SitesBLAST
Comparing CCNA_02881 FitnessBrowser__Caulo:CCNA_02881 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
47% identity, 95% coverage: 25:523/528 of query aligns to 8:501/504 of 1eyyA
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
29% identity, 60% coverage: 3:321/528 of query aligns to 1:298/488 of 5u0mA
- active site: N148 (= N160), K171 (= K185), E246 (= E266), C280 (= C303)
- binding nicotinamide-adenine-dinucleotide: F144 (= F156), Y147 (≠ S159), N148 (= N160), K171 (= K185), S173 (≠ H187), E174 (≠ P188), G207 (≠ S226), T222 (= T241), G223 (= G242), S224 (= S243), V227 (≠ G246), E246 (= E266), M247 (= M267), G248 (≠ S268), C280 (= C303)
Sites not aligning to the query:
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
29% identity, 60% coverage: 3:321/528 of query aligns to 1:298/488 of 5u0lA
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
31% identity, 54% coverage: 39:321/528 of query aligns to 35:297/486 of 3ju8A
- active site: N147 (= N160), K170 (= K185), E245 (= E266), C279 (= C303)
- binding nicotinamide-adenine-dinucleotide: G144 (= G157), Y146 (≠ S159), N147 (= N160), L152 (≠ V167), K170 (= K185), S172 (≠ H187), F220 (= F240), T221 (= T241), G222 (= G242), S223 (= S243), T226 (≠ G246), E245 (= E266), M246 (= M267), G247 (≠ S268), C279 (= C303)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
29% identity, 57% coverage: 7:305/528 of query aligns to 7:287/489 of 4cazA
- active site: N152 (= N160), K175 (= K185), E251 (= E266), C285 (= C303)
- 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 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ P188), G208 (= G222), G212 (≠ S226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ G246), V236 (≠ L250), E251 (= E266), L252 (≠ M267), C285 (= C303)
Sites not aligning to the query:
- active site: 386, 463
- 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: 386, 388
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
29% identity, 57% coverage: 7:305/528 of query aligns to 7:287/489 of 2woxA
- active site: N152 (= N160), K175 (= K185), E251 (= E266), C285 (= C303)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), S177 (≠ H187), E178 (≠ P188), G208 (= G222), G212 (≠ S226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ G246), V236 (≠ L250), E251 (= E266), L252 (≠ M267), C285 (= C303)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
29% identity, 57% coverage: 7:305/528 of query aligns to 7:287/489 of 2wmeA
- active site: N152 (= N160), K175 (= K185), E251 (= E266), C285 (= C303)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G157), W151 (≠ S159), K175 (= K185), S177 (≠ H187), E178 (≠ P188), G208 (= G222), G212 (≠ S226), F226 (= F240), G228 (= G242), G229 (≠ S243), T232 (≠ G246), V236 (≠ L250)
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)
29% identity, 57% coverage: 7:305/528 of query aligns to 8:288/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 157:160) binding
- K162 (≠ D171) active site, Charge relay system
- KPSE 176:179 (≠ KAHP 185:188) binding
- G209 (= G222) binding
- GTST 230:233 (≠ SRRG 243:246) binding
- E252 (= E266) active site, Proton acceptor
- C286 (= C303) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
3efvA Crystal structure of a putative succinate-semialdehyde dehydrogenase from salmonella typhimurium lt2 with bound NAD (see paper)
28% identity, 42% coverage: 25:245/528 of query aligns to 9:212/459 of 3efvA
- active site: N134 (= N160)
- binding nicotinamide-adenine-dinucleotide: I130 (≠ F156), M131 (≠ G157), P132 (≠ A158), W133 (≠ S159), N134 (= N160), Q139 (≠ F165), R142 (≠ A168), K157 (= K185), A159 (≠ H187), N190 (≠ G222), V193 (= V225), T208 (= T241), G209 (= G242), S210 (= S243)
Sites not aligning to the query:
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
27% identity, 58% coverage: 6:310/528 of query aligns to 11:303/505 of O24174
- N164 (= N160) 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 (≠ G170) 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.
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 20:247/483 of 4ou2A
- active site: N152 (= N160), K175 (= K185)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), G208 (= G222), G213 (vs. gap), E214 (≠ Q227), F227 (= F240), T228 (= T241), G229 (= G242), E230 (vs. gap), T233 (≠ R245)
Sites not aligning to the query:
- active site: 251, 285, 387, 464
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: 285, 445, 447, 453
- binding nicotinamide-adenine-dinucleotide: 251, 252, 253, 285, 387, 389
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)
27% identity, 58% coverage: 7:310/528 of query aligns to 9:298/497 of P17202
- I28 (≠ V25) binding
- D96 (≠ E92) binding
- SPW 156:158 (≠ GAS 157:159) binding
- Y160 (≠ F161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G170) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KP-------SE 182:185 (≠ KAHPAHPGASE 185:195) binding
- L186 (= L196) binding
- SSAT 236:239 (≠ SRRG 243:246) binding
- V251 (≠ P258) binding in other chain
- L258 (≠ M267) binding
- W285 (≠ L297) mutation to A: Decreases binding affinity for betaine aldehyde.
