SitesBLAST
Comparing WP_013537247.1 NCBI__GCF_000185805.1:WP_013537247.1 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
41% identity, 89% coverage: 48:472/477 of query aligns to 53:475/480 of 5kf0A
- active site: N157 (= N152), K180 (= K175), E252 (= E248), C288 (= C284), E382 (= E379), E460 (= E457)
- binding magnesium ion: E88 (= E83)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I153 (= I148), S154 (≠ T149), P155 (= P150), F156 (= F151), N157 (= N152), L162 (= L157), K180 (= K175), S183 (≠ E178), R184 (≠ N179), R213 (≠ E209), T231 (= T227), G232 (= G228), S233 (= S229), V236 (≠ T232), E252 (= E248), L253 (= L249), C288 (= C284), E382 (= E379), F384 (= F381)
Sites not aligning to the query:
5j6bA Crystal structure of aldehyde dehydrogenase from burkholderia thailandensis in covelent complex with NADPH
40% identity, 88% coverage: 55:472/477 of query aligns to 61:476/481 of 5j6bA
- active site: N158 (= N152), K181 (= K175), E253 (= E248), C289 (= C284), E383 (= E379), E461 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I154 (= I148), S155 (≠ T149), P156 (= P150), F157 (= F151), N158 (= N152), L163 (= L157), K181 (= K175), A183 (≠ S177), S184 (≠ E178), R214 (≠ E209), T232 (= T227), G233 (= G228), S234 (= S229), V237 (≠ T232), L241 (≠ I236), E253 (= E248), L254 (= L249), C289 (= C284), E383 (= E379), F385 (= F381), Y450 (= Y446)
5n5sB Crystal structure of aldehyde dehydrogenase 21 (aldh21) from physcomitrella patens in complex with NADP+ (see paper)
41% identity, 87% coverage: 61:474/477 of query aligns to 64:475/481 of 5n5sB
- active site: N155 (= N152), K178 (= K175), E251 (= E248), C286 (= C284), E380 (= E379), E458 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V151 (≠ I148), S152 (≠ T149), P153 (= P150), W154 (≠ F151), N155 (= N152), L160 (= L157), K178 (= K175), A180 (≠ S177), S181 (≠ E178), R212 (≠ E209), A215 (≠ G212), T230 (= T227), G231 (= G228), S232 (= S229), I235 (≠ T232), E251 (= E248), L252 (= L249), C286 (= C284), 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, 97% coverage: 14:474/477 of query aligns to 1:454/456 of 3rhdA
- active site: N133 (= N152), H156 (≠ K175), E233 (= E248), C267 (= C284), E360 (= E379), E437 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (= I148), T130 (= T149), F132 (= F151), H156 (≠ K175), S158 (= S177), S159 (≠ E178), K160 (≠ N179), G193 (= G208), E194 (= E209), G197 (= G212), D198 (= D213), F211 (= F226), S214 (= S229), V217 (≠ T232)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
40% identity, 96% coverage: 17:476/477 of query aligns to 1:465/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I148), L137 (≠ T149), F139 (= F151), K163 (= K175), S165 (= S177), I166 (≠ E178), S196 (≠ G208), G200 (= G212), G216 (= G228), S217 (= S229), T220 (= T232), I224 (= I236)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
40% identity, 96% coverage: 17:476/477 of query aligns to 1:465/466 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 (= I148), L137 (≠ T149), F139 (= F151), K163 (= K175), S165 (= S177), I166 (≠ E178), S196 (≠ G208), G200 (= G212), G216 (= G228), S217 (= S229), T220 (= T232), I224 (= I236), L239 (= L249), C272 (= C284), E368 (= E379), F370 (= F381)
1uxuA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1uxuA
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding adenosine monophosphate: R70 (≠ K56), R77 (= R63), I131 (≠ V117), G132 (≠ L118), R152 (= R138), R153 (= R139)
- binding glyceraldehyde-3-phosphate: N166 (= N152), Y167 (≠ F153), R294 (≠ V283), C295 (= C284), D296 (≠ I285), R452 (≠ T438), H453 (≠ F439), G454 (≠ R440)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I148), T163 (= T149), P164 (= P150), F165 (= F151), K189 (= K175), S191 (= S177), I192 (≠ E178), P221 (≠ Y207), G222 (= G208), E226 (≠ D213), G241 (= G228), S242 (= S229), V245 (≠ T232), E393 (= E379), F395 (= F381)
1uxtA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1uxtA
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding 1-O-phosphono-alpha-D-glucopyranose: R70 (≠ K56), R77 (= R63), R152 (= R138), R153 (= R139)
- binding nicotinamide-adenine-dinucleotide: I162 (= I148), T163 (= T149), F165 (= F151), N166 (= N152), K189 (= K175), S191 (= S177), G222 (= G208), E226 (≠ D213), T240 (= T227), G241 (= G228), S242 (= S229), V245 (≠ T232), E261 (= E248), G263 (= G250), C295 (= C284), E393 (= E379), F395 (= F381)
1uxrA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1uxrA
