##gff-version 3
Q05514	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000084547;Note=Methylaspartate ammonia-lyase	
Q05514	UniProtKB	Active site	331	331	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11748244,ECO:0000269|PubMed:19670200;Dbxref=PMID:11748244,PMID:19670200	
Q05514	UniProtKB	Binding site	172	172	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q05514	UniProtKB	Binding site	238	238	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11748244,ECO:0000269|PubMed:22614383;Dbxref=PMID:11748244,PMID:22614383	
Q05514	UniProtKB	Binding site	273	273	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11748244,ECO:0000269|PubMed:22614383;Dbxref=PMID:11748244,PMID:22614383	
Q05514	UniProtKB	Binding site	307	307	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11748244,ECO:0000269|PubMed:22614383;Dbxref=PMID:11748244,PMID:22614383	
Q05514	UniProtKB	Binding site	329	329	.	.	.	.	
Q05514	UniProtKB	Binding site	360	361	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q05514	UniProtKB	Binding site	361	361	.	.	.	.	
Q05514	UniProtKB	Site	194	194	.	.	.	Note=Transition state stabilizer	
Q05514	UniProtKB	Mutagenesis	73	73	.	.	.	Note=It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22614383;Dbxref=PMID:22614383	
Q05514	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	194	194	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	329	329	.	.	.	Note=Very strong decrease of the catalytic efficiency for deamination%2C whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	329	329	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	331	331	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	331	331	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. K->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	331	331	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. K->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	331	331	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	331	331	.	.	.	Note=It abolishes deaminase and aminase activities and does not show any major conformational changes. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19670200;Dbxref=PMID:19670200	
Q05514	UniProtKB	Mutagenesis	384	384	.	.	.	Note=It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22614383;Dbxref=PMID:22614383	
Q05514	UniProtKB	Beta strand	2	11	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	14	18	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	20	24	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	52	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	64	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	86	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	98	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	109	118	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	128	146	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	150	158	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	179	186	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	190	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	200	204	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	209	225	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	234	238	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	242	246	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Turn	247	249	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	251	265	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	270	273	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	281	298	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	302	306	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	313	321	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	325	330	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	333	335	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	339	350	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	354	357	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	365	378	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	381	384	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Beta strand	387	391	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ	
Q05514	UniProtKB	Helix	392	410	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KCZ