SitesBLAST

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
52% identity, 88% coverage: 18:212/221 of query aligns to 7:201/210 of 6oviA

query
sites
6oviA

A

A

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binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E53), R46 (= R57), T70 (= T81), P91 (= P102), K130 (= K141), F132 (= F143)

1euaA Schiff base intermediate in kdpg aldolase from escherichia coli (see paper)
53% identity, 81% coverage: 34:213/221 of query aligns to 26:205/213 of 1euaA

query
sites
1euaA

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active site: E45 (= E53), R49 (= R57), K133 (= K141)
binding pyruvic acid: E45 (= E53), T73 (= T81), I92 (= I100), K133 (= K141)

P0A955 KHG/KDPG aldolase; (4S)-4-hydroxy-2-oxoglutarate aldolase; 2-dehydro-3-deoxy-phosphogluconate aldolase; 2-keto-3-deoxy-6-phosphogluconate aldolase; KDPG aldolase; 2-keto-4-hydroxyglutarate aldolase; KHG aldolase; Ketohydroxyglutarate aldolase; Entner-Douderoff aldolase; Oxaloacetate decarboxylase; Phospho-2-dehydro-3-deoxygluconate aldolase; Phospho-2-keto-3-deoxygluconate aldolase; EC 4.1.3.42; EC 4.1.2.14; EC 4.1.1.112 from Escherichia coli (strain K12) (see 5 papers)
53% identity, 81% coverage: 34:213/221 of query aligns to 26:205/213 of P0A955

query
sites
P0A955

L

L

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x
N

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x
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R

E45 (= E53) mutation to N: Aldolase activity is significantly impaired.
R49 (= R57) binding pyruvate
T73 (= T81) binding pyruvate
K133 (= K141) active site, Schiff-base intermediate with substrate; binding covalent; mutation to Q: Absence of aldolase activity. Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with K-161.
T161 (= T169) mutation to A: 13-fold decrease in catalytic efficiency with KDPG as substrate and 250-fold increase in catalytic efficiency with KDPGal as substrate.; mutation to K: Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with Q-133.; mutation to V: Shows little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. The change in specificity is accompanied by a very significant loss of activity against KDPG and a 5-fold increase in catalytic efficiency with KDPGal as substrate.
N168 (≠ T176) mutation to S: Shows activity significantly greater than wild-type.
S184 (≠ T192) mutation to A: 1.35-fold decrease in catalytic efficiency with KDPG as substrate. Has only a modest effect on the catalytic efficiency with KDG or KHO as substrate.; mutation to D: 300-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. Enhances the selectivity for reaction with KHO compared to KDPG by 780-fold.; mutation to L: 4-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. 40-fold increase in catalytic efficiency for the synthesis of KHPB, a precursor of nikkomycin, making this mutant a useful biocatalyst for the preparation of fine chemicals.

2c0aB Mechanism of the class i kdpg aldolase (see paper)
52% identity, 81% coverage: 34:213/221 of query aligns to 27:206/214 of 2c0aB

query
sites
2c0aB

L

L

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active site: N46 (≠ E53), R50 (= R57), K134 (= K141)
binding phosphate ion: E132 (= E139)

Sites not aligning to the query:

binding phosphate ion: 1, 5, 8, 9, 10

1wauA Structure of kdpg aldolase e45n mutant (see paper)
52% identity, 81% coverage: 34:213/221 of query aligns to 26:205/213 of 1wauA

query
sites
1wauA

L

L

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active site: N45 (≠ E53), R49 (= R57), K133 (= K141)
binding sulfate ion: G162 (= G170), G163 (= G171), S184 (≠ T192)

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
46% identity, 87% coverage: 21:212/221 of query aligns to 10:207/216 of 3vcrA

query
sites
3vcrA

Q

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P

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K

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A

active site: E42 (= E53), R46 (= R57), K136 (= K141)
binding pyruvic acid: R46 (= R57), T70 (= T81), V89 (≠ I100), S90 (≠ T101), P91 (= P102)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
44% identity, 90% coverage: 16:213/221 of query aligns to 5:198/209 of 5xsfA

query
sites
5xsfA

V

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N

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binding 3-hydroxypyruvic acid: V19 (≠ A30), E21 (≠ Q32), D22 (= D33), D25 (= D36)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
33% identity, 80% coverage: 15:190/221 of query aligns to 1:175/203 of 1wa3D

query
sites
1wa3D

R

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x
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-

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G

active site: E39 (= E53), T43 (≠ R57), K128 (= K141)
binding pyruvic acid: T68 (= T81), S88 (≠ T101), P89 (= P102), K128 (= K141), F130 (= F143)
binding sulfate ion: G157 (= G171)

Sites not aligning to the query:

binding sulfate ion: 177, 178

2v82A Kdpgal complexed to kdpgal (see paper)
26% identity, 73% coverage: 24:184/221 of query aligns to 7:168/205 of 2v82A

query
sites
2v82A

P

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G

active site: E36 (= E53), N40 (≠ R57), K125 (= K141)
binding 2-keto-deoxy-galactose: R13 (≠ A30), T65 (= T81), V84 (≠ I100), T85 (= T101), K125 (= K141), F127 (= F143), V153 (≠ T169)

Sites not aligning to the query:

binding 2-keto-deoxy-galactose: 175, 176, 205

Q6BF16 2-dehydro-3-deoxy-6-phosphogalactonate aldolase; 2-oxo-3-deoxygalactonate 6-phosphate aldolase; 6-phospho-2-dehydro-3-deoxygalactonate aldolase; 6-phospho-2-keto-3-deoxygalactonate aldolase; KDPGal aldolase; EC 4.1.2.21 from Escherichia coli (strain K12) (see paper)
26% identity, 73% coverage: 24:184/221 of query aligns to 8:169/205 of Q6BF16

query
sites
Q6BF16

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K

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G

E37 (= E53) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
K126 (= K141) active site, Schiff-base intermediate with substrate
V154 (≠ T169) mutation to T: Little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. Reduced the preference for KDPGal. It diminishes the activity against KDPGal and increases activity against KDPG.

Query Sequence

>GFF2223 FitnessBrowser__Marino:GFF2223
MEKTVSQLSDYHRERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEH
GLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAGAQFVITPGVTEAILEFGLTSEAPLL
PGIATISEMMIGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRNTAADY
LALGNVQAVGGTWLTPADLVAAKDWAQITEIARGSLADLAL

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