SitesBLAST
Comparing Pf6N2E2_3298 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) 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)
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)
36% 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 (= E178), G222 (= G208), G226 (= G212), G242 (= G228), G243 (≠ S229), T246 (≠ V232), H249 (≠ Q235), I250 (= I236), C298 (= C284), E399 (= E383), F401 (= F385)
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 (≠ E178), 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
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 (≠ E178), 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 (≠ E178), 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 (≠ KPAE 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)
38% identity, 97% coverage: 10:475/481 of query aligns to 29:494/500 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)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% 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)
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)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
39% identity, 97% coverage: 10:476/481 of query aligns to 21:493/498 of 7yjjC
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)
39% 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.
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
37% identity, 99% coverage: 5:479/481 of query aligns to 9:482/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W151), K180 (= K175), A182 (= A177), T212 (≠ S207), G213 (= G208), G217 (= G212), F231 (= F226), G233 (= G228), S234 (= S229), V237 (= V232), Q337 (= Q331), E388 (= E383), F390 (= F385)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
37% identity, 98% coverage: 3:472/481 of query aligns to 10:493/511 of 6fkuA
- active site: N159 (= N152), E261 (= E250), C295 (= C284), E483 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I148), T156 (= T149), N159 (= N152), K182 (= K175), S184 (≠ A177), E185 (= E178), G214 (≠ S207), G215 (= G208), K216 (≠ R209), G220 (= G212), Q221 (≠ D213), F237 (= F226), T238 (= T227), G239 (= G228), S240 (= S229), V243 (= V232), E261 (= E250), L262 (≠ M251), C295 (= C284), R342 (≠ A330), F343 (≠ Q331), E404 (= E383), F406 (= 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)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 19:486/496 of 4fr8C
- active site: N165 (= N152), K188 (= K175), Q264 (≠ E250), C298 (= C284), E395 (= E383), E472 (= E462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I148), I162 (≠ T149), W164 (= W151), K188 (= K175), G221 (= G208), G225 (= G212), A226 (≠ D213), F239 (= F226), G241 (= G228), S242 (= S229), I245 (≠ V232), Q345 (= Q331), E395 (= E383), F397 (= F385)
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)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 17:484/494 of 4kwfA
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E383), E470 (= E462)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F153), M168 (≠ I157), W171 (= W160), E262 (= E250), C295 (≠ R283), C296 (= C284), C297 (≠ T285), D451 (≠ H447), F453 (vs. gap), F459 (= F450)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
39% identity, 97% coverage: 10:476/481 of query aligns to 17:484/494 of 3sz9A
- active site: N163 (= N152), K186 (= K175), E262 (= E250), C296 (= C284), E393 (= E383), E470 (= E462)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F153), C295 (≠ R283), C296 (= C284), D451 (≠ H447), F453 (vs. gap), F459 (= F450)
Query Sequence
>Pf6N2E2_3298 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26)
VADSKRFDNYINGQWVAGADYCTNINPSDLSDVIGEYAKADAAQVNAAIEAARAAFPAWS
TSGIQARHDALDKVGSEILARREELGQLLAREEGKTLPEAIGEVTRAGNIFKFFAGECLR
LSGDYVPSVRPGVNVEVTREALGVVGLITPWNFPIAIPAWKIAPALAYGNCVVIKPAELV
PGCAWALAEIISRAGFPAGAFNLVMGSGRVVGDILVNSPKVDGISFTGSVGVGRQIAVNC
VSRQAKVQLEMGGKNPQIILDDADLKQAVELAVQSAFYSTGQRCTASSRLIVTAGIHDKF
VAAMAERMQSIKVGHALKAGTDIGPVVSEAQLSQDLKYIDIGQSEGARLVSGGGLVTCDT
EGYFLAPTLFADSEASMRISREEIFGPVANVVRVADYEAALAMANDTEFGLSAGIATTSL
KYANHFKRHSQAGMVMVNLPTAGVDYHVPFGGRKGSSYGSREQGRYAQEFYTVVKTSYIG
S
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