SitesBLAST
Comparing WP_089214808.1 NCBI__GCF_900188185.1:WP_089214808.1 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)
5kf0A Crystal structure of an aldedhyde dehydrogenase from burkholderia vietnamiensis
69% identity, 99% coverage: 3:476/477 of query aligns to 5:479/480 of 5kf0A
- active site: N157 (= N155), K180 (= K178), E252 (= E251), C288 (= C285), E382 (= E379), E460 (= E457)
- binding magnesium ion: E88 (≠ Y86)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I153 (= I151), S154 (= S152), P155 (= P153), F156 (= F154), N157 (= N155), L162 (= L160), K180 (= K178), S183 (= S181), R184 (≠ M182), R213 (= R212), T231 (= T230), G232 (= G231), S233 (= S232), V236 (= V235), E252 (= E251), L253 (= L252), C288 (= C285), E382 (= E379), F384 (= F381)
Sites not aligning to the query:
5j6bA Crystal structure of aldehyde dehydrogenase from burkholderia thailandensis in covelent complex with NADPH
69% identity, 99% coverage: 3:476/477 of query aligns to 6:480/481 of 5j6bA
- active site: N158 (= N155), K181 (= K178), E253 (= E251), C289 (= C285), E383 (= E379), E461 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I154 (= I151), S155 (= S152), P156 (= P153), F157 (= F154), N158 (= N155), L163 (= L160), K181 (= K178), A183 (= A180), S184 (= S181), R214 (= R212), T232 (= T230), G233 (= G231), S234 (= S232), V237 (= V235), L241 (= L239), E253 (= E251), L254 (= L252), C289 (= C285), E383 (= E379), F385 (= F381), Y450 (= Y446)
5n5sB Crystal structure of aldehyde dehydrogenase 21 (aldh21) from physcomitrella patens in complex with NADP+ (see paper)
52% identity, 98% coverage: 7:475/477 of query aligns to 6:476/481 of 5n5sB
- active site: N155 (= N155), K178 (= K178), E251 (= E251), C286 (= C285), E380 (= E379), E458 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V151 (≠ I151), S152 (= S152), P153 (= P153), W154 (≠ F154), N155 (= N155), L160 (= L160), K178 (= K178), A180 (= A180), S181 (= S181), R212 (= R212), A215 (= A215), T230 (= T230), G231 (= G231), S232 (= S232), I235 (≠ V235), E251 (= E251), L252 (= L252), C286 (= C285), E380 (= E379), F382 (= F381), Y447 (= Y446)
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
39% identity, 96% coverage: 21:476/477 of query aligns to 5:456/456 of 3rhdA
- active site: N133 (= N155), H156 (≠ K178), E233 (= E251), C267 (= C285), E360 (= E379), E437 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (= I151), T130 (≠ S152), F132 (= F154), H156 (≠ K178), S158 (≠ A180), S159 (= S181), K160 (≠ M182), G193 (≠ T211), E194 (≠ R212), G197 (≠ A215), D198 (= D216), F211 (= F229), S214 (= S232), V217 (= V235)
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)
36% identity, 90% coverage: 47:474/477 of query aligns to 53:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
36% identity, 90% coverage: 47:474/477 of query aligns to 52:479/481 of 3jz4A
- active site: N156 (= N155), K179 (= K178), E254 (= E251), C288 (= C285), E385 (= E379), E462 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P153), W155 (≠ F154), K179 (= K178), A181 (= A180), S182 (= S181), A212 (≠ R212), G216 (≠ A215), G232 (= G231), S233 (= S232), I236 (≠ V235), C288 (= C285), K338 (≠ R335), E385 (= E379), F387 (= F381)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
35% identity, 86% coverage: 58:468/477 of query aligns to 39:457/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I151), L137 (≠ S152), F139 (= F154), K163 (= K178), S165 (≠ A180), I166 (≠ S181), S196 (≠ T211), G200 (≠ A215), G216 (= G231), S217 (= S232), T220 (≠ V235), I224 (≠ L239)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
35% identity, 86% coverage: 58:468/477 of query aligns to 39:457/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (= I151), L137 (≠ S152), F139 (= F154), K163 (= K178), S165 (≠ A180), I166 (≠ S181), S196 (≠ T211), G200 (≠ A215), G216 (= G231), S217 (= S232), T220 (≠ V235), I224 (≠ L239), L239 (= L252), C272 (= C285), E368 (= E379), F370 (= F381)
Q92UV7 Phosphonoacetaldehyde dehydrogenase; EC 1.2.1.- from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
34% identity, 86% coverage: 60:471/477 of query aligns to 63:479/485 of Q92UV7
- R108 (= R105) binding substrate; mutation to A: Decreased catalytic activity and decreased affinity for phosphonoacetaldehyde.