Sites not aligning to the query:
- 390 binding
- 441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- 450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 20:247/483 of 4npiA
- active site: N152 (= N160), K175 (= K185)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165), W160 (≠ G170)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), K175 (= K185), E178 (≠ P188), G208 (= G222), G213 (vs. gap), E214 (≠ Q227), F227 (= F240), G229 (= G242), E230 (vs. gap), T233 (≠ R245)
Sites not aligning to the query:
- active site: 251, 285, 387, 464
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: 251, 285, 445, 447, 453
- binding nicotinamide-adenine-dinucleotide: 253, 285, 335, 387, 389
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 20:247/483 of 4i2rA
- active site: N152 (= N160), K175 (= K185)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ P188), G208 (= G222), F227 (= F240), T228 (= T241), G229 (= G242), E230 (vs. gap), T233 (≠ R245)
Sites not aligning to the query:
- active site: 251, 285, 387, 464
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: 285, 445, 447, 453
- binding nicotinamide-adenine-dinucleotide: 251, 252, 253, 285, 387, 389
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 20:247/483 of 4i25A
- active site: N152 (= N160), K175 (= K185)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R106), L157 (≠ F165)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), S149 (≠ G157), P150 (≠ A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ P188), G208 (= G222), G213 (vs. gap), F227 (= F240), T228 (= T241), G229 (= G242), E230 (vs. gap), T233 (≠ R245)
Sites not aligning to the query:
- active site: 251, 285, 387, 464
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: 285, 445, 447, 453
- binding nicotinamide-adenine-dinucleotide: 251, 252, 285, 387, 389
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 21:248/484 of 5kj5B
- active site: D153 (≠ N160), K176 (= K185)
- binding nicotinamide-adenine-dinucleotide: I149 (≠ F156), S150 (≠ G157), P151 (≠ A158), W152 (≠ S159), D153 (≠ N160), L158 (≠ F165), K176 (= K185), G209 (= G222), K210 (≠ Y223), G214 (vs. gap), F228 (= F240), T229 (= T241), G230 (= G242), E231 (vs. gap), T234 (≠ R245)
Sites not aligning to the query:
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
27% identity, 45% coverage: 24:259/528 of query aligns to 20:247/483 of 5kllA
Sites not aligning to the query:
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)
29% identity, 61% coverage: 9:328/528 of query aligns to 14:313/482 of P25526
Sites not aligning to the query:
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
26% identity, 82% coverage: 24:455/528 of query aligns to 46:465/515 of 2d4eC
- active site: N173 (= N160), K196 (= K185), E271 (= E266), C305 (= C303), E409 (= E395)
- binding nicotinamide-adenine-dinucleotide: I169 (≠ F156), T170 (≠ G157), P171 (≠ A158), W172 (≠ S159), K196 (= K185), A198 (≠ H187), G229 (= G222), G233 (≠ S226), A234 (≠ Q227), T248 (= T241), G249 (= G242), E250 (≠ S243), T253 (≠ G246), E271 (= E266), L272 (≠ M267), C305 (= C303), E409 (= E395), F411 (= F397)
Sites not aligning to the query:
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
28% identity, 57% coverage: 7:305/528 of query aligns to 7:285/495 of 4v37A
- active site: N157 (= N160), K180 (= K185), E255 (= E266)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F156), S154 (≠ G157), P155 (≠ A158), W156 (≠ S159), N157 (= N160), M162 (≠ V167), K180 (= K185), S182 (= S194), E183 (= E195), G213 (= G222), G217 (≠ S226), A218 (≠ Q227), T232 (= T241), G233 (= G242), S234 (= S243), T237 (≠ G246), E255 (= E266), L256 (≠ M267)
Sites not aligning to the query:
Query Sequence
>CCNA_02881 FitnessBrowser__Caulo:CCNA_02881
MAHLTGELLIGGERRFGIHGEIKGVNPATGETLEPAFGGATTADVEAACALAAEAFGPYR
SLPYETRAQFLESIAEHIEAIGDDLIVRTMAETGLPRPRLEGERGRTVGQLRLFAGVLRD
GGFLEARIDPAMPDRKPLPRPDLRLRNVPLGPVAVFGASNFPLAFSVAGGDTASALAAGC
PVIVKAHPAHPGASELVGRAIQAAVAACGLPPGVFALIHDSGYEVSQALVADPRVKAAGF
TGSRRGGLALLAIAQGRPEPIPFYAEMSSINPVILLPAALKARADKIAPDFVAALTLGAG
QFCTNPGLILAIDGPELDAFIEAAGKAVEAAPASVMLTPGICQAFAHGVAALTDAAEVTT
VARGVPGPDGSHTGRAALFSVTAADFLANPHLHEEVFGAASLVVRCAGQAELEAVIAALE
GQLTIALHMDEADHGIAGALLPALELKAGRILVNGFGTGVEVAPAMVHGGPFPSTSDGRT
TSVGTLAIARFLRPVSYQNLPEALLPAELKTQNPLGVVRRVDGVMKLG
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