SitesBLAST
Comparing WP_089214808.1 NCBI__GCF_900188185.1:WP_089214808.1 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)
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