= S233), T237 (≠ V236), E255 (= E254), L256 (= L255), A289 (≠ C288), E388 (= E385), F390 (= F387)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 98% coverage: 2:475/482 of query aligns to 12:492/498 of 4go2A
- active site: N170 (= N156), K193 (= K179), E269 (= E254), C303 (= C288), E400 (= E385), D479 (≠ E462)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I152), I167 (≠ T153), P168 (= P154), W169 (= W155), K193 (= K179), A195 (= A181), Q196 (≠ S182), S225 (= S211), G226 (≠ A212), G230 (= G216), Q231 (≠ G217), F244 (= F230), G246 (= G232), S247 (= S233), V250 (= V236), I254 (≠ L240), E269 (= E254), G271 (= G256), C303 (= C288), E400 (= E385), F402 (= F387)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 98% coverage: 2:475/482 of query aligns to 12:492/498 of 2o2rA
- active site: N170 (= N156), K193 (= K179), E269 (= E254), C303 (= C288), E400 (= E385), D479 (≠ E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I152), I167 (≠ T153), W169 (= W155), K193 (= K179), A195 (= A181), Q196 (≠ S182), S225 (= S211), G226 (≠ A212), G230 (= G216), Q231 (≠ G217), F244 (= F230), S247 (= S233), V250 (= V236), I254 (≠ L240)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 98% coverage: 2:475/482 of query aligns to 97:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K179), S310 (= S211), G311 (≠ A212), G315 (= G216), G331 (= G232), S332 (= S233), V335 (= V236)
- binding 4'-phosphopantetheine: K201 (≠ R105), F382 (≠ R282), N387 (≠ T287), C388 (= C288), N545 (≠ L443)
6popA Crystal structure of daua in complex with NADP+ (see paper)
36% identity, 97% coverage: 10:475/482 of query aligns to 2:467/475 of 6popA
- active site: N148 (= N156), E246 (= E254), C280 (= C288), D454 (≠ E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F144 (≠ I152), L145 (≠ T153), W147 (= W155), N148 (= N156), K171 (= K179), S173 (≠ A181), S174 (= S182), D204 (≠ A212), G208 (= G216), I223 (≠ T231), G224 (= G232), S225 (= S233), V228 (= V236), H231 (≠ T239), E246 (= E254), L247 (= L255), G248 (= G256), C280 (= C288), E378 (= E385), F380 (= F387), H443 (≠ F451)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 96% coverage: 11:475/482 of query aligns to 9:485/505 of O24174
- N164 (= N156) 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 (≠ R164) 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.
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)
38% identity, 98% coverage: 2:475/482 of query aligns to 416:896/902 of P28037
- IPW 571:573 (≠ TPW 153:155) binding
- KPAQ 597:600 (≠ KPAS 179:182) binding
- GSLVGQ 630:635 (≠ AAAIGG 212:217) binding
- GS 650:651 (= GS 232:233) binding
- E673 (= E254) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 254:255) binding
- C707 (= C288) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K338) binding
- ESF 804:806 (≠ ETF 385:387) 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.
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 96% coverage: 10:472/482 of query aligns to 3:468/477 of 2opxA
- active site: N151 (= N156), K174 (= K179), E249 (= E254), C283 (= C288), E381 (= E385), A458 (≠ E462)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y110), F152 (= F157), N284 (≠ V289), F312 (≠ V317), G313 (= G318), R318 (vs. gap), D320 (≠ G324), I321 (≠ V325), A322 (≠ R326), Y362 (≠ F366), F440 (≠ I444), F440 (≠ I444), E441 (≠ S445)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
39% identity, 96% coverage: 12:475/482 of query aligns to 18:492/498 of 7yjjC
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 96% coverage: 10:472/482 of query aligns to 5:470/479 of P25553
- L150 (≠ T153) binding
- R161 (= R164) binding
- KPSE 176:179 (≠ KPAS 179:182) binding
- F180 (≠ Q183) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G217) binding
- S230 (= S233) binding
- E251 (= E254) binding
- N286 (≠ V289) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ K338) binding
- E443 (≠ S445) binding
- H449 (≠ F451) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>RR42_RS21760 FitnessBrowser__Cup4G11:RR42_RS21760
MLQLQDPSLLRQQCYIDGRWTDAQRHIDVTNPATGERVGQVPLLGADETRQAIEAANRAL
PAWRARTAKERSALLRKWFELLLANQDDLARIMTAEQGKPFAEARGEIGYAASFIEWFAE
EGKRVYGETIPAPVSNQRIVVTKEPVGVCAAITPWNFPAAMITRKAGPALAAGCTMVVKP
ASQTPLTALAMVALAERAGIPAGVLSVVTGSAAAIGGELSSNPLVRKLTFTGSTEVGRTL
MAQTASTIKKVSMELGGNAPFIVFEDADLDAAVEGAIVSKYRNAGQTCVCANRLYVHSKV
YDAFAEKLVAAVRALKVGNGMEDGVRIGPLIDGKAVTKVEEHITDAISKGARVLQGGKRH
ALGQSFFEPTVLADVTPGMLVAREETFGPLAPLFRFETEDEVVAMANDTEFGLASYFYAR
DLGRVWRVSERLEYGMVGVNTGLISNEVAPFGGVKQSGVGREGSHYGIEDYLVIKYTCMA
GI
Or try a new SitesBLAST search
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