SitesBLAST
Comparing RR42_RS31855 FitnessBrowser__Cup4G11:RR42_RS31855 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
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)
74% identity, 97% coverage: 3:296/303 of query aligns to 4:297/304 of Q79AF6
- C131 (= C130) active site, Acyl-thioester intermediate; mutation C->A,S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity.
- N170 (= N169) mutation N->A,D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
- I171 (= I170) 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 (= I194) 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 (= D207) 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)
60% identity, 96% coverage: 2:292/303 of query aligns to 3:297/303 of P9WQH3
- S41 (= S40) mutation to D: 2200-fold decrease in catalytic efficiency with coenzyme A.; mutation to I: 6600-fold decrease in catalytic efficiency with coenzyme A.
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
59% identity, 96% coverage: 1:290/303 of query aligns to 2:295/295 of 4lrtB
- binding coenzyme a: G11 (= G10), P12 (= P11), G13 (= G12), N14 (= N13), I15 (= I14), G36 (= G35), V37 (= V36), S41 (= S40), A75 (= A76), T76 (= T77), C127 (= C130), T163 (= T166), N277 (= N272), L278 (= L273)
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
59% identity, 95% coverage: 3:290/303 of query aligns to 2:293/294 of 4lrsB
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), P10 (= P11), G11 (= G12), N12 (= N13), I13 (= I14), V35 (= V36), A73 (= A76), T74 (= T77), L96 (= L99), T97 (= T100), C125 (= C130), G158 (= G163), P159 (= P164), G160 (= G165), T161 (= T166), N164 (= N169), N275 (= N272), L276 (= L273), M279 (= M276)
1nvmB Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
57% identity, 96% coverage: 3:293/303 of query aligns to 4:311/312 of 1nvmB
- binding nicotinamide-adenine-dinucleotide: I10 (= I9), G11 (= G10), S12 (≠ P11), G13 (= G12), N14 (= N13), I15 (= I14), G37 (= G35), I38 (≠ V36), A78 (= A76), T79 (= T77), L103 (= L99), T104 (= T100), C132 (= C130), G165 (= G163), P166 (= P164), G167 (= G165), T168 (= T166), N171 (= N169), N290 (= N272), L291 (= L273), M294 (= M276)
Q52060 Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. (strain CF600) (see paper)
57% identity, 96% coverage: 3:293/303 of query aligns to 4:311/312 of Q52060
- SGNI 12:15 (≠ PGNI 11:14) binding
- 163:171 (vs. 161:169, 78% identical) binding
- N290 (= N272) binding
Query Sequence
>RR42_RS31855 FitnessBrowser__Cup4G11:RR42_RS31855
MAKIKCALIGPGNIGTDLLYKLRRSTILEPVWMVGVDPASDGLARARELGLKTTDQGLDG
LLAHLAADDIRIAFDATSAYVHRQHSDQLTARGVRVIDLTPAAIGPFCVPPVNLDEHLGS
NAMNVNMVTCGGQATIPMVYAVSRVQAVAYGEIVATVSSRSVGPGTRRNIDEFTRTTAGA
IEQVGGARQGKAIIVINPAEPPLIMRDTIHCLTEDEPDVDAITASVHDMIAEVRQYVPGY
TLKNGPVFDGKRVSIFMEVEGLGDYLPRYAGNLDIMTAAAARTAERIGAAMLRGALPAMA
TTA
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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