SitesBLAST
Comparing PP_2694 FitnessBrowser__Putida:PP_2694 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)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
35% identity, 99% coverage: 1:474/480 of query aligns to 13:489/505 of 4neaA
- active site: N166 (= N151), K189 (= K174), E264 (= E249), C298 (= C283), E399 (= E382), E476 (= E461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P149), K189 (= K174), E192 (≠ N177), G222 (= G207), G226 (= G211), G242 (= G227), G243 (≠ S228), T246 (= T231), H249 (≠ R234), I250 (≠ V235), C298 (= C283), E399 (= E382), F401 (= F384)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
38% identity, 98% coverage: 9:476/480 of query aligns to 14:484/494 of 4pz2B
- active site: N159 (= N151), K182 (= K174), E258 (= E249), C292 (= C283), E392 (= E382), D469 (≠ E461)
- binding nicotinamide-adenine-dinucleotide: I155 (= I147), I156 (≠ T148), P157 (= P149), W158 (= W150), N159 (= N151), M164 (≠ T156), K182 (= K174), A184 (= A176), E185 (≠ N177), G215 (= G207), G219 (= G211), F233 (= F225), T234 (= T226), G235 (= G227), S236 (= S228), V239 (≠ T231), E258 (= E249), L259 (≠ M250), C292 (= C283), E392 (= E382), F394 (= F384)
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)
35% identity, 97% coverage: 9:474/480 of query aligns to 11:480/497 of P17202
- I28 (≠ Y24) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ TPW 148:150) binding
- Y160 (≠ F152) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAN 174:177) binding
- L186 (= L178) binding
- SSAT 236:239 (≠ SLQT 228:231) binding
- V251 (= V244) binding in other chain
- L258 (≠ M250) binding
- W285 (≠ F277) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E382) binding
- A441 (≠ C433) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ T443) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F449) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K453) binding
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
36% identity, 97% coverage: 9:474/480 of query aligns to 13:485/505 of O24174
- N164 (= N151) 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 (= W159) 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.
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 97% coverage: 9:474/480 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N151), K180 (= K174), E255 (= E249), A289 (≠ C283), E388 (= E382), E465 (= E461)
- binding 3-aminopropan-1-ol: C448 (≠ T443), W454 (≠ F449)
- binding nicotinamide-adenine-dinucleotide: I153 (= I147), S154 (≠ T148), P155 (= P149), W156 (= W150), N157 (= N151), M162 (≠ T156), K180 (= K174), S182 (≠ A176), E183 (≠ N177), G213 (= G207), G217 (= G211), A218 (≠ E212), T232 (= T226), G233 (= G227), S234 (= S228), T237 (= T231), E255 (= E249), L256 (≠ M250), A289 (≠ C283), E388 (= E382), F390 (= F384)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
35% identity, 97% coverage: 10:474/480 of query aligns to 14:475/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E249), C288 (= C283), E385 (= E382), E462 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (= A176), S182 (≠ N177), A212 (≠ G207), G216 (= G211), G232 (= G227), S233 (= S228), I236 (≠ T231), C288 (= C283), K338 (≠ Q333), E385 (= E382), F387 (= F384)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
36% identity, 97% coverage: 9:475/480 of query aligns to 9:477/489 of 4cazA
- active site: N152 (= N151), K175 (= K174), E251 (= E249), C285 (= C283), E386 (= E382), E463 (= E461)
- 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 (= I147), G149 (≠ T148), W151 (= W150), N152 (= N151), K175 (= K174), E178 (≠ N177), G208 (= G207), G212 (= G211), F226 (= F225), T227 (= T226), G228 (= G227), G229 (≠ S228), T232 (= T231), V236 (= V235), E251 (= E249), L252 (≠ M250), C285 (= C283), E386 (= E382), F388 (= F384)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
36% identity, 97% coverage: 9:475/480 of query aligns to 9:477/489 of 2woxA
- active site: N152 (= N151), K175 (= K174), E251 (= E249), C285 (= C283), E386 (= E382), E463 (= E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I147), G149 (≠ T148), W151 (= W150), N152 (= N151), K175 (= K174), S177 (≠ A176), E178 (≠ N177), G208 (= G207), G212 (= G211), F226 (= F225), T227 (= T226), G228 (= G227), G229 (≠ S228), T232 (= T231), V236 (= V235), E251 (= E249), L252 (≠ M250), C285 (= C283), E386 (= E382), F388 (= F384)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
36% identity, 97% coverage: 9:475/480 of query aligns to 9:477/489 of 2wmeA
- active site: N152 (= N151), K175 (= K174), E251 (= E249), C285 (= C283), E386 (= E382), E463 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T148), W151 (= W150), K175 (= K174), S177 (≠ A176), E178 (≠ N177), G208 (= G207), G212 (= G211), F226 (= F225), G228 (= G227), G229 (≠ S228), T232 (= T231), V236 (= V235)
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)
36% identity, 97% coverage: 9:475/480 of query aligns to 10:478/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 148:151) binding
