SitesBLAST
Comparing 8501044 FitnessBrowser__Miya:8501044 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)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
31% identity, 79% coverage: 85:525/560 of query aligns to 32:466/480 of 3rhhD
- active site: N155 (= N208), K178 (= K231), E251 (≠ G305), C285 (= C339), E378 (= E435), Q456 (≠ L515)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ M204), P153 (= P206), F154 (≠ Y207), K178 (= K231), P179 (≠ T232), A180 (≠ P233), T181 (≠ R234), G211 (≠ R263), G215 (vs. gap), D216 (≠ K267), F229 (= F280), G231 (= G282), G232 (≠ S283), T235 (≠ A286)
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
31% identity, 80% coverage: 85:530/560 of query aligns to 30:470/474 of 2esdA
- active site: N153 (= N208), K176 (= K231), A249 (≠ G305), C283 (= C339), E376 (= E435), Q454 (≠ L515)
- binding glyceraldehyde-3-phosphate: R102 (= R161), Y154 (= Y209), R282 (= R338), C283 (= C339), T284 (= T340), Q435 (= Q496), R436 (= R497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ Y207), K176 (= K231), P178 (= P233), T179 (≠ R234), G209 (≠ D262), G213 (≠ V266), D214 (≠ K267), F227 (= F280), S230 (= S283), I233 (≠ A286), K328 (≠ G385), S329 (≠ K386), Y332 (= Y389)
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
30% identity, 80% coverage: 85:530/560 of query aligns to 31:471/475 of Q59931
- R103 (= R161) binding
- S151 (≠ G205) binding
- K177 (= K231) binding
- T180 (≠ R234) binding
- D215 (≠ K267) binding
- 230:251 (vs. 282:306, 23% identical) binding
- E377 (= E435) binding
- R437 (= R497) binding
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
31% identity, 80% coverage: 85:530/560 of query aligns to 30:470/474 of 1qi1B
- active site: N153 (= N208), K176 (= K231), E249 (≠ G305), S283 (≠ C339), E376 (= E435), Q454 (≠ L515)
- binding sn-glycerol-3-phosphate: Y154 (= Y209), R282 (= R338), S283 (≠ C339), T284 (= T340), R436 (= R497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (= P206), F152 (≠ Y207), N153 (= N208), L158 (≠ E213), K176 (= K231), P178 (= P233), T179 (≠ R234), G209 (≠ D262), G213 (≠ V266), G229 (= G282), S230 (= S283), I233 (≠ A286), E249 (≠ G305), L250 (= L306), S283 (≠ C339)
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
25% identity, 81% coverage: 80:533/560 of query aligns to 12:456/456 of 3rhdA
- active site: N133 (= N208), H156 (≠ K231), E233 (≠ G305), C267 (= C339), E360 (= E435), E437 (≠ L515)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (≠ M204), T130 (≠ G205), F132 (≠ Y207), H156 (≠ K231), S158 (≠ P233), S159 (≠ R234), K160 (≠ L235), G193 (≠ R263), E194 (≠ R264), G197 (vs. gap), D198 (≠ K267), F211 (= F280), S214 (= S283), V217 (≠ A286)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
24% identity, 81% coverage: 81:533/560 of query aligns to 29:478/484 of 1t90A
- active site: N151 (= N208), K174 (= K231), L248 (≠ V303), C282 (= C339), E380 (= E435), A460 (≠ V517)
- binding nicotinamide-adenine-dinucleotide: I147 (≠ M204), A148 (≠ G205), P149 (= P206), F150 (≠ Y207), N151 (= N208), W159 (≠ T217), K174 (= K231), E177 (≠ R234), R178 (≠ L235), H207 (≠ R263), V225 (≠ I281), G226 (= G282), S227 (= S283), V230 (≠ A286), L248 (≠ V303), T249 (≠ L304), C282 (= C339), E380 (= E435), F382 (= F437)
P42412 Malonate-semialdehyde dehydrogenase; MSA dehydrogenase; Methylmalonate-semialdehyde dehydrogenase; MMSA dehydrogenase; MMSDH; MSDH; EC 1.2.1.27 from Bacillus subtilis (strain 168) (see 3 papers)
24% identity, 81% coverage: 81:533/560 of query aligns to 31:480/487 of P42412
- C36 (≠ G86) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413.
- R107 (= R161) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ G205) binding
- F152 (≠ Y207) binding
- C160 (= C216) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-287; A-351 and A-413.