- TPF 155:157 (≠ SPF 152:154) binding NAD(+)
- N158 (= N155) mutation to A: Strongly decreased catalytic activity.
- H159 (≠ F156) binding substrate
- KPTE 181:184 (≠ KPAS 178:181) binding NAD(+)
- S235 (= S232) binding NAD(+)
- E254 (= E251) active site, Proton donor/acceptor; mutation to A: Loss of catalytic activity.
- R290 (≠ S284) mutation to A: Decreased catalytic activity and slightly decreased affinity for phosphonoacetaldehyde.
- RCT 290:292 (≠ SCI 284:286) binding substrate
- C291 (= C285) active site, Nucleophile; mutation to A: Loss of catalytic activity.
- E385 (= E379) binding NAD(+); mutation to A: Decreased catalytic activity and decreased affinity for phosphonoacetaldehyde.
- R447 (= R440) binding substrate; mutation to A: Decreased catalytic activity and strongly decreased affinity for phosphonoacetaldehyde.
4i3wA Structure of phosphonoacetaldehyde dehydrogenase in complex with gylceraldehyde-3-phosphate and cofactor NAD+ (see paper)
34% identity, 86% coverage: 60:471/477 of query aligns to 52:468/473 of 4i3wA
- active site: N147 (= N155), K170 (= K178), E243 (= E251), C280 (= C285), E374 (= E379), E454 (= E457)
- binding glyceraldehyde-3-phosphate: R97 (= R105), H148 (≠ F156), M152 (≠ L160), R279 (≠ S284), C280 (= C285), R436 (= R440)
- binding nicotinamide-adenine-dinucleotide: I143 (= I151), T144 (≠ S152), P145 (= P153), F146 (= F154), K170 (= K178), T172 (≠ A180), P203 (≠ T211), G207 (≠ A215), F221 (= F229), G223 (= G231), S224 (= S232), V227 (= V235)
4i3uA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetaldehyde (see paper)
34% identity, 86% coverage: 60:471/477 of query aligns to 52:468/473 of 4i3uA
- active site: N147 (= N155), K170 (= K178), E243 (= E251), C280 (= C285), E374 (= E379), E454 (= E457)
- binding phosphonoacetaldehyde: R97 (= R105), H148 (≠ F156), M152 (≠ L160), R279 (≠ S284), C280 (= C285), R436 (= R440)
4i3xA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetate and cofactor NAD+ (see paper)
34% identity, 86% coverage: 60:471/477 of query aligns to 54:470/476 of 4i3xA
- active site: N149 (= N155), K172 (= K178), E245 (= E251), C282 (= C285), E376 (= E379), E456 (= E457)
- binding nicotinamide-adenine-dinucleotide: I145 (= I151), T146 (≠ S152), P147 (= P153), F148 (= F154), N149 (= N155), K172 (= K178), T174 (≠ A180), P205 (≠ T211), G209 (≠ A215), F223 (= F229), T224 (= T230), G225 (= G231), S226 (= S232), V229 (= V235), E245 (= E251), L246 (= L252), G247 (= G253), C282 (= C285), E376 (= E379), F378 (= F381), F444 (≠ Y446)
- binding phosphonoacetic acid: R99 (= R105), H150 (≠ F156), R281 (≠ S284), C282 (= C285), R438 (= R440)
4i3tA Structure of phosphonoacetaldehyde dehydrogenase in the apo state (see paper)
34% identity, 86% coverage: 60:471/477 of query aligns to 53:469/474 of 4i3tA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
34% identity, 99% coverage: 3:474/477 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I151), T153 (≠ S152), P154 (= P153), K179 (= K178), A212 (≠ R212), K213 (≠ D213), F230 (= F229), T231 (= T230), G232 (= G231), S233 (= S232), V236 (= V235), W239 (= W237), G256 (= G253)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
