SitesBLAST
Comparing PP_1256 FitnessBrowser__Putida:PP_1256 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)
49% identity, 96% coverage: 19:522/525 of query aligns to 3:502/504 of 1eyyA
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
29% identity, 61% coverage: 3:320/525 of query aligns to 2:298/488 of 5u0mA
- active site: N148 (= N159), K171 (= K184), E246 (= E265), C280 (= C302)
- binding nicotinamide-adenine-dinucleotide: F144 (= F155), Y147 (≠ S158), N148 (= N159), K171 (= K184), S173 (≠ H186), E174 (≠ S187), G207 (= G225), T222 (= T240), G223 (= G241), S224 (= S242), V227 (≠ G245), E246 (= E265), M247 (= M266), G248 (≠ S267), C280 (= C302)
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, 61% coverage: 3:320/525 of query aligns to 2:298/488 of 5u0lA
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)
28% identity, 81% coverage: 6:431/525 of query aligns to 8:402/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 156:159) binding
- K162 (≠ D170) active site, Charge relay system
- KPSE 176:179 (≠ KAHS 184:187) binding
- G209 (= G221) binding
- GTST 230:233 (≠ SRSG 242:245) binding
- E252 (= E265) active site, Proton acceptor
- C286 (= C302) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (≠ H416) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
26% identity, 82% coverage: 2:431/525 of query aligns to 12:412/482 of 5ek6A
- active site: N147 (= N159), K170 (= K184), E245 (= E265), C279 (= C302), E374 (= E393)
- binding 2-methylpropanal: I152 (≠ F164), K155 (≠ A167), T222 (= T240), E245 (= E265)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F155), T144 (≠ G156), W146 (≠ S158), N147 (= N159), I152 (≠ F164), K170 (= K184), A172 (≠ H186), S173 (= S187), P202 (≠ S220), G203 (= G221), G207 (= G225), F221 (= F239), T222 (= T240), G223 (= G241), E224 (≠ S242), T227 (≠ G245), I231 (≠ L249), E245 (= E265), L246 (≠ M266), C279 (= C302), E374 (= E393)
Sites not aligning to the query:
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
26% identity, 82% coverage: 2:431/525 of query aligns to 12:412/482 of 4h73A
- active site: N147 (= N159), K170 (= K184), E245 (= E265), C279 (= C302), E374 (= E393)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ F155), T144 (≠ G156), P145 (≠ A157), W146 (≠ S158), K170 (= K184), A172 (≠ H186), S173 (= S187), G203 (= G221), G207 (= G225), F221 (= F239), G223 (= G241), E224 (≠ S242), T227 (≠ G245)
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
28% identity, 81% coverage: 6:431/525 of query aligns to 7:401/489 of 4cazA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302), E386 (≠ H416)
- 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 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), E178 (≠ S187), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302), E386 (≠ H416), F388 (≠ E418)
Sites not aligning to the query:
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
28% identity, 81% coverage: 6:431/525 of query aligns to 7:401/489 of 2woxA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302), E386 (≠ H416)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), S177 (≠ H186), E178 (≠ S187), G208 (= G221), G212 (= G225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302), E386 (≠ H416), F388 (≠ E418)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
28% identity, 81% coverage: 6:431/525 of query aligns to 7:401/489 of 2wmeA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302), E386 (≠ H416)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G156), W151 (≠ S158), K175 (= K184), S177 (≠ H186), E178 (≠ S187), G208 (= G221), G212 (= G225), F226 (= F239), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249)
Sites not aligning to the query:
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
26% identity, 82% coverage: 2:431/525 of query aligns to 19:419/490 of 5ekcE
- active site: N154 (= N159), K177 (= K184), E252 (= E265), C286 (= C302), E381 (= E393)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ F155), T151 (≠ G156), P152 (≠ A157), W153 (≠ S158), K177 (= K184), S180 (= S187), G210 (= G221), G214 (= G225), F228 (= F239), G230 (= G241), E231 (≠ S242), T234 (≠ G245), N331 (≠ F341), R333 (≠ A343), Q334 (≠ Y344)
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
30% identity, 59% coverage: 3:313/525 of query aligns to 2:290/486 of 3ju8A
