SitesBLAST
Comparing RR42_RS35145 FitnessBrowser__Cup4G11:RR42_RS35145 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)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
66% identity, 97% coverage: 1:501/514 of query aligns to 2:508/521 of 2vroA
- active site: N160 (= N159), K183 (= K182), E258 (= E257), C297 (= C296), E401 (= E400), L496 (= L489)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I155), K183 (= K182), S217 (≠ A216), S235 (= S234), T238 (= T237), L242 (≠ I241), F403 (= F402)
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
66% identity, 97% coverage: 1:501/514 of query aligns to 2:507/529 of 2y53A
- active site: N160 (= N159), K183 (= K182), Q258 (≠ E257), C297 (= C296), E401 (= E400), L495 (= L489)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I155), N157 (= N156), F159 (= F158), N160 (= N159), K183 (= K182), A185 (= A184), T186 (= T185), S217 (≠ A216), F232 (= F231), G234 (= G233), S235 (= S234), A236 (= A235), T238 (= T237), A259 (= A258), D260 (= D259), C297 (= C296), F403 (= F402)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
46% identity, 99% coverage: 5:514/514 of query aligns to 4:509/681 of P77455
- E256 (= E257) 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)
46% identity, 99% coverage: 5:512/514 of query aligns to 3:506/678 of 6jqoA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L489)
- binding crotonyl coenzyme a: V97 (= V100), F107 (≠ G110), S111 (≠ K114), F158 (= F160), W161 (= W163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N156), F156 (= F158), N157 (= N159), T183 (= T185), T230 (= T232), G231 (= G233), S232 (= S234), T235 (= T237), A256 (= A258), D257 (= D259), C294 (= C296)
Sites not aligning to the query:
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
46% identity, 99% coverage: 5:512/514 of query aligns to 3:506/678 of 6jqnA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L489)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ A21), I153 (= I155), N154 (= N156), A155 (= A157), F156 (= F158), K180 (= K182), A182 (= A184), T183 (= T185), T230 (= T232), G231 (= G233), S232 (= S234), T235 (= T237), L239 (≠ I241), E255 (= E257), A256 (= A258), D257 (= D259), C294 (= C296), F396 (= F402), H471 (= H477)
Sites not aligning to the query:
6jqmA Structure of paaz with NADPH (see paper)
46% identity, 99% coverage: 5:512/514 of query aligns to 3:506/678 of 6jqmA
- active site: N157 (= N159), E255 (= E257), C294 (= C296), L483 (= L489)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ A21), I153 (= I155), N154 (= N156), A155 (= A157), F156 (= F158), N157 (= N159), K180 (= K182), A182 (= A184), T183 (= T185), G231 (= G233), S232 (= S234), T235 (= T237), A256 (= A258), D257 (= D259), C294 (= C296), E394 (= E400), F396 (= F402)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
28% identity, 97% coverage: 8:505/514 of query aligns to 10:480/490 of Q9HTJ1
- GAWN 150:153 (≠ NAFN 156:159) binding
- K162 (= K168) active site, Charge relay system
- KPSE 176:179 (≠ KPAT 182:185) binding
- G209 (≠ A216) binding
- GTST 230:233 (≠ SAQT 234:237) binding
- E252 (= E257) active site, Proton acceptor
- C286 (= C296) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E400) binding
- E464 (= E488) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
28% identity, 97% coverage: 8:505/514 of query aligns to 9:479/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E488)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I155), G149 (≠ N156), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (≠ T185), G208 (≠ A216), G212 (vs. gap), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ I241), E251 (= E257), L252 (≠ A258), C285 (= C296), E386 (= E400), F388 (= F402)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
28% identity, 97% coverage: 8:505/514 of query aligns to 9:479/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E488)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ N156), W151 (≠ F158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (≠ T185), G208 (≠ A216), G212 (vs. gap), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ I241), E251 (= E257), L252 (≠ A258), C285 (= C296), E386 (= E400), F388 (= F402)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
28% identity, 97% coverage: 8:505/514 of query aligns to 9:479/489 of 2wmeA
- active site: N152 (= N159), K175 (= K182), E251 (= E257), C285 (= C296), E386 (= E400), E463 (= E488)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ N156), W151 (≠ F158), K175 (= K182), S177 (≠ A184), E178 (≠ T185), G208 (≠ A216), G212 (vs. gap), F226 (= F231), G228 (= G233), G229 (≠ S234), T232 (= T237), V236 (≠ I241)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
