SitesBLAST
Comparing 15509 b1387 fused aldehyde dehydrogenase/enoyl-CoA hydratase (NCBI) 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)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:681/681 of query aligns to 1:681/681 of P77455
- E256 (= E256) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
100% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqoA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding crotonyl coenzyme a: V97 (= V98), F107 (= F108), S111 (= S112), F158 (= F159), W161 (= W162), R638 (= R639)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N155), F156 (= F157), N157 (= N158), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
100% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqnA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding octanoyl-coenzyme a: F562 (= F563), H565 (= H566), F576 (= F577), G583 (= G584), V595 (= V596), A604 (= A605), N605 (= N606), Y606 (= Y607), F613 (= F614), I614 (= I615)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (= R20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), K180 (= K181), A182 (= A183), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), L239 (= L240), E255 (= E256), A256 (= A257), D257 (= D258), C294 (= C295), F396 (= F397), H471 (= H472)
6jqmA Structure of paaz with NADPH (see paper)
100% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqmA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (= R20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), N157 (= N158), K180 (= K181), A182 (= A183), T183 (= T184), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295), E394 (= E395), F396 (= F397)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
43% identity, 69% coverage: 2:472/681 of query aligns to 4:484/521 of 2vroA
- active site: N160 (= N158), K183 (= K181), E258 (= E256), C297 (= C295), E401 (= E395)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), K183 (= K181), S217 (≠ A215), S235 (= S233), T238 (= T236), L242 (= L240), F403 (= F397)
Sites not aligning to the query:
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
43% identity, 69% coverage: 2:472/681 of query aligns to 4:483/529 of 2y53A
- active site: N160 (= N158), K183 (= K181), Q258 (≠ E256), C297 (= C295), E401 (= E395)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), N157 (= N155), F159 (= F157), N160 (= N158), K183 (= K181), A185 (= A183), T186 (= T184), S217 (≠ A215), F232 (= F230), G234 (= G232), S235 (= S233), A236 (= A234), T238 (= T236), A259 (= A257), D260 (= D258), C297 (= C295), F403 (= F397)
Sites not aligning to the query:
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)
25% identity, 74% coverage: 7:511/681 of query aligns to 21:505/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (= E256), C298 (= C295), E399 (= E395), E476 (= E483)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A156), K189 (= K181), E192 (≠ T184), G222 (≠ A215), G226 (= G216), G242 (= G232), G243 (≠ S233), T246 (= T236), H249 (≠ R241), I250 (≠ V242), C298 (= C295), E399 (= E395), F401 (= F397)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
26% identity, 56% coverage: 51:431/681 of query aligns to 34:404/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I154), L137 (≠ N155), F139 (= F157), K163 (= K181), S165 (≠ A183), I166 (≠ T184), S196 (≠ A215), G200 (≠ L219), G216 (= G232), S217 (= S233), T220 (= T236), I224 (≠ L240)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
26% identity, 56% coverage: 51:431/681 of query aligns to 34:404/466 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 (= I154), L137 (≠ N155), F139 (= F157), K163 (= K181), S165 (≠ A183), I166 (≠ T184), S196 (≠ A215), G200 (≠ L219), G216 (= G232), S217 (= S233), T220 (= T236), I224 (≠ L240), L239 (≠ A257), C272 (= C295), E368 (= E395), F370 (= F397)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
26% identity, 64% coverage: 63:499/681 of query aligns to 68:475/483 of 3b4wA
- active site: N154 (= N158), K177 (= K181), E251 (= E256), C285 (= C295), E384 (= E395), E460 (≠ A478)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ N155), W153 (≠ F157), N154 (= N158), K177 (= K181), I210 (vs. gap), G213 (= G216), T228 (= T231), G229 (= G232), S230 (= S233), V233 (≠ T236), E236 (≠ M239), E251 (= E256), L252 (≠ A257), C285 (= C295), E384 (= E395), F386 (= F397)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
26% identity, 65% coverage: 6:451/681 of query aligns to 12:439/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C295), E385 (= E395)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A156), W155 (≠ F157), K179 (= K181), A181 (= A183), S182 (≠ T184), A212 (= A215), G216 (≠ L219), G232 (= G232), S233 (= S233), I236 (≠ T236), C288 (= C295), K338 (≠ D345), E385 (= E395), F387 (= F397)
Sites not aligning to the query:
4ywuA Structural insight into the substrate inhibition mechanism of NADP+- dependent succinic semialdehyde dehydrogenase from streptococcus pyogenes (see paper)
