9IX8

Crystallization and structural characterization of phosphopentomutase from the hyperthermophilic archaeon Thermococcus kodakarensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004615	molecular_function	phosphomannomutase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0008966	molecular_function	phosphoglucosamine mutase activity
A	0008973	molecular_function	phosphopentomutase activity
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004615	molecular_function	phosphomannomutase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0008966	molecular_function	phosphoglucosamine mutase activity
B	0008973	molecular_function	phosphopentomutase activity
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004615	molecular_function	phosphomannomutase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0008966	molecular_function	phosphoglucosamine mutase activity
C	0008973	molecular_function	phosphopentomutase activity
C	0016853	molecular_function	isomerase activity
C	0016868	molecular_function	intramolecular phosphotransferase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004615	molecular_function	phosphomannomutase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0008966	molecular_function	phosphoglucosamine mutase activity
D	0008973	molecular_function	phosphopentomutase activity
D	0016853	molecular_function	isomerase activity
D	0016868	molecular_function	intramolecular phosphotransferase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00710
Number of Residues	10
Details	PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmITASHNP

Chain	Residue	Details
A	GLY87-PRO96

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"UniProtKB","id":"P31120","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"via phosphate group","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P31120","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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