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding 6-O-phosphono-beta-D-fructofuranose: R70 (≠ K56), R77 (= R63), I131 (≠ V117), R152 (= R138)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I148), T163 (= T149), F165 (= F151), N166 (= N152), K189 (= K175), S191 (= S177), I192 (≠ E178), P221 (≠ Y207), G222 (= G208), A225 (= A211), E226 (≠ D213), F239 (= F226), T240 (= T227), G241 (= G228), S242 (= S229), V245 (≠ T232), E261 (= E248), L262 (= L249), G263 (= G250), C295 (= C284), E393 (= E379), F395 (= F381)
1uxqA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1uxqA
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding 1-O-phosphono-alpha-D-glucopyranose: R70 (≠ K56), R77 (= R63), R152 (= R138), R153 (= R139)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I148), T163 (= T149), P164 (= P150), F165 (= F151), N166 (= N152), K189 (= K175), S191 (= S177), I192 (≠ E178), P221 (≠ Y207), G222 (= G208), A225 (= A211), E226 (≠ D213), T240 (= T227), G241 (= G228), S242 (= S229), V245 (≠ T232), E261 (= E248), L262 (= L249), G263 (= G250), C295 (= C284), E393 (= E379), F395 (= F381)
1uxnA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1uxnA
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding adenosine monophosphate: R70 (≠ K56), R77 (= R63), I131 (≠ V117), G132 (≠ L118), R152 (= R138), R153 (= R139), E154 (≠ V140), Y182 (≠ A168)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I148), T163 (= T149), F165 (= F151), N166 (= N152), K189 (= K175), S191 (= S177), I192 (≠ E178), P221 (≠ Y207), G222 (= G208), E226 (≠ D213), F239 (= F226), T240 (= T227), G241 (= G228), S242 (= S229), V245 (≠ T232), E261 (= E248), L262 (= L249), G263 (= G250), C295 (= C284), E393 (= E379), F395 (= F381)
O57693 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde phosphate dehydrogenase (NAD(P)); GAPN; EC 1.2.1.90 from Thermoproteus tenax (see 2 papers)
37% identity, 96% coverage: 17:475/477 of query aligns to 32:491/501 of O57693
- R72 (≠ K56) binding alpha-D-glucose 1-phosphate; binding AMP; binding beta-D-fructose 6-phosphate
- R79 (= R63) binding alpha-D-glucose 1-phosphate; binding AMP; binding beta-D-fructose 6-phosphate
- G134 (≠ L118) binding AMP
- RR 154:155 (= RR 138:139) binding alpha-D-glucose 1-phosphate; binding AMP
- T165 (= T149) binding NAD(+); binding NADP(+)
- N168 (= N152) binding D-glyceraldehyde 3-phosphate
- Y184 (≠ A168) binding beta-D-fructose 6-phosphate
- K191 (= K175) binding NAD(+)
- KPSI 191:194 (≠ KPSE 175:178) binding NADP(+)
- G224 (= G208) binding NADP(+)
- E228 (≠ D213) binding NAD(+); binding NADP(+)
- S244 (= S229) binding NAD(+); binding NADP(+)
- G265 (= G250) binding NAD(+); binding NADP(+)
- RCD 296:298 (≠ VCI 283:285) binding D-glyceraldehyde 3-phosphate
- E395 (= E379) binding NAD(+); binding NADP(+)
- HG 455:456 (≠ FR 439:440) binding D-glyceraldehyde 3-phosphate
1ky8A Crystal structure of the non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase (see paper)
37% identity, 96% coverage: 17:475/477 of query aligns to 30:489/499 of 1ky8A
- active site: N166 (= N152), K189 (= K175), E261 (= E248), C295 (= C284), E393 (= E379), E471 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I148), T163 (= T149), F165 (= F151), N166 (= N152), K189 (= K175), S191 (= S177), I192 (≠ E178), P221 (≠ Y207), G222 (= G208), A225 (= A211), E226 (≠ D213), F239 (= F226), T240 (= T227), G241 (= G228), S242 (= S229), V245 (≠ T232), E261 (= E248), L262 (= L249), G263 (= G250), C295 (= C284), E393 (= E379), F395 (= F381)
4i3xA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetate and cofactor NAD+ (see paper)
36% identity, 98% coverage: 6:474/477 of query aligns to 6:473/476 of 4i3xA
- active site: N149 (= N152), K172 (= K175), E245 (= E248), C282 (= C284), E376 (= E379), E456 (= E457)
- binding nicotinamide-adenine-dinucleotide: I145 (= I148), T146 (= T149), P147 (= P150), F148 (= F151), N149 (= N152), K172 (= K175), T174 (≠ S177), P205 (≠ G208), G209 (= G212), F223 (= F226), T224 (= T227), G225 (= G228), S226 (= S229), V229 (≠ T232), E245 (= E248), L246 (= L249), G247 (= G250), C282 (= C284), E376 (= E379), F378 (= F381), F444 (≠ Y446)
- binding phosphonoacetic acid: R99 (= R102), H150 (≠ F153), R281 (≠ V283), C282 (= C284), R438 (= R440)
4i3tA Structure of phosphonoacetaldehyde dehydrogenase in the apo state (see paper)
36% identity, 98% coverage: 6:474/477 of query aligns to 5:472/474 of 4i3tA
Q92UV7 Phosphonoacetaldehyde dehydrogenase; EC 1.2.1.- from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
36% identity, 98% coverage: 6:474/477 of query aligns to 15:482/485 of Q92UV7
- R108 (= R102) binding substrate; mutation to A: Decreased catalytic activity and decreased affinity for phosphonoacetaldehyde.