25% identity, 62% coverage: 63:487/681 of query aligns to 46:440/455 of 4ywuA
- active site: N131 (= N158), K154 (= K181), E228 (= E256), C262 (= C295), E359 (= E395), E436 (= E483)
- binding 4-oxobutanoic acid: N131 (= N158), Q136 (≠ G163), R139 (≠ E166), E228 (= E256), V261 (≠ K294), C262 (= C295), F425 (≠ H472)
4ohtA Crystal structure of succinic semialdehyde dehydrogenase from streptococcus pyogenes in complex with NADP+ as the cofactor (see paper)
25% identity, 62% coverage: 63:487/681 of query aligns to 46:440/455 of 4ohtA
- active site: N131 (= N158), K154 (= K181), E228 (= E256), C262 (= C295), E359 (= E395), E436 (= E483)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V127 (≠ I154), E128 (≠ N155), P129 (≠ A156), W130 (≠ F157), K154 (= K181), H155 (≠ P182), A156 (= A183), S157 (≠ T184), Y187 (≠ A215), S207 (= S233), I214 (≠ L240)
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)
26% identity, 65% coverage: 6:451/681 of query aligns to 13:440/482 of P25526
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
27% identity, 51% coverage: 149:496/681 of query aligns to 152:484/498 of 4pxnA
- active site: N161 (= N158), K184 (= K181), E262 (= E256), C296 (= C295), E392 (= E395), E472 (= E483)
- binding nicotinamide-adenine-dinucleotide: I157 (= I154), T158 (≠ N155), A159 (= A156), F160 (= F157), N161 (= N158), K184 (= K181), T221 (≠ D217), G224 (≠ D220), Q225 (≠ H221), F238 (= F230), T239 (= T231), G240 (= G232), S241 (= S233), A244 (≠ T236), V248 (= V242), E262 (= E256), L263 (≠ A257), S264 (≠ D258), C296 (= C295), E392 (= E395), F394 (= F397), F461 (≠ H472)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
27% identity, 44% coverage: 135:434/681 of query aligns to 124:420/494 of 5izdA
- active site: N149 (= N158), K172 (= K181), E247 (= E256), C281 (= C295), E381 (= E395)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I154), T146 (≠ N155), W148 (≠ F157), K172 (= K181), P173 (= P182), S174 (≠ A183), S175 (≠ T184), R204 (≠ S214), G205 (≠ A215), G209 (≠ L219), D210 (= D220), G225 (= G232), S226 (= S233), T229 (= T236)
Sites not aligning to the query:
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
26% identity, 58% coverage: 48:439/681 of query aligns to 50:425/477 of 2opxA
- active site: N151 (= N158), K174 (= K181), E249 (≠ V264), C283 (= C295), E381 (= E395)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ I104), F152 (= F159), N284 (≠ T296), F312 (≠ V324), G313 (= G325), R318 (≠ E330), D320 (vs. gap), I321 (≠ V332), A322 (≠ K333), Y362 (≠ F374)
Sites not aligning to the query:
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
26% identity, 58% coverage: 48:439/681 of query aligns to 52:427/479 of P25553
- L150 (≠ N155) binding
- R161 (≠ E166) binding
- KPSE 176:179 (≠ KPAT 181:184) binding
- F180 (≠ A185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D217) binding
- S230 (= S233) binding
- E251 (≠ V264) binding
- N286 (≠ T296) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ D345) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
26% identity, 58% coverage: 48:439/681 of query aligns to 50:425/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (≠ V264), C283 (= C295), E381 (= E395)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ N155), P149 (≠ A156), W150 (≠ F157), K174 (= K181), E177 (≠ T184), F178 (≠ A185), G207 (vs. gap), G211 (= G216), Q212 (≠ D217), S228 (= S233), A231 (≠ T236), K234 (≠ M239), R334 (≠ D345)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
26% identity, 58% coverage: 48:439/681 of query aligns to 50:425/477 of 2iluA
- active site: N151 (= N158), K174 (= K181), E249 (≠ V264), C283 (= C295), E381 (= E395)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), L148 (≠ N155), P149 (≠ A156), W150 (≠ F157), K174 (= K181), S176 (≠ A183), E177 (≠ T184), R206 (vs. gap), G207 (vs. gap), G211 (= G216), Q212 (≠ D217), S228 (= S233), A231 (≠ T236), K234 (≠ M239), I235 (≠ L240), N328 (= N339), R334 (≠ D345), F383 (= F397)
Sites not aligning to the query:
Query Sequence
>15509 b1387 fused aldehyde dehydrogenase/enoyl-CoA hydratase (NCBI)
MQQLASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARQFAIEKGAPALRAMT
FIERAAMLKAVAKHLLSEKERFYALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPD
DTLWPEDELIPLSKEGGFAARHLLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAII
KPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQML
RVQPNIVAKSIPFTMEADSLNCCVLGEDVTPDQPEFALFIREVVREMTTKAGQKCTAIRR
IIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNILLAAGCEI
RLGGQADLSAAGAFFPPTLLYCPQPDETPAVHATEAFGPVATLMPAQNQRHALQLACAGG
GSLAGTLVTADPQIARQFIADAARTHGRIQILNEESAKESTGHGSPLPQLVHGGPGRAGG
GEELGGLRAVKHYMQRTAVQGSPTMLAAISKQWVRGAKVEEDRIHPFRKYFEELQPGDSL
LTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGV
GPVIANYGLESLRFIEPVKPGDTIQVRLTCKRKTLKKQRSAEEKPTGVVEWAVEVFNQHQ
TPVALYSILTLVARQHGDFVD
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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