32% identity, 96% coverage: 16:474/477 of query aligns to 39:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I151), A171 (≠ S152), P172 (= P153), W173 (≠ F154), K197 (= K178), A230 (≠ R212), F248 (= F229), G250 (= G231), S251 (= S232), V254 (= V235), M257 (≠ D238), L273 (= L252), C306 (= C285), K356 (≠ R335), E403 (= E379), F405 (= F381)
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)
31% identity, 98% coverage: 7:473/477 of query aligns to 5:471/475 of Q59931
- R103 (= R105) binding substrate
- S151 (= S152) binding NADP(+)
- K177 (= K178) binding NADP(+)
- T180 (≠ S181) binding NADP(+)
- D215 (= D216) binding NADP(+)
- 230:251 (vs. 231:252, 36% identical) binding NADP(+)
- E377 (= E379) binding NADP(+)
- R437 (≠ Y439) binding substrate
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 91% coverage: 42:475/477 of query aligns to 63:496/503 of O14293
- S248 (= S232) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
31% identity, 98% coverage: 7:473/477 of query aligns to 4:470/474 of 2esdA
- active site: N153 (= N155), K176 (= K178), A249 (≠ E251), C283 (= C285), E376 (= E379), Q454 (≠ E457)
- binding glyceraldehyde-3-phosphate: R102 (= R105), Y154 (≠ F156), R282 (≠ S284), C283 (= C285), T284 (≠ I286), Q435 (≠ S438), R436 (≠ Y439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (= F154), K176 (= K178), P178 (≠ A180), T179 (≠ S181), G209 (vs. gap), G213 (≠ A215), D214 (= D216), F227 (= F229), S230 (= S232), I233 (≠ V235), K328 (= K331), S329 (≠ E332), Y332 (≠ R335)
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
31% identity, 98% coverage: 7:473/477 of query aligns to 4:470/474 of 1qi1B
- active site: N153 (= N155), K176 (= K178), E249 (= E251), S283 (≠ C285), E376 (= E379), Q454 (≠ E457)
- binding sn-glycerol-3-phosphate: Y154 (≠ F156), R282 (≠ S284), S283 (≠ C285), T284 (≠ I286), R436 (≠ Y439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (= P153), F152 (= F154), N153 (= N155), L158 (= L160), K176 (= K178), P178 (≠ A180), T179 (≠ S181), G209 (vs. gap), G213 (≠ A215), G229 (= G231), S230 (= S232), I233 (≠ V235), E249 (= E251), L250 (= L252), S283 (≠ C285)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
35% identity, 91% coverage: 44:477/477 of query aligns to 43:476/480 of 3rhhD
- active site: N155 (= N155), K178 (= K178), E251 (= E251), C285 (= C285), E378 (= E379), Q456 (≠ E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (= I151), P153 (= P153), F154 (= F154), K178 (= K178), P179 (= P179), A180 (= A180), T181 (≠ S181), G211 (= G214), G215 (vs. gap), D216 (= D216), F229 (= F229), G231 (= G231), G232 (≠ S232), T235 (≠ V235)
Query Sequence
>WP_089214808.1 NCBI__GCF_900188185.1:WP_089214808.1
MKLKDVYPLYLNNKAAQPNSDLVVTDKYSGEVAFRTALATPDVIDEAIAGAVRAAGPMAK
LASYEKQEVLNHCVVRFKERFDELAYALCVEAGKPIRDSEGEVTRLIDTFRIAAEEAVRN
YGEVQPLDISARARGYMGMWKRVPIGPCSFISPFNFPLNLAAHKIAPAIAMGCPFVMKPA
SMTPLGAIIMGEVLAECDILPEGAFSILPATRDGADLFTTDERLKLLSFTGSPAVGWDLK
AKAGKKKVILELGGNAAVIVDKDADLDHALERIIFGAFYQSGQSCIGVQRIIIHAEIYEK
FRDMLIEKTKTLVAGDPKDRATFIGPMISEKEAARLDGWIQDAIADGAKLLTGGKRDGAM
LEATLLENVDRGAKAYREEAFGPLAILSKFSDWKDAMAEVNDSKFGLQAGLFTRDFQQIL
DAWDELDVGGIVVNDVSSYRVDNMPYGGVKDSGLGREGIRFAMEDMSEIRNMVIRRA
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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