SitesBLAST
Comparing AZOBR_RS32240 AZOBR_RS32240 acetaldehyde dehydrogenase 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)
P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 8 papers)
75% identity, 98% coverage: 1:866/886 of query aligns to 1:870/891 of P0A9Q7
- M1 (= M1) modified: Initiator methionine, Removed
- IVPTTN 110:115 (= IVPTTN 110:115) binding
- G195 (= G195) binding
- G213 (= G213) binding
- A267 (= A267) mutation to T: Shows aerobic growth ability on ethanol. Shows 5-6 fold increase in acetaldehyde dehydrogenase activity, but does not affect ethanol dehydrogenase activity. Shows decreased thermal enzyme stability and increased sensitivity to MCO damage. Shows increased protein stability and resistance to MCO; when associated with K-568.
- E335 (= E335) binding
- K358 (≠ A358) modified: N6-acetyllysine
- L419 (= L419) binding
- KRAE 446:449 (= KRAE 446:449) mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
- D487 (= D485) binding
- D519 (= D517) binding
- GSPMD 546:550 (= GSPMD 544:548) binding
- E568 (≠ D566) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V608) binding
- K619 (= K617) binding
- D653 (= D651) binding
- H657 (= H655) binding
- F670 (≠ Y668) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H721) binding
- H737 (= H735) binding
P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see paper)
75% identity, 98% coverage: 1:866/886 of query aligns to 1:870/891 of P0A9Q8
7bvpA Adhe spirosome in extended conformation (see paper)
75% identity, 98% coverage: 1:865/886 of query aligns to 1:869/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P112), T113 (= T113), H139 (= H139), G194 (= G194), G195 (= G195), M198 (= M198), V212 (= V212), G213 (= G213), A214 (= A214), C246 (= C246), E335 (= E335), L337 (= L337), H367 (= H367), T418 (= T418), L419 (= L419), D487 (= D485), F489 (= F487), D519 (= D517), S547 (= S545), D550 (= D548), T597 (= T595), T598 (= T596), T601 (= T599), V610 (= V608), K619 (= K617), L646 (= L644), H737 (= H735)
- binding zinc ion: D653 (= D651), H657 (= H655), H723 (= H721), H737 (= H735)
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
75% identity, 98% coverage: 1:865/886 of query aligns to 1:869/869 of 6tqmA
- binding fe (iii) ion: D653 (= D651), H657 (= H655), H723 (= H721), H737 (= H735)
- 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: D487 (= D485), L490 (= L488), G545 (= G543), S547 (= S545), D550 (= D548), T597 (= T595), S603 (= S601), F608 (= F606), L646 (= L644), H727 (= H725)
6scgA Structure of adhe form 1 (see paper)
69% identity, 47% coverage: 450:865/886 of query aligns to 1:406/406 of 6scgA
- binding fe (iii) ion: D204 (= D651), H208 (= H655), H274 (= H721), H288 (= H735)
- binding nicotinamide-adenine-dinucleotide: D38 (= D485), F40 (= F487), A69 (= A516), D70 (= D517), G96 (= G543), G97 (= G544), S98 (= S545), T148 (= T595), T149 (= T596), T152 (= T599), V161 (= V608), L197 (= L644), H278 (= H725)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
52% identity, 46% coverage: 450:860/886 of query aligns to 1:402/403 of 3zdrA
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
44% identity, 50% coverage: 5:445/886 of query aligns to 11:446/456 of 5j7iB
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
44% identity, 50% coverage: 5:445/886 of query aligns to 10:445/455 of 5j7iC
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
37% identity, 49% coverage: 9:440/886 of query aligns to 3:428/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P112), I107 (≠ T113), H133 (= H139), P134 (= P140), T185 (= T193), G186 (= G194), G187 (= G195), R190 (≠ M198), V204 (= V212), C238 (= C246), E328 (= E335), L407 (= L419)
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
37% identity, 49% coverage: 9:440/886 of query aligns to 3:428/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (≠ A72), P106 (= P112), T108 (= T114), N109 (= N115), A131 (≠ S137), P132 (= P138), H133 (= H139), P134 (= P140), R169 (≠ V175), G189 (= G197), R190 (≠ M198), I237 (≠ V245), C238 (= C246), S239 (≠ A247), T391 (≠ S401), G394 (= G406), T405 (≠ L417), L407 (= L419)
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
37% identity, 49% coverage: 9:440/886 of query aligns to 3:428/449 of 8cejA
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
35% identity, 46% coverage: 451:859/886 of query aligns to 1:377/378 of A0A0S1X9S7
- D195 (= D651) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H655) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H721) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (= H725) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H735) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