- K162 (= K160) active site, Charge relay system
- KPSE 176:179 (≠ KPAN 174:177) binding
- G209 (= G207) binding
- GTST 230:233 (≠ SLQT 228:231) binding
- E252 (= E249) active site, Proton acceptor
- C286 (= C283) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E382) binding
- E464 (= E461) active site, Charge relay system
7radA Crystal structure analysis of aldh1b1
36% identity, 99% coverage: 6:479/480 of query aligns to 12:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (≠ T156), K185 (= K174), E188 (≠ N177), G218 (= G207), G222 (= G211), A223 (≠ E212), T237 (= T226), G238 (= G227), S239 (= S228), V242 (≠ T231), E261 (= E249), L262 (≠ M250), C295 (= C283), E392 (= E382), F394 (= F384)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ R105), F163 (= F152), E285 (≠ N273), F289 (= F277), N450 (≠ T440), V452 (≠ G442)
7mjdA Crystal structure analysis of aldh1b1
36% identity, 99% coverage: 6:479/480 of query aligns to 12:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (≠ T156), K185 (= K174), E188 (≠ N177), G218 (= G207), G222 (= G211), F236 (= F225), T237 (= T226), G238 (= G227), S239 (= S228), V242 (≠ T231), E261 (= E249), L262 (≠ M250), C295 (= C283), E392 (= E382), F394 (= F384)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R105), E285 (≠ N273), F289 (= F277), N450 (≠ T440), V452 (≠ G442)
7mjcA Crystal structure analysis of aldh1b1
36% identity, 99% coverage: 6:479/480 of query aligns to 12:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), K185 (= K174), E188 (≠ N177), G218 (= G207), G222 (= G211), T237 (= T226), G238 (= G227), S239 (= S228), V242 (≠ T231), E261 (= E249), L262 (≠ M250), C295 (= C283), E392 (= E382), F394 (= F384)
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)
34% identity, 97% coverage: 10:474/480 of query aligns to 15:476/482 of P25526
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
37% identity, 97% coverage: 9:474/480 of query aligns to 9:479/496 of 4i9bA
- active site: N157 (= N151), K180 (= K174), E255 (= E249), C290 (= C283), E389 (= E382), D466 (≠ E461)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C283), W455 (≠ F449)
- binding nicotinamide-adenine-dinucleotide: I153 (= I147), T154 (= T148), W156 (= W150), K180 (= K174), S182 (≠ A176), E183 (≠ N177), G213 (= G207), G217 (= G211), G218 (≠ E212), F231 (= F225), S234 (= S228), T237 (= T231), I241 (≠ V235)
Q56R04 Aminoaldehyde dehydrogenase 1; SlAMADH1; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Betaine aldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; 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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) (see paper)
37% identity, 97% coverage: 9:474/480 of query aligns to 14:484/504 of Q56R04
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)
37% identity, 88% coverage: 58:478/480 of query aligns to 68:491/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
37% identity, 88% coverage: 58:478/480 of query aligns to 63:486/500 of 4i8pA
- active site: N159 (= N151), K182 (= K174), E257 (= E249), C291 (= C283), E390 (= E382), E467 (= E461)
- binding nicotinamide-adenine-dinucleotide: I155 (= I147), T156 (= T148), P157 (= P149), W158 (= W150), N159 (= N151), M164 (≠ T156), K182 (= K174), S184 (≠ A176), E185 (≠ N177), G215 (= G207), G219 (= G211), A220 (≠ E212), T234 (= T226), G235 (= G227), S236 (= S228), T239 (= T231), E257 (= E249), L258 (≠ M250), C291 (= C283), E390 (= E382), F392 (= F384), W456 (≠ F449)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
32% identity, 98% coverage: 8:479/480 of query aligns to 12:486/487 of Q9H2A2
- R109 (= R105) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N151) mutation to A: Complete loss of activity.
- R451 (≠ T443) mutation to A: Complete loss of activity.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 98% coverage: 9:479/480 of query aligns to 20:489/491 of 5gtlA
- active site: N165 (= N151), K188 (= K174), E263 (= E249), C297 (= C283), E394 (= E382), E471 (= E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I147), P163 (= P149), K188 (= K174), A190 (= A176), E191 (≠ N177), Q192 (≠ L178), G221 (= G207), G225 (= G211), G241 (= G227), S242 (= S228), T245 (= T231), L264 (≠ M250), C297 (= C283), E394 (= E382), F396 (= F384)
Query Sequence
>PP_2694 FitnessBrowser__Putida:PP_2694
MSHKTYNNYIDGQWCEGHATLGNYSPSDTGDLIGQYHQASAEQARQAIQAARAAQPLWAA
SGLESRQQVLMAIGDELIARKEELGELLSREEGKPLAEGIGEVNRSGQFFHYYAAEVLRQ
MGETAASVRPGVDIEVHREPVGVVGIITPWNFPMATAAWKIAPALAFGNAVVFKPANLVP
ASAWALTEIISRQGLPSGTFNLVMGSGADVGEALIQSAEIDALTFTGSLQTGRRVAVATA
GNLVRCQLEMGSKNALVVMDDADLELAVECALNGAFFGTGQKCTASSRLIVCDGIHDRFV
EALRLRMRQLKVGHALEAGVQIGPVADARQLEQNLAYLQLAQAEGATLIEGGERLQLACD
GYYMRPALFINSRNDMRINREEVFGPIACVIRVRDFEEALATLNDTEYGLTAGIITQSLR
HASHFKRRAQTGCVMVNLPTAGTDYHVPFGGRKASSFGPREQGQYARDFYTVVKTTYLRP
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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