3QKE

Crystal structure of D-mannonate dehydratase from Chromohalobacter Salexigens complexed with Mg and D-Gluconate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008927	molecular_function	mannonate dehydratase activity
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0047929	molecular_function	gluconate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0008927	molecular_function	mannonate dehydratase activity
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0047929	molecular_function	gluconate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0008927	molecular_function	mannonate dehydratase activity
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
C	0047929	molecular_function	gluconate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0008927	molecular_function	mannonate dehydratase activity
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
D	0047929	molecular_function	gluconate dehydratase activity
E	0000287	molecular_function	magnesium ion binding
E	0008927	molecular_function	mannonate dehydratase activity
E	0009063	biological_process	amino acid catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
E	0047929	molecular_function	gluconate dehydratase activity
F	0000287	molecular_function	magnesium ion binding
F	0008927	molecular_function	mannonate dehydratase activity
F	0009063	biological_process	amino acid catabolic process
F	0016052	biological_process	carbohydrate catabolic process
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding
F	0047929	molecular_function	gluconate dehydratase activity
G	0000287	molecular_function	magnesium ion binding
G	0008927	molecular_function	mannonate dehydratase activity
G	0009063	biological_process	amino acid catabolic process
G	0016052	biological_process	carbohydrate catabolic process
G	0016829	molecular_function	lyase activity
G	0046872	molecular_function	metal ion binding
G	0047929	molecular_function	gluconate dehydratase activity
H	0000287	molecular_function	magnesium ion binding
H	0008927	molecular_function	mannonate dehydratase activity
H	0009063	biological_process	amino acid catabolic process
H	0016052	biological_process	carbohydrate catabolic process
H	0016829	molecular_function	lyase activity
H	0046872	molecular_function	metal ion binding
H	0047929	molecular_function	gluconate dehydratase activity

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKaagmPLyqLLG

Chain	Residue	Details
A	ALA87-GLY112

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant P317A of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate.","authors":["Fedorov A.A.","Fedorov E.V.","Wichelecki D.","Gerlt J.A.","Almo S.C."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Site: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity"}

Chain

Residue

Details

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