SitesBLAST
Comparing PfGW456L13_5044 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_5044 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
38% identity, 98% coverage: 11:480/481 of query aligns to 14:480/481 of 3jz4A
- active site: N156 (= N152), K179 (= K175), E254 (= E250), C288 (= C284), E385 (= E383), E462 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P150), W155 (= W151), K179 (= K175), A181 (= A177), S182 (≠ D178), A212 (≠ G208), G216 (= G212), G232 (= G228), S233 (= S229), I236 (≠ V232), C288 (= C284), K338 (≠ Q334), E385 (= E383), F387 (= F385)
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)
38% identity, 98% coverage: 11:480/481 of query aligns to 15:481/482 of P25526
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, 97% coverage: 10:475/481 of query aligns to 21:489/505 of 4neaA
- active site: N166 (= N152), K189 (= K175), E264 (= E250), C298 (= C284), E399 (= E383), E476 (= E462)
- binding nicotinamide-adenine-dinucleotide: P164 (= P150), K189 (= K175), E192 (≠ D178), G222 (= G208), G226 (= G212), G242 (= G228), G243 (≠ S229), T246 (≠ V232), H249 (≠ Q235), I250 (= I236), C298 (= C284), E399 (= E383), F401 (= F385)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 97% coverage: 10:476/481 of query aligns to 21:493/498 of 4go2A
- active site: N170 (= N152), K193 (= K175), E269 (= E250), C303 (= C284), E400 (= E383), D479 (≠ E462)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I148), I167 (≠ T149), P168 (= P150), W169 (= W151), K193 (= K175), A195 (= A177), Q196 (≠ D178), S225 (= S207), G226 (= G208), G230 (= G212), Q231 (≠ D213), F244 (= F226), G246 (= G228), S247 (= S229), V250 (= V232), I254 (= I236), E269 (= E250), G271 (= G252), C303 (= C284), E400 (= E383), F402 (= F385)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 97% coverage: 10:476/481 of query aligns to 21:493/498 of 2o2rA
- active site: N170 (= N152), K193 (= K175), E269 (= E250), C303 (= C284), E400 (= E383), D479 (≠ E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I148), I167 (≠ T149), W169 (= W151), K193 (= K175), A195 (= A177), Q196 (≠ D178), S225 (= S207), G226 (= G208), G230 (= G212), Q231 (≠ D213), F244 (= F226), S247 (= S229), V250 (= V232), I254 (= I236)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 97% coverage: 10:476/481 of query aligns to 106:578/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K175), S310 (= S207), G311 (= G208), G315 (= G212), G331 (= G228), S332 (= S229), V335 (= V232)
- binding 4'-phosphopantetheine: K201 (≠ G102), F382 (≠ Y278), N387 (≠ R283), C388 (= C284), N545 (≠ T441)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
38% identity, 97% coverage: 10:476/481 of query aligns to 425:897/902 of P28037
- IPW 571:573 (≠ TPW 149:151) binding
- KPAQ 597:600 (≠ KPAD 175:178) binding
- GSLVGQ 630:635 (≠ GRVVGD 208:213) binding
- GS 650:651 (= GS 228:229) binding
- E673 (= E250) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (≠ EM 250:251) binding
- C707 (= C284) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ Q334) binding
- ESF 804:806 (≠ EIF 383:385) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
P54115 Magnesium-activated aldehyde dehydrogenase, cytosolic; Mg(2+)-activated acetaldehyde dehydrogenase; Mg(2+)-ACDH; EC 1.2.1.-; EC 1.2.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
37% identity, 98% coverage: 10:479/481 of query aligns to 29:498/500 of P54115
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 3 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
40% identity, 97% coverage: 10:476/481 of query aligns to 21:493/498 of 7yjjC
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
37% identity, 97% coverage: 9:476/481 of query aligns to 29:500/515 of 2d4eC
- active site: N173 (= N152), K196 (= K175), E271 (= E250), C305 (= C284), E409 (= E383), E486 (= E462)
- binding nicotinamide-adenine-dinucleotide: I169 (= I148), T170 (= T149), P171 (= P150), W172 (= W151), K196 (= K175), A198 (= A177), G229 (= G208), G233 (= G212), A234 (≠ D213), T248 (= T227), G249 (= G228), E250 (≠ S229), T253 (≠ V232), E271 (= E250), L272 (≠ M251), C305 (= C284), E409 (= E383), F411 (= F385), F475 (= F450)
O75891 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; EC 1.5.1.6 from Homo sapiens (Human) (see 2 papers)
40% identity, 97% coverage: 10:476/481 of query aligns to 425:897/902 of O75891
- A511 (≠ E93) to V: in a colorectal cancer sample; somatic mutation; dbSNP:rs768309358
Sites not aligning to the query:
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity.