29% identity, 96% coverage: 15:505/514 of query aligns to 17:478/489 of 6wsbA
- active site: N152 (= N159), E250 (= E257), C284 (= C296), E462 (= E488)
- binding nicotinamide-adenine-dinucleotide: I148 (= I155), G149 (≠ N156), A150 (= A157), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (≠ T185), G208 (vs. gap), G211 (≠ A217), A212 (≠ G218), F225 (= F231), T226 (= T232), G227 (= G233), G228 (≠ S234), T231 (= T237), V235 (≠ I241), E250 (= E257), L251 (≠ A258), G252 (≠ D259), C284 (= C296), E385 (= E400), F387 (= F402)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
26% identity, 83% coverage: 9:436/514 of query aligns to 14:421/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (≠ N255), C288 (= C296), E385 (= E400)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A157), W155 (≠ F158), K179 (= K182), A181 (= A184), S182 (≠ T185), A212 (= A216), G216 (≠ L220), G232 (= G233), S233 (= S234), I236 (≠ T237), C288 (= C296), K338 (≠ S346), E385 (= E400), F387 (= F402)
Sites not aligning to the query:
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, 83% coverage: 9:436/514 of query aligns to 15:422/482 of P25526
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
25% identity, 86% coverage: 1:444/514 of query aligns to 2:424/454 of 3ty7B
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 86% coverage: 1:440/514 of query aligns to 19:439/501 of Q56YU0
- G152 (≠ Q140) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A417) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
24% identity, 90% coverage: 42:505/514 of query aligns to 52:484/497 of P17202
- D96 (≠ N90) binding
- SPW 156:158 (≠ NAF 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAT 182:185) binding
- L186 (≠ A186) binding
- SSAT 236:239 (≠ SAQT 234:237) binding
- V251 (≠ Q249) binding in other chain
- L258 (≠ I256) binding
- W285 (vs. gap) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E400) binding
- A441 (≠ H451) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ V471) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H477) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G481) binding
Sites not aligning to the query:
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
27% identity, 96% coverage: 3:494/514 of query aligns to 36:504/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
25% identity, 77% coverage: 52:447/514 of query aligns to 34:415/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I155), L137 (≠ N156), F139 (= F158), K163 (= K182), S165 (≠ A184), I166 (≠ T185), S196 (≠ A216), G200 (≠ L220), G216 (= G233), S217 (= S234), T220 (= T237), I224 (= I241)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
25% identity, 77% coverage: 52:447/514 of query aligns to 34:415/466 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 (= I155), L137 (≠ N156), F139 (= F158), K163 (= K182), S165 (≠ A184), I166 (≠ T185), S196 (≠ A216), G200 (≠ L220), G216 (= G233), S217 (= S234), T220 (= T237), I224 (= I241), L239 (≠ A258), C272 (= C296), E368 (= E400), F370 (= F402)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
24% identity, 90% coverage: 42:505/514 of query aligns to 50:482/495 of 4v37A
- active site: N157 (= N159), K180 (= K182), E255 (≠ N255), A289 (≠ C296), E388 (= E400), E465 (= E488)
- binding 3-aminopropan-1-ol: C448 (≠ V471), W454 (≠ H477)
- binding nicotinamide-adenine-dinucleotide: I153 (= I155), S154 (≠ N156), P155 (≠ A157), W156 (≠ F158), N157 (= N159), M162 (vs. gap), K180 (= K182), S182 (≠ A184), E183 (≠ T185), G213 (vs. gap), G217 (≠ A217), A218 (≠ G218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (= T237), E255 (≠ N255), L256 (≠ I256), A289 (≠ C296), E388 (= E400), F390 (= F402)
Query Sequence
>RR42_RS35145 FitnessBrowser__Cup4G11:RR42_RS35145
MTELLSNYLGGRWQAGSGAGATLSDPVLGDALVRVDATGLDLAAGFAFAREQGGAALRAM
TYRERAAMLAAIVKILQTNRDAYYEIATANSGTVHNDSAVDIDGGIFTLGTYAKLGDALG
ERRYLIDGDAARLGKDPLFQSQHVLVPTRGVALLINAFNFPSWGLWEKAAPALLAGVPVI
VKPATATAWLTQRMVRDVVDAGVLPPGALSVVCGSAAGLLDQLQPFDVVSFTGSAQTAAL
IRSHAAVTQRSVRVNIEADSVNSALLLPGEAAGSEAFDLLAKEAAREMTVKSGQKCTAIR
RIFVPEALYGAAADAIGARLARVTVGNPRHEAVRMGALVSRAQLASVREGLGYLQAQAEV
LHDGATHALVDADPAVACCVGPTLLGARDAHAADRVHDTEVFGPVATLVPYRDNADALAL
VRRGQGSLVASLYGSDADALAKAAVELADSHGRVHVISPDVAQLHTGHGNVMPQSLHGGP
GRAGGGEELGGLRALNFYHRRSAVQASTSVLAQL
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