- K176 (= K231) binding
- E179 (≠ R234) binding
- R180 (≠ L235) binding
- S229 (= S283) binding
- T251 (≠ L304) binding
- R283 (= R338) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L342) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413.
- C351 (≠ N406) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413.
- E382 (= E435) binding
- C413 (≠ S466) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
5n5sB Crystal structure of aldehyde dehydrogenase 21 (aldh21) from physcomitrella patens in complex with NADP+ (see paper)
27% identity, 70% coverage: 121:511/560 of query aligns to 65:454/481 of 5n5sB
- active site: N155 (= N208), K178 (= K231), E251 (≠ G305), C286 (= C339), E380 (= E435)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V151 (≠ M204), S152 (≠ G205), P153 (= P206), W154 (≠ Y207), N155 (= N208), L160 (≠ E213), K178 (= K231), A180 (vs. gap), S181 (vs. gap), R212 (= R263), A215 (≠ V266), T230 (≠ I281), G231 (= G282), S232 (= S283), I235 (≠ A286), E251 (≠ G305), L252 (= L306), C286 (= C339), E380 (= E435), F382 (= F437), Y447 (≠ F504)
Sites not aligning to the query:
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
26% identity, 68% coverage: 114:495/560 of query aligns to 66:453/503 of Q84LK3
- N162 (= N208) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ C216) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
31% identity, 62% coverage: 194:538/560 of query aligns to 167:511/512 of P47895
- K204 (= K231) binding
- E207 (vs. gap) binding
- GSTEVG 257:262 (≠ GSSTAA 282:287) binding
- Q361 (≠ K386) binding
- E411 (= E435) binding
- A493 (= A520) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 89 R → C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
26% identity, 68% coverage: 114:495/560 of query aligns to 68:455/505 of C0P9J6
Sites not aligning to the query:
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
26% identity, 68% coverage: 114:495/560 of query aligns to 63:450/500 of 4i8pA
- active site: N159 (= N208), K182 (= K231), E257 (≠ G305), C291 (= C339), E390 (= E435)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ M204), T156 (≠ G205), P157 (= P206), W158 (≠ Y207), N159 (= N208), M164 (≠ E213), K182 (= K231), S184 (≠ P233), E185 (≠ R234), G215 (≠ D262), G219 (≠ V266), A220 (≠ K267), T234 (≠ I281), G235 (= G282), S236 (= S283), T239 (≠ A286), E257 (≠ G305), L258 (= L306), C291 (= C339), E390 (= E435), F392 (= F437)
Sites not aligning to the query:
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
31% identity, 57% coverage: 194:513/560 of query aligns to 149:468/489 of 7a6qB
- active site: N163 (= N208), E262 (≠ G305), C296 (= C339)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ M204), W162 (≠ Y207), K186 (= K231), E189 (vs. gap), G219 (≠ R263), G223 (≠ K267), S240 (= S283), V243 (≠ A286), K342 (≠ G385)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: E189 (vs. gap), Q190 (vs. gap), F218 (≠ D262), I339 (≠ P382), D340 (≠ V383)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: N451 (≠ S493), L453 (≠ C495), A455 (≠ R497)
Sites not aligning to the query:
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
31% identity, 57% coverage: 194:513/560 of query aligns to 149:468/489 of 7a6qA
- active site: N163 (= N208), E262 (≠ G305), C296 (= C339)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ M204), T160 (≠ G205), W162 (≠ Y207), K186 (= K231), A188 (vs. gap), E189 (vs. gap), G219 (≠ R263), G223 (≠ K267), S240 (= S283), V243 (≠ A286), K342 (≠ G385), K346 (≠ Y389)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: N451 (≠ S493), L453 (≠ C495), Y454 (≠ Q496)
Sites not aligning to the query:
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
31% identity, 57% coverage: 194:513/560 of query aligns to 149:468/489 of 5fhzA