- TPF 155:157 (= TPF 149:151) binding NAD(+)
- N158 (= N152) mutation to A: Strongly decreased catalytic activity.
- H159 (≠ F153) binding substrate
- KPTE 181:184 (≠ KPSE 175:178) binding NAD(+)
- S235 (= S229) binding NAD(+)
- E254 (= E248) active site, Proton donor/acceptor; mutation to A: Loss of catalytic activity.
- R290 (≠ V283) mutation to A: Decreased catalytic activity and slightly decreased affinity for phosphonoacetaldehyde.
- RCT 290:292 (≠ VCI 283:285) binding substrate
- C291 (= C284) 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)
36% identity, 98% coverage: 6:474/477 of query aligns to 4:471/473 of 4i3wA
- active site: N147 (= N152), K170 (= K175), E243 (= E248), C280 (= C284), E374 (= E379), E454 (= E457)
- binding glyceraldehyde-3-phosphate: R97 (= R102), H148 (≠ F153), M152 (≠ L157), R279 (≠ V283), C280 (= C284), R436 (= R440)
- binding nicotinamide-adenine-dinucleotide: I143 (= I148), T144 (= T149), P145 (= P150), F146 (= F151), K170 (= K175), T172 (≠ S177), P203 (≠ G208), G207 (= G212), F221 (= F226), G223 (= G228), S224 (= S229), V227 (≠ T232)
4i3uA Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetaldehyde (see paper)
36% identity, 98% coverage: 6:474/477 of query aligns to 4:471/473 of 4i3uA
- active site: N147 (= N152), K170 (= K175), E243 (= E248), C280 (= C284), E374 (= E379), E454 (= E457)
- binding phosphonoacetaldehyde: R97 (= R102), H148 (≠ F153), M152 (≠ L157), R279 (≠ V283), C280 (= C284), R436 (= R440)
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)
36% identity, 100% coverage: 1:476/477 of query aligns to 1:474/475 of Q59931
- R103 (= R102) binding substrate
- S151 (≠ T149) binding NADP(+)
- K177 (= K175) binding NADP(+)
- T180 (≠ E178) binding NADP(+)
- D215 (= D213) binding NADP(+)
- 230:251 (vs. 228:249, 32% identical) binding NADP(+)
- E377 (= E379) binding NADP(+)
- R437 (≠ F439) binding substrate
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
36% identity, 98% coverage: 8:476/477 of query aligns to 8:473/474 of 2esdA
- active site: N153 (= N152), K176 (= K175), A249 (≠ E248), C283 (= C284), E376 (= E379), Q454 (≠ E457)
- binding glyceraldehyde-3-phosphate: R102 (= R102), Y154 (≠ F153), R282 (≠ V283), C283 (= C284), T284 (≠ I285), Q435 (≠ T438), R436 (≠ F439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (= F151), K176 (= K175), P178 (≠ S177), T179 (≠ E178), G209 (= G208), G213 (= G212), D214 (= D213), F227 (= F226), S230 (= S229), I233 (≠ T232), K328 (≠ N330), S329 (≠ A331), Y332 (≠ R334)
Query Sequence
>WP_013537247.1 NCBI__GCF_000185805.1:WP_013537247.1
MIKGYMLIGGKKVFKKEEIVIDFPFDGSPVGTVPRGKKEDVELAVETALKGFEKVKSMTA
YERYQALQKAARIIASRSREFAELLTLEVGKTIKESMGEVGRAVNTITLSAEEAKRVLGE
EVRFDAAPGIKGKVGFFRRVPLGVIGCITPFNFPLNLTCHKVAPALAAGNAVVIKPSENT
SLTVIKLAEVLVEAGFPPEAVNVVTGYGEEAGDALVRDERVRMITFTGSVATGKIIMSRG
GLKKYAMELGSNAGVYVDKDQTGRLKELAERIGRGGYALAGQVCISVQRVFVHESLFEEF
TKELCSFSKSLKVGDPRLEETDVGPVIDRNAADRIMEWIEEARSMGAQVLCGGRRLSETL
IEPTVVVNVPREAKLFRQEVFGPVIVVNPVDSLEAAIEAVNDSPYGLQAGIFTNDLKAAF
KFAEEVECGGIMVNEIPTFRVDQMPYGGVKESGIGREGPKFAVEEMTEIKTICFDLN
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