Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2YII

Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0006558	biological_process	L-phenylalanine metabolic process
A	0006559	biological_process	L-phenylalanine catabolic process
A	0009698	biological_process	phenylpropanoid metabolic process
A	0009800	biological_process	cinnamic acid biosynthetic process
A	0009820	biological_process	alkaloid metabolic process
A	0009821	biological_process	alkaloid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016841	molecular_function	ammonia-lyase activity
A	0016853	molecular_function	isomerase activity
A	0016869	molecular_function	intramolecular aminotransferase activity
A	0042617	biological_process	paclitaxel biosynthetic process
A	0045548	molecular_function	phenylalanine ammonia-lyase activity
A	0051289	biological_process	protein homotetramerization
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0006558	biological_process	L-phenylalanine metabolic process
B	0006559	biological_process	L-phenylalanine catabolic process
B	0009698	biological_process	phenylpropanoid metabolic process
B	0009800	biological_process	cinnamic acid biosynthetic process
B	0009820	biological_process	alkaloid metabolic process
B	0009821	biological_process	alkaloid biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016841	molecular_function	ammonia-lyase activity
B	0016853	molecular_function	isomerase activity
B	0016869	molecular_function	intramolecular aminotransferase activity
B	0042617	biological_process	paclitaxel biosynthetic process
B	0045548	molecular_function	phenylalanine ammonia-lyase activity
B	0051289	biological_process	protein homotetramerization
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0006558	biological_process	L-phenylalanine metabolic process
C	0006559	biological_process	L-phenylalanine catabolic process
C	0009698	biological_process	phenylpropanoid metabolic process
C	0009800	biological_process	cinnamic acid biosynthetic process
C	0009820	biological_process	alkaloid metabolic process
C	0009821	biological_process	alkaloid biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016841	molecular_function	ammonia-lyase activity
C	0016853	molecular_function	isomerase activity
C	0016869	molecular_function	intramolecular aminotransferase activity
C	0042617	biological_process	paclitaxel biosynthetic process
C	0045548	molecular_function	phenylalanine ammonia-lyase activity
C	0051289	biological_process	protein homotetramerization
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0006558	biological_process	L-phenylalanine metabolic process
D	0006559	biological_process	L-phenylalanine catabolic process
D	0009698	biological_process	phenylpropanoid metabolic process
D	0009800	biological_process	cinnamic acid biosynthetic process
D	0009820	biological_process	alkaloid metabolic process
D	0009821	biological_process	alkaloid biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016841	molecular_function	ammonia-lyase activity
D	0016853	molecular_function	isomerase activity
D	0016869	molecular_function	intramolecular aminotransferase activity
D	0042617	biological_process	paclitaxel biosynthetic process
D	0045548	molecular_function	phenylalanine ammonia-lyase activity
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME A 1089

Chain	Residue
A	CYS89
C	GLY412
C	ASN413
C	SER415
C	ASP423
C	TYR424

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME A 1175

Chain	Residue
A	LEU227
A	GLN459
A	FMT1679
B	TYR322
A	TYR80
A	MDO175
A	LEU179

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 1679

Chain	Residue
A	TYR80
A	ASN231
A	ASN355
A	PHE371
A	BME1175
A	HOH2190
B	GLN319
B	ARG325

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME B 1089

Chain	Residue
B	CYS89
B	ARG92
B	HOH2193
D	GLY412
D	ASN413
D	SER415
D	LEU420
D	ASP423

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME B 1175

Chain	Residue
A	TYR322
B	TYR80
B	MDO175
B	LEU179
B	GLN459
B	FMT1680

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1679

Chain	Residue
B	ASP423
B	GLY425
B	SER642
B	ALA643
B	PRO649
B	HOH2129
B	HOH2179
D	ARG106
D	CYS107

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT B 1680

Chain	Residue
A	GLN319
A	ARG325
A	HOH2118
B	TYR80
B	ASN231
B	ASN355
B	PHE371
B	BME1175

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME C 1089

Chain	Residue
A	GLY412
A	ASN413
A	SER415
A	ASP423
C	CYS89
C	ARG92

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BME C 1175

Chain	Residue
C	TYR80
C	GLY87
C	MDO175
C	LEU179
C	LEU227
C	ASN231
C	GLN459
C	FMT1680
D	TYR322

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT C 1680

Chain	Residue
C	TYR80
C	ASN231
C	ASN355
C	PHE371
C	BME1175
C	HOH2031
D	GLN319
D	ARG325

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME D 1089

Chain	Residue
B	GLY412
B	ASN413
B	SER415
B	LEU420
B	ASP423
D	CYS89

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME D 1175

Chain	Residue
C	TYR322
D	TYR80
D	MDO175
D	LEU179
D	LEU227
D	GLN459
D	FMT1679

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT D 1679

Chain	Residue
C	GLN319
C	ARG325
C	HOH2129
D	TYR80
D	ASN231
D	ASN355
D	PHE371
D	BME1175

Functional Information from PROSITE/UniProt

site_id	PS00488
Number of Residues	17
Details	PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GSVSASGDLiPLAyiaG

Chain	Residue	Details
A	GLY171-LEU189

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22113970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24786474","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24786474","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CQ5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P11544","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"2,3-didehydroalanine (Ser)","evidences":[{"source":"PubMed","id":"24786474","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Cross-link: {"description":"5-imidazolinone (Ala-Gly)","evidences":[{"source":"PubMed","id":"24786474","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)