SitesBLAST
Comparing 6937537 Sama_1693 bifunctional acetaldehyde-CoA/alcohol dehydrogenase (RefSeq) 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)
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)
77% identity, 100% coverage: 1:863/867 of query aligns to 1:867/891 of P0A9Q7
- M1 (= M1) modified: Initiator methionine, Removed
- IVPTTN 110:115 (= IVPTTN 110:115) binding
- G195 (= G195) binding
- G213 (= G213) binding
- A267 (≠ S267) 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)
77% identity, 100% coverage: 1:863/867 of query aligns to 1:867/891 of P0A9Q8
7bvpA Adhe spirosome in extended conformation (see paper)
77% identity, 100% coverage: 1:863/867 of query aligns to 1:867/869 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)
77% identity, 100% coverage: 1:863/867 of query aligns to 1:867/869 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)
71% identity, 48% coverage: 450:863/867 of query aligns to 1:404/406 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)
53% identity, 47% coverage: 450:860/867 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)
47% identity, 51% coverage: 7:445/867 of query aligns to 13:446/456 of 5j7iB
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
47% identity, 51% coverage: 7:445/867 of query aligns to 12:445/455 of 5j7iC
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
39% identity, 50% coverage: 9:440/867 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)
39% identity, 50% coverage: 9:440/867 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)
39% identity, 50% coverage: 9:440/867 of query aligns to 3:428/449 of 8cejA
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
36% identity, 47% coverage: 451:859/867 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)
35% identity, 47% coverage: 451:860/867 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)
35% identity, 47% coverage: 451:860/867 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)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
36% identity, 46% coverage: 464:858/867 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, 46% coverage: 464:858/867 of query aligns to 15:382/382 of 3owoA
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, 46% coverage: 464:858/867 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
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
36% identity, 47% coverage: 451:858/867 of query aligns to 2:382/382 of 3bfjA
4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
33% identity, 45% coverage: 8:400/867 of query aligns to 7:390/435 of 4c3sA
- active site: T110 (= T114), A208 (≠ V212), C242 (= C246)
- binding nicotinamide-adenine-dinucleotide: I106 (= I110), T107 (≠ V111), P108 (= P112), C109 (≠ T113), H135 (= H139), L171 (≠ V175), T189 (= T193), G190 (= G194), G191 (= G195), V194 (≠ M198), A208 (≠ V212), G209 (= G213), C242 (= C246), E330 (= E335), M332 (≠ L337), H360 (= H367)
Sites not aligning to the query:
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
35% identity, 44% coverage: 476:858/867 of query aligns to 28:381/381 of P31005
- D88 (= D536) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G543) mutation to A: Shows a 10-fold decreased affinity for NAD and NADH and a strongly reduced dehydrogenase activity. Completely insensitive to the stimulating effect of the activator protein Act.
- S97 (= S545) mutation to G: Shows an increase of the dehydrogenase activity and a decrease of the affinity for NAD and NADH. Completely insensitive to the stimulating effect of the activator protein Act. It does not bind NAD.; mutation to T: Shows an increase of the dehydrogenase activity and affinity for NAD and NADH.
- D100 (= D548) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K551) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 13 G→A: Shows a reduced dehydrogenase activity.
- 15 G→A: Shows almost the same dehydrogenase activity as the wild-type.
Query Sequence
>6937537 Sama_1693 bifunctional acetaldehyde-CoA/alcohol dehydrogenase (RefSeq)
MTVTNTQELNELVARVAKAQAQFASYSQEQVDRIFRAAALAAADARIRLAKMAAEETRMG
VVEDKVIKNHFASEYIYNKYKDEKTCGILAEDATFGTITIAEPVGIICGIVPTTNPTSTA
IFKALISLKTRNGIIFSPHPRAKVSTTTAARIVLDAAIAAGAPKDIIGWIDEPSVALSNQ
LMTHEKINLILATGGPGMVKAAYSSGKPAIGVGAGNTPIVIDETADIKRAVSSILMSKTF
DNGVVCASEQAVVVVDAVYDAVKERFSSHGGYLLSKKENAALQKVILKDGGLNADIVGQS
AATIAAMANIKVPAHTKVLIGEVTDIDEKEAFAHEKLSPLLGMYRAANFEEALDKAEALV
ALGGIGHTSGLYTDQDTQDERVKSFGYRMKTARILINTPASQGGIGDLYNFKLAPSLTLG
CGSWGGNSISENVGPSHLINKKTVAKRAENMLWHKLPSSIYFRRGSLPIALEELSGKKRA
LIVTDKFLFNNGYCDETIRILKSQGLETEVFYEVEADPTLAVVRAGAKVATSFQPDVIVA
LGGGSPMDAAKIIWVMYEHPDVDFADLALRFMDIRKRIYKFPKLGAKAMMVAIPTTSGTG
SEVTPFAVVTDEQTGAKYPIADYELTPNMAIVDPNLVMDMPKSLTAFGGIDAITHALEAY
VSVMANEYSDGQALQALDLLFKYLPDSYARGAQAPLAREKVHNGATIAGIAFANAFLGIC
HSMAHKLGAEFHLPHGLANALLISNVIRFNATDLPTKQAAFSQYDRPKALCRYAAIASHL
GLAGNNDEAKVEALIAKIEELKAAIGIPVSIKDAGVNEADFMAKLDELAEDAFDDQCTGA
NPRYPLISELKQLLIDSFHGRAYQDSL
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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