7radA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 10:479/481 of query aligns to 16:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), M167 (≠ I157), K185 (= K175), E188 (≠ D178), G218 (= G208), G222 (= G212), A223 (≠ D213), T237 (= T227), G238 (= G228), S239 (= S229), V242 (= V232), E261 (= E250), L262 (≠ M251), C295 (= C284), E392 (= E383), F394 (= F385)
- 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 (≠ R106), F163 (= F153), E285 (≠ Q274), F289 (≠ Y278), N450 (≠ T441), V452 (= V444)
7mjdA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 10:479/481 of query aligns to 16:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), M167 (≠ I157), K185 (= K175), E188 (≠ D178), G218 (= G208), G222 (= G212), F236 (= F226), T237 (= T227), G238 (= G228), S239 (= S229), V242 (= V232), E261 (= E250), L262 (≠ M251), C295 (= C284), E392 (= E383), F394 (= F385)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R106), E285 (≠ Q274), F289 (≠ Y278), N450 (≠ T441), V452 (= V444)
7mjcA Crystal structure analysis of aldh1b1
38% identity, 98% coverage: 10:479/481 of query aligns to 16:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), K185 (= K175), E188 (≠ D178), G218 (= G208), G222 (= G212), T237 (= T227), G238 (= G228), S239 (= S229), V242 (= V232), E261 (= E250), L262 (≠ M251), C295 (= C284), E392 (= E383), F394 (= F385)
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: 10:475/481 of query aligns to 11:480/497 of P17202
- I28 (= I25) binding
- D96 (≠ E92) binding
- SPW 156:158 (≠ TPW 149:151) binding
- Y160 (≠ F153) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAD 175:178) binding
- L186 (= L179) binding
- SSAT 236:239 (≠ SVGV 229:232) binding
- V251 (≠ Q244) binding in other chain
- L258 (≠ M251) binding
- W285 (≠ Y278) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E383) binding
- A441 (≠ M434) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V444) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F450) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K454) binding
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
36% identity, 98% coverage: 10:479/481 of query aligns to 7:477/489 of 4o6rA
- active site: N150 (= N152), K173 (= K175), E248 (= E250), C282 (= C284), E383 (= E383), E460 (= E462)
- binding adenosine monophosphate: I146 (= I148), V147 (≠ T149), K173 (= K175), G206 (= G208), G210 (= G212), Q211 (≠ D213), F224 (= F226), G226 (= G228), S227 (= S229), T230 (≠ V232), R233 (≠ Q235)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 97% coverage: 10:476/481 of query aligns to 14:483/494 of 4pz2B
- active site: N159 (= N152), K182 (= K175), E258 (= E250), C292 (= C284), E392 (= E383), D469 (≠ E462)
- binding nicotinamide-adenine-dinucleotide: I155 (= I148), I156 (≠ T149), P157 (= P150), W158 (= W151), N159 (= N152), M164 (≠ I157), K182 (= K175), A184 (= A177), E185 (≠ D178), G215 (= G208), G219 (= G212), F233 (= F226), T234 (= T227), G235 (= G228), S236 (= S229), V239 (= V232), E258 (= E250), L259 (≠ M251), C292 (= C284), E392 (= E383), F394 (= F385)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 16:483/493 of 4fr8A
- active site: N162 (= N152), K185 (= K175), Q261 (≠ E250), C295 (= C284), E392 (= E383), E469 (= E462)
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), W161 (= W151), K185 (= K175), G218 (= G208), G222 (= G212), A223 (≠ D213), F236 (= F226), G238 (= G228), S239 (= S229), I242 (≠ V232), Q342 (= Q331), K345 (≠ Q334), E392 (= E383), F394 (= F385)
- binding propane-1,2,3-triyl trinitrate: F163 (= F153), L166 (≠ A156), W170 (= W160), F289 (≠ Y278), S294 (≠ R283), C295 (= C284), D450 (≠ H447), F452 (vs. gap)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 17:484/494 of 5l13A
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E383), E470 (= E462)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F153), M168 (≠ I157), W171 (= W160), F290 (≠ Y278), C295 (≠ R283), C296 (= C284), C297 (≠ T285), D451 (≠ H447), F453 (vs. gap)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 17:484/494 of 4kwgA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E383), E470 (= E462)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F153), M168 (≠ I157), C295 (≠ R283), C296 (= C284), C297 (≠ T285), D451 (≠ H447), F453 (vs. gap)
Query Sequence
>PfGW456L13_5044 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_5044
VADTKRFDNYINGEWVAGGDYSTNINPSELTDAIGDYAKADLAQVHAAIDAARAAFPAWS
TSGIQARHDSLDKVGTEILARREELGTLLAREEGKTLPEAIGEVTRAGNIFKFFAGECLR
LSGDYLPSVRPGVNVEVTREALGVVGLITPWNFPIAIPAWKIAPALAYGNCVVLKPADLV
PGCAWALAEIISRAGFPAGVFNLVMGSGRVVGDALVHSPKVDGISFTGSVGVGRQIAVSC
VSRQAKVQLEMGGKNPQIILDDADLKQAVELSVQSAFYSTGQRCTASSRFIVTAGIHDQF
VEAMAERMKSIKVGHALKAGTDIGPVVSQAQLEQDMKYIDIGQSEGARLVSGGGLVTCDT
EGYFLAPTLFADSEASMRISQEEIFGPVANIVRVADYEAALAMANDTEFGLSAGIATTSL
KYANHFKRHSQAGMVMVNLPTAGVDYHVPFGGRKGSSYGSREQGRYAQEFYTVVKTSYIG
S
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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