SitesBLAST
Comparing H281DRAFT_05316 FitnessBrowser__Burk376:H281DRAFT_05316 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
48% identity, 87% coverage: 67:531/535 of query aligns to 42:502/504 of 1eyyA
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
26% identity, 82% coverage: 27:463/535 of query aligns to 42:466/515 of 2d4eC
- active site: N173 (= N168), K196 (= K193), E271 (= E274), C305 (= C311), E409 (= E402)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F164), T170 (≠ G165), P171 (≠ A166), W172 (≠ S167), K196 (= K193), A198 (≠ H195), G229 (= G230), G233 (= G234), A234 (≠ E235), T248 (= T249), G249 (= G250), E250 (≠ S251), T253 (≠ G254), E271 (= E274), L272 (≠ M275), C305 (= C311), E409 (= E402), F411 (= F404)
Sites not aligning to the query:
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
26% identity, 77% coverage: 12:423/535 of query aligns to 6:401/454 of 3ty7B
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
26% identity, 76% coverage: 29:437/535 of query aligns to 27:431/505 of O24174
- N164 (= N168) 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 (≠ G178) 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.
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
25% identity, 82% coverage: 63:503/535 of query aligns to 521:945/959 of 5ur2B
Sites not aligning to the query:
- binding N-propargylglycine-modified flavin adenine dinucleotide: 174, 215, 216, 249, 278, 279, 280, 281, 283, 300, 301, 302, 303, 306, 329, 330, 331, 332, 356, 357, 358, 379, 398, 403, 405
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)
27% identity, 81% coverage: 33:463/535 of query aligns to 53:468/512 of P47895
- R89 (= R68) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K193) binding
- E207 (≠ R196) binding
- GSTEVG 257:262 (≠ GSRAGG 250:255) binding
- Q361 (= Q355) binding
- E411 (= E402) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 493 A → P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 34:449/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (vs. gap), T159 (vs. gap), P160 (vs. gap), W161 (≠ S167), K185 (= K193), E188 (≠ R196), G218 (= G230), G222 (= G234), F236 (= F248), S239 (= S251), V242 (≠ G254)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 35:450/489 of 7a6qB
- active site: N163 (= N168), E262 (= E274), C296 (= C311)
- binding nicotinamide-adenine-dinucleotide: I159 (vs. gap), W162 (≠ S167), K186 (= K193), E189 (≠ R196), G219 (= G230), G223 (= G234), S240 (= S251), V243 (≠ G254), K342 (≠ T354)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: P36 (= P34), D103 (≠ T115), E189 (≠ R196), Q190 (≠ A197), F218 (≠ A229), I339 (≠ S351), D340 (≠ A352)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (vs. gap), D141 (≠ S149), N143 (≠ L151)
Sites not aligning to the query:
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 35:450/489 of 7a6qA
- active site: N163 (= N168), E262 (= E274), C296 (= C311)
- binding nicotinamide-adenine-dinucleotide: I159 (vs. gap), T160 (vs. gap), W162 (≠ S167), K186 (= K193), A188 (≠ H195), E189 (≠ R196), G219 (= G230), G223 (= G234), S240 (= S251), V243 (≠ G254), K342 (≠ T354), K346 (≠ S358)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (vs. gap), D141 (≠ S149), N143 (≠ L151)
Sites not aligning to the query:
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 35:450/489 of 5fhzA
- active site: N163 (= N168), K186 (= K193), E262 (= E274), C296 (= C311), E393 (= E402)
- binding nicotinamide-adenine-dinucleotide: I159 (vs. gap), T160 (vs. gap), W162 (≠ S167), K186 (= K193), E189 (≠ R196), G219 (= G230), G223 (= G234), F237 (= F248), G239 (= G250), S240 (= S251), T241 (≠ R252), V243 (≠ G254), G264 (≠ S276), Q343 (= Q355), E393 (= E402)
- binding retinoic acid: G118 (vs. gap), R121 (= R127), F164 (= F169), M168 (≠ F173), W171 (≠ G178), C295 (≠ F310), C296 (= C311)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
25% identity, 84% coverage: 14:463/535 of query aligns to 7:443/489 of 4cazA
- active site: N152 (= N168), K175 (= K193), E251 (= E274), C285 (= C311), E386 (= E402)
- 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 (≠ F164), G149 (= G165), W151 (≠ S167), N152 (= N168), K175 (= K193), E178 (≠ R196), G208 (= G230), G212 (= G234), F226 (= F248), T227 (= T249), G228 (= G250), G229 (≠ S251), T232 (≠ G254), V236 (≠ L258), E251 (= E274), L252 (≠ M275), C285 (= C311), E386 (= E402), F388 (= F404)
Sites not aligning to the query:
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
25% identity, 84% coverage: 14:463/535 of query aligns to 7:443/489 of 2woxA
- active site: N152 (= N168), K175 (= K193), E251 (= E274), C285 (= C311), E386 (= E402)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F164), G149 (= G165), W151 (≠ S167), N152 (= N168), K175 (= K193), S177 (≠ H195), E178 (≠ R196), G208 (= G230), G212 (= G234), F226 (= F248), T227 (= T249), G228 (= G250), G229 (≠ S251), T232 (≠ G254), V236 (≠ L258), E251 (= E274), L252 (≠ M275), C285 (= C311), E386 (= E402), F388 (= F404)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
25% identity, 84% coverage: 14:463/535 of query aligns to 7:443/489 of 2wmeA
- active site: N152 (= N168), K175 (= K193), E251 (= E274), C285 (= C311), E386 (= E402)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G165), W151 (≠ S167), K175 (= K193), S177 (≠ H195), E178 (≠ R196), G208 (= G230), G212 (= G234), F226 (= F248), G228 (= G250), G229 (≠ S251), T232 (≠ G254), V236 (≠ L258)
Sites not aligning to the query:
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)
25% identity, 84% coverage: 14:463/535 of query aligns to 8:444/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 165:168) binding
- K162 (≠ D179) active site, Charge relay system
- KPSE 176:179 (≠ KAHR 193:196) binding
- G209 (= G230) binding
- GTST 230:233 (≠ SRAG 251:254) binding
- E252 (= E274) active site, Proton acceptor
- C286 (= C311) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E402) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
24% identity, 74% coverage: 67:461/535 of query aligns to 66:448/503 of Q84LK3
- N162 (= N168) 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 (≠ G178) 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).