- active site: N163 (= N208), K186 (= K231), E262 (≠ G305), C296 (= C339), E393 (= E435)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ M204), T160 (≠ G205), W162 (≠ Y207), K186 (= K231), E189 (vs. gap), G219 (≠ R263), G223 (≠ K267), F237 (= F280), G239 (= G282), S240 (= S283), T241 (≠ S284), V243 (≠ A286), G264 (≠ D307), Q343 (≠ K386), E393 (= E435)
- binding retinoic acid: F164 (≠ Y209), M168 (≠ E213), W171 (≠ C216), C295 (≠ R338), C296 (= C339), L453 (≠ C495)
Sites not aligning to the query:
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
31% identity, 57% coverage: 194:513/560 of query aligns to 148:467/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (≠ M204), T159 (≠ G205), P160 (= P206), W161 (≠ Y207), K185 (= K231), E188 (vs. gap), G218 (≠ R263), G222 (≠ K267), F236 (= F280), S239 (= S283), V242 (≠ A286)
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
27% identity, 75% coverage: 96:513/560 of query aligns to 43:456/484 of 4jz6A
- active site: N150 (= N208), K173 (= K231), E251 (≠ G305), C285 (= C339), E380 (= E435)
- binding salicylaldehyde: W97 (≠ D154), G151 (≠ Y209), V154 (≠ N212), R247 (= R301), C248 (= C302), I284 (≠ R338), C285 (= C339), M286 (≠ T340), Y447 (≠ F504), Y455 (≠ E512)
Sites not aligning to the query:
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)
25% identity, 81% coverage: 45:495/560 of query aligns to 4:450/497 of P17202
- I28 (≠ G72) binding
- D96 (≠ E147) binding
- SPW 156:158 (≠ GPY 205:207) binding
- Y160 (= Y209) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ C216) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KTPR 231:234) binding
- L186 (= L235) binding
- SSAT 236:239 (≠ SSTA 283:286) binding
- V251 (≠ A293) binding in other chain
- L258 (= L306) binding
- W285 (≠ S333) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E435) binding
- A441 (≠ V486) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (= C495) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
Sites not aligning to the query:
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
31% identity, 57% coverage: 194:513/560 of query aligns to 141:457/478 of 6tgwA
- active site: N155 (= N208), E254 (≠ G305), C288 (= C339)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: F156 (≠ Y209), Q278 (= Q329), F282 (≠ S333), L442 (≠ C495), A444 (≠ R497)
- binding nicotinamide-adenine-dinucleotide: I151 (≠ M204), T152 (≠ G205), P153 (= P206), W154 (≠ Y207), K178 (= K231), G211 (≠ R263), G215 (≠ K267), F229 (= F280), G231 (= G282), S232 (= S283), V235 (≠ A286)
Sites not aligning to the query:
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
29% identity, 75% coverage: 92:513/560 of query aligns to 56:475/501 of P00352
- N121 (≠ R167) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ GPYN 205:208) binding
- I177 (≠ F215) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ K--- 231) binding
- GP 226:227 (≠ RR 263:264) binding
- GS 246:247 (= GS 282:283) binding
- E269 (≠ G305) active site, Proton acceptor
- ELG 269:271 (≠ GLD 305:307) binding
- C302 (≠ R338) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C339) active site, Nucleophile
- EQYDK 349:353 (≠ GKSAY 385:389) binding
- EIF 400:402 (≠ EQF 435:437) binding
- G458 (vs. gap) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
Query Sequence
>8501044 FitnessBrowser__Miya:8501044
MSSQPTATATGPAASPAAAHTPESLRALFPVAGQPLPEAAHAFAPIEQRTCLIDGKLEEW
PGEMQQVFSPIGETDGAGGFTPRLLGRCPILDEAAALRAVDAADHAWADGMGAWPTMGVA
ERIRHVEDFARRMAARRTEVVRIMMWEICKSWQDASGEFDRTMEYLRDTIDALKDLDRAS
SRFVIEKGIYAQIRRAPLGPVLCMGPYNYPLNETFCTLMPALIMGNPVIVKTPRLGRLLY
SPLMEAFRDAFPAGVVNILHGDRRIVKPIMASGRINVLAFIGSSTAADALRLAHPYPHRL
RCVLGLDAKNAGIVLDCADMDLTVAEALQGSFSFNGQRCTALKMLFVHQKRLDEFLARMD
EGIRKLRIGMPWDEGVRITPLPVPGKSAYLDDLVQDAAAQGGKVANSGGGTHAETLYHPT
VVCPATPQMRVYHEEQFGPVIPVIPFTDIETPVRYVVGSQYGQQLSIFGNDPDDVARLID
PMVNQVCRVNINSQCQRGPDTFPFTGRKDSAEGTLSVSDALRCFSIRTLVAAKGSDANKT
LLTSIIRDRRSNFLSNDFIL
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