- active site: N147 (= N159), K170 (= K184), E245 (= E265), C279 (= C302)
- binding nicotinamide-adenine-dinucleotide: G144 (= G156), Y146 (≠ S158), N147 (= N159), L152 (≠ V166), K170 (= K184), S172 (≠ H186), F220 (= F239), T221 (= T240), G222 (= G241), S223 (= S242), T226 (≠ G245), E245 (= E265), M246 (= M266), G247 (≠ S267), C279 (= C302)
Sites not aligning to the query:
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
28% identity, 88% coverage: 6:468/525 of query aligns to 4:446/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
28% identity, 88% coverage: 6:468/525 of query aligns to 4:446/474 of 1wndA
- active site: N149 (= N159), K172 (= K184), E246 (= E265), C280 (= C302), E378 (= E393)
- binding calcium ion: G249 (≠ S268), K250 (≠ I269), A251 (≠ N270), G405 (≠ Q420), L406 (= L421), A407 (≠ T422), Y427 (≠ A446)
Sites not aligning to the query:
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
28% identity, 88% coverage: 6:468/525 of query aligns to 4:446/474 of 1wnbB
- active site: N149 (= N159), K172 (= K184), E246 (= E265), C280 (= C302), E378 (= E393)
- binding betaine aldehyde: D279 (≠ F301), F436 (≠ V458), L438 (≠ V460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ F155), A146 (≠ G156), W148 (≠ S158), K172 (= K184), G204 (= G221), G208 (= G225), D209 (≠ I226), T223 (= T240), G224 (= G241), S225 (= S242), T228 (≠ G245), H231 (≠ A248), G248 (≠ S267), E378 (= E393)
Sites not aligning to the query:
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
28% identity, 88% coverage: 6:468/525 of query aligns to 4:446/474 of 1wnbA
- active site: N149 (= N159), K172 (= K184), E246 (= E265), C280 (= C302), E378 (= E393)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ F155), A146 (≠ G156), W148 (≠ S158), K172 (= K184), G204 (= G221), G208 (= G225), D209 (≠ I226), G224 (= G241), S225 (= S242), T228 (≠ G245), H231 (≠ A248), G248 (≠ S267), F380 (= F395)
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)
25% identity, 74% coverage: 66:452/525 of query aligns to 74:448/503 of Q84LK3
- N162 (= N159) 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 (≠ G169) 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).
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)
24% identity, 84% coverage: 11:452/525 of query aligns to 17:445/497 of P17202
- I28 (= I24) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ GAS 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KAHS 184:187) binding
- L186 (≠ A188) binding
- SSAT 236:239 (≠ SR-S 242:244) binding
- V251 (≠ R256) binding in other chain
- L258 (≠ M266) binding
- W285 (≠ Q296) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E393) binding
- A441 (≠ R448) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
Sites not aligning to the query:
- 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
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
30% identity, 51% coverage: 11:276/525 of query aligns to 15:266/495 of 4v37A
- active site: N157 (= N159), K180 (= K184), E255 (= E265)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F155), S154 (≠ G156), P155 (≠ A157), W156 (≠ S158), N157 (= N159), M162 (≠ V166), K180 (= K184), S182 (≠ H186), E183 (≠ S187), G213 (= G221), G217 (= G225), A218 (≠ I226), T232 (= T240), G233 (= G241), S234 (= S242), T237 (≠ S244), E255 (= E265), L256 (≠ M266)
Sites not aligning to the query:
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
25% identity, 94% coverage: 1:494/525 of query aligns to 469:945/959 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
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 50% coverage: 58:322/525 of query aligns to 56:305/485 of 4u3wA
Sites not aligning to the query:
Query Sequence
>PP_1256 FitnessBrowser__Putida:PP_1256
MPLTGNLLIGQRPVTGSRDAIRAIDPTTGQTLEPAYLGGTGEHVAQACALAWAAFDAYRE
TSLEQRAEFLEAIATQIEALGDALIDRAVIETGLPKARIQGERGRTCTQLRTFARTVRAG
EWLDVRIDSALPERQPLPRADLRQRQVALGPVAVFGASNFPLAFSVAGGDTASALAAGCP
VVVKAHSAHPGTSELVGQAVAQAVKQCGLPEGVFSLLYGSGREVGIALVSDPRIKAVGFT
GSRSGGMALCQAAQARPEPIPVYAEMSSINPVFLFDAALQARAEALAQGFVASLTQGAGQ
FCTNPGLVIARQGPALQRFITAAAGYVQQGAAQTMLTPGIFSAYQAGIAALADNPHAQAI
TSGQAGQGPNQCQAQLFVTQAEAFLADPALQAEVFGAASLVVACTDDEQVRQVAEHLEGQ
LTATLQLDEADIDSARALLPTLERKAGRILVNGWPTGVEVCDAMVHGGPFPATSDARTTS
VGTAAILRFLRPVCYQDVPDALLPQALKHGNPLQLRRLLDGKRED
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