1UJQ

Crystal structure of 2-methylisocitrate lyase (PrpB) from Salmonella enterica serovar typhimurium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0016833	molecular_function	oxo-acid-lyase activity
A	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
A	0046421	molecular_function	methylisocitrate lyase activity
A	0046872	molecular_function	metal ion binding
A	0140677	molecular_function	molecular function activator activity
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0016833	molecular_function	oxo-acid-lyase activity
B	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
B	0046421	molecular_function	methylisocitrate lyase activity
B	0046872	molecular_function	metal ion binding
B	0140677	molecular_function	molecular function activator activity
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0016833	molecular_function	oxo-acid-lyase activity
C	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
C	0046421	molecular_function	methylisocitrate lyase activity
C	0046872	molecular_function	metal ion binding
C	0140677	molecular_function	molecular function activator activity
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0016829	molecular_function	lyase activity
D	0016833	molecular_function	oxo-acid-lyase activity
D	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
D	0046421	molecular_function	methylisocitrate lyase activity
D	0046872	molecular_function	metal ion binding
D	0140677	molecular_function	molecular function activator activity

Functional Information from PROSITE/UniProt

site_id	PS00161
Number of Residues	6
Details	ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR

Chain	Residue	Details
A	LYS121-ARG126

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:14575713

Chain	Residue	Details
A	GLY46
D	GLY46
D	ALA86
D	THR159
A	ALA86
A	THR159
B	GLY46
B	ALA86
B	THR159
C	GLY46
C	ALA86
C	THR159

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site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939

Chain	Residue	Details
A	ILE88
B	ILE211
B	ALA242
B	ASN271
C	ILE88
C	GLY124
C	ALA189
C	ILE211
C	ALA242
C	ASN271
D	ILE88
A	GLY124
D	GLY124
D	ALA189
D	ILE211
D	ALA242
D	ASN271
A	ALA189
A	ILE211
A	ALA242
A	ASN271
B	ILE88
B	GLY124
B	ALA189

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8m

Chain	Residue	Details
A	HIS113
A	ARG158

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8m

Chain	Residue	Details
B	HIS113
B	ARG158

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8m

Chain	Residue	Details
C	HIS113
C	ARG158

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8m

Chain	Residue	Details
D	HIS113
D	ARG158

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