6c75B Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
34% identity, 46% coverage: 451:860/886 of query aligns to 1:377/378 of 6c75B
6c75A Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
34% identity, 46% coverage: 451:860/886 of query aligns to 1:377/378 of 6c75A
- binding fe (iii) ion: D193 (= D651), H197 (= H655), H260 (= H721), H272 (= H735)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S33 (≠ D485), S35 (≠ F487), G91 (= G543), G92 (= G544), S93 (= S545), D96 (= D548), S139 (≠ T595), T140 (= T596), A143 (≠ T599), S148 (≠ T604), V152 (= V608), K159 (= K617), T181 (≠ D639), M182 (= M640), P183 (= P641), V186 (≠ L644), F251 (= F712), H272 (= H735)
P0DJA2 Alcohol dehydrogenase 2; Alcohol dehydrogenase II; ADH II; EC 1.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
36% identity, 45% coverage: 464:858/886 of query aligns to 16:383/383 of P0DJA2
- D39 (= D485) binding
- N71 (≠ D517) binding
- G98 (= G544) binding
- S99 (= S545) binding
- T138 (= T595) binding
- T139 (= T596) binding
- T147 (= T604) binding
- F149 (= F606) binding
- K160 (= K617) binding
- L179 (= L636) binding
- G182 (≠ D639) binding
- M183 (= M640) binding
- D194 (= D651) binding
- H198 (= H655) binding
- H263 (= H721) binding
- H267 (= H725) binding
- H277 (= H735) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
36% identity, 45% coverage: 464:858/886 of query aligns to 15:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D651), H197 (= H655), H262 (= H721), H276 (= H735)
- binding nicotinamide-adenine-dinucleotide: D38 (= D485), F40 (= F487), M41 (≠ L488), N70 (≠ D517), G96 (= G543), G97 (= G544), S98 (= S545), T137 (= T595), T138 (= T596), F148 (= F606), I150 (≠ V608), G181 (≠ D639), M182 (= M640), L186 (= L644), H276 (= H735)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
36% identity, 45% coverage: 464:858/886 of query aligns to 15:382/382 of 3owoA
1rrmA Crystal structure of lactaldehyde reductase
34% identity, 46% coverage: 456:860/886 of query aligns to 7:384/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D485), T40 (≠ F487), L41 (= L488), N70 (≠ D517), G96 (= G543), G97 (= G544), S98 (= S545), T139 (= T595), T140 (= T596), T143 (= T599), V152 (= V608), K161 (= K617), G183 (≠ D639), M184 (= M640), L188 (= L644), H276 (= H735)
- binding fe (ii) ion: L258 (= L717), C361 (= C837)
- binding zinc ion: D195 (= D651), H199 (= H655), H262 (= H721), H276 (= H735)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
34% identity, 45% coverage: 456:853/886 of query aligns to 7:377/382 of 2bi4A
- binding fe (iii) ion: D195 (= D651), H199 (= H655), H262 (= H721), H276 (= H735)
- binding nicotinamide-adenine-dinucleotide: D38 (= D485), T40 (≠ F487), L41 (= L488), G96 (= G543), G97 (= G544), S98 (= S545), T139 (= T595), T140 (= T596), V152 (= V608), K161 (= K617), G183 (≠ D639), M184 (= M640), L188 (= L644), D195 (= D651), H199 (= H655), H262 (= H721), H276 (= H735)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
34% identity, 45% coverage: 456:853/886 of query aligns to 7:377/382 of P0A9S1
- G16 (= G465) mutation to D: No effect on enzyme activity.
- D38 (= D485) mutation to G: Enzyme can now use NADP.
- G96 (= G543) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D651) mutation to L: Complete loss of iron-binding.
- H199 (= H655) mutation H->A,F: Complete loss of iron-binding.
Sites not aligning to the query:
- 1:9 MANRMILNE→M: Loss of enzyme activity, loss of dimerization.
Query Sequence
>AZOBR_RS32240 AZOBR_RS32240 acetaldehyde dehydrogenase
MPVTTLADLNDLVLRVREAQKVYAGFPQETVDRIFRSAALAAANARIPLAKLAVAETRMG
VMEDKVVKNHFASEYIYNKYKDEKTCGILEEDPEYGIMTIAEPVGLICAIVPTTNPTSTA
IFKALISLKTRNGIVFSPHPRARKATCEAARIVLQAAVEAGAPADIIGWIDEPSVDLSNA
VMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPAVIDEFADIKRAVASILMSKTF
DNGVVCASEQSAIVVDAVYDAVRDRFAHHGGHILSGTDADAVRKVLLKNGALNADIVGQS
AGAIAAMAGVSVPANTKVLIAEVEAVTEDEPFAHEKLSPTLALYRARDFMDACDKAAALV
ALGGIGHTSALYTDQDQQPERIRHFGQAMKTARILINTPSSQGGIGDLYNFRLAPSLTLG
CGSWGGNSISENVGPQHLINRKTVAKRAENMLWHKLPKSIYFRRGCLPFALEELRGKKRC
LIVTDRFLFENGHVDETVRILKGLGLAVETFFEVAADPTLAVVRRGLALANAFQPDVILA
LGGGSPMDAAKIMWVMYEAPDVAFEDLALRFMDIRKRIYTFPKLGVKAQFVAVPTTSGTG
SEVTPFAVVTDERTGIKYPIADYELTPNMAIIDANLVMDMPKGLTAAGGIDAVTHALEAY
VSVLANEYTDGQALQALKLLKEHLPSAYANGGKDPKAREQVHSAATLAGIAFANAFLGVC
HSMAHKLGAEFHLPHGVANALLIANVIRYNAADIPTKQTAFSQYDRPKGVARYAEIARHL
GLGGSRDHERVETLVAWVEELKRTLDIPASIQAAGVPEAEFLARLDAIAEAAFDDQCTGA
NPRFPLVAEIRQLLLDSYYGRAYAEGAEREPDAKAERKPVALVRSR
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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