SitesBLAST

Q79AF6 Acetaldehyde dehydrogenase 4; Acetaldehyde dehydrogenase [acetylating] 4; Propanal dehydrogenase (CoA-propanoylating); EC 1.2.1.10; EC 1.2.1.87 from Paraburkholderia xenovorans (strain LB400) (see 2 papers)
57% identity, 100% coverage: 1:310/311 of query aligns to 1:293/304 of Q79AF6

query
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Q79AF6

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C131 (= C132) active site, Acyl-thioester intermediate; mutation C->A,S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity.
N170 (= N171) mutation N->A,D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I171 (= I172) mutation I->A,F: Exhibits preferences for aldehydes similar as wild-type. Exhibits about 80% of wild-type acetaldehyde channeling efficiency. Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I195 (= I196) mutation to A: 5-fold decrease in affinity for acetaldehyde. Increase in affinity for butyraldehyde and pentaldehyde, leading to a 9- and 20-fold increase in catalytic efficiency with butyraldehyde and pentaldehyde as substrate, respectively. Exhibits 84% of wild-type acetaldehyde channeling efficiency.; mutation to F: 4- to 7-fold decrease in catalytic efficiency with aldehydes three to four carbons in length. Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde.; mutation to L: Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde.; mutation to W: 5- to 16-fold decrease in catalytic efficiency with aldehydes two to four carbons in length. Exhibits 59% of wild-type acetaldehyde channeling efficiency.
D208 (= D209) mutation to A: 2-fold decrease in catalytic efficiency.

P9WQH3 Propanal dehydrogenase (CoA-propanoylating); Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.87; EC 1.2.1.10 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
54% identity, 100% coverage: 1:310/311 of query aligns to 1:298/303 of P9WQH3

query
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P9WQH3

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S41 (= S42) mutation to D: 2200-fold decrease in catalytic efficiency with coenzyme A.; mutation to I: 6600-fold decrease in catalytic efficiency with coenzyme A.

4lrsB Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
55% identity, 98% coverage: 4:308/311 of query aligns to 2:293/294 of 4lrsB

query
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4lrsB

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binding nicotinamide-adenine-dinucleotide: G9 (= G11), P10 (≠ S12), G11 (= G13), N12 (= N14), I13 (= I15), V35 (≠ I38), A73 (= A78), T74 (= T79), L96 (≠ M103), T97 (= T104), C125 (= C132), G158 (= G165), P159 (= P166), G160 (= G167), T161 (= T168), N164 (= N171), N275 (= N290), L276 (= L291), M279 (= M294)

4lrtB Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
55% identity, 98% coverage: 4:308/311 of query aligns to 4:295/295 of 4lrtB

query
sites
4lrtB

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M

T

T

S

A

A

A

L

A

G

R

T

V

A

G

E

E

R

L

I

L

A

A

E

Q

S

A

binding coenzyme a: G11 (= G11), P12 (≠ S12), G13 (= G13), N14 (= N14), I15 (= I15), G36 (= G37), V37 (≠ I38), S41 (= S42), A75 (= A78), T76 (= T79), C127 (= C132), T163 (= T168), N277 (= N290), L278 (= L291)

Query Sequence

>GFF4095 HP15_4035 acetaldehyde dehydrogenase
MSKKIKAAIIGSGNIGTDLMIKILRNGKNIEMGAMVGIDPESDGLARAARMGVATTHEGV
DGLVKMPEFADIDIVFDATSAKAHMHNEVFLRGHKESIKIIDMTPAAIGPYCVPVVNLEQ
QLQEGNVNMVTCGGQATIPMVAAVSRVAKAHYAEIVASISSKSAGPGTRANIDEFTQTTS
RAIEVVGGAQKGKAIIILNPAEPPLLMRDTVYVLSDAADKAEVEASVEEMVQAVNSYVPG
YRLKQKVQFDDIPEDQPMNVPGLGRFSGLKTSIFLEVEGAAHYLPAYAGNLDIMTSAALG
TAERIAESLVN

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