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
25% identity, 77% coverage: 29:441/535 of query aligns to 22:420/477 of 2opxA
- active site: N151 (= N168), K174 (= K193), E249 (= E274), C283 (= C311), E381 (= E402)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ R114), F152 (= F169), N284 (= N313), F312 (vs. gap), G313 (= G338), R318 (vs. gap), D320 (vs. gap), I321 (≠ T343), A322 (≠ M344), Y362 (≠ A381)
Sites not aligning to the query:
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 29:439/479 of 6te5B
- active site: N157 (= N168), E256 (= E274), C290 (= C311)
- binding 6-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)imidazo[1,2-a]pyridine: E111 (vs. gap), G112 (vs. gap), T116 (≠ S128)
- binding nicotinamide-adenine-dinucleotide: I153 (vs. gap), T154 (vs. gap), W156 (≠ S167), K180 (= K193), E183 (≠ R196), G213 (= G230), F231 (= F248), S234 (= S251), V237 (≠ G254), Q337 (= Q355), K340 (≠ S358)
Sites not aligning to the query:
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
27% identity, 81% coverage: 33:463/535 of query aligns to 28:438/478 of 6tryA
- active site: N156 (= N168), E255 (= E274), C289 (= C311)
- binding nicotinamide-adenine-dinucleotide: I152 (vs. gap), T153 (vs. gap), W155 (≠ S167), K179 (= K193), A181 (≠ H195), E182 (≠ R196), G212 (= G230), G216 (= G234), A217 (≠ E235), F230 (= F248), G232 (= G250), S233 (= S251), V236 (≠ G254), K335 (≠ T354)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: I107 (≠ V126), G111 (vs. gap), T115 (≠ S128), L160 (≠ A172), C288 (≠ F310)
Sites not aligning to the query:
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
25% identity, 77% coverage: 29:441/535 of query aligns to 22:420/477 of 2impA
- active site: N151 (= N168), K174 (= K193), E249 (= E274), C283 (= C311), E381 (= E402)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ F164), L148 (≠ G165), P149 (≠ A166), W150 (≠ S167), K174 (= K193), E177 (≠ R196), F178 (≠ A197), G207 (= G230), G211 (= G234), Q212 (≠ E235), S228 (= S251), A231 (≠ G254), K234 (≠ A257), R334 (≠ G356)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
25% identity, 77% coverage: 29:441/535 of query aligns to 22:420/477 of 2iluA
- active site: N151 (= N168), K174 (= K193), E249 (= E274), C283 (= C311), E381 (= E402)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ F164), L148 (≠ G165), P149 (≠ A166), W150 (≠ S167), K174 (= K193), S176 (≠ H195), E177 (≠ R196), R206 (≠ A229), G207 (= G230), G211 (= G234), Q212 (≠ E235), S228 (= S251), A231 (≠ G254), K234 (≠ A257), I235 (≠ L258), N328 (≠ H350), R334 (≠ G356), F383 (= F404)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_05316 FitnessBrowser__Burk376:H281DRAFT_05316
MSSSSEVIGRITGEMLIGRQSVRGAEEALHAFNPATGADIAEPVFGSGTARDVGLACELA
QKAFDPYRQLPLSVRAEFLERIADGITALGDALVERAQQESGLPKARLEGERGRTTGQLK
LFAQFVRSGQWLDATLDSPLPERKPLPRSDLRMQKIAIGPVAVFGASNFPLAFSVAGGDT
AAALAAGCPVVVKAHRAHLGTSEMVGRVIQRVAQEMDLPEGVFSLIVGAGNSVGEALVAH
PAIKAVGFTGSRAGGLALMRVAAARPEPIPVFAEMSSINPVFLLPNALTQRTENIARGFV
DSLVLGAGQFCTNPGLAIAVDSDALKNFVAVASEALGGKPAQTMLTSGIHSAYTQGESKL
AGIPGVETVARGVDVTGPNQARAALFVTDAKTFLATPALEDEVFGPASTIVRCKDENELL
QVAEHFAGQLTATIQMDSADVPAARRLVPILERKAGRLLVNGYPTGVEVCHAMVHGGPFP
ATSDSRATSVGTTAIERFLRPVCYQDFPADLLPQALADDNPLDLWRRRDGEITRS
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