query	query_gene_id	query_protein_id	source_reference	hit_rank	swissprot_acc	swissprot_entry	database_section	target_gene_id	description	organism	homolog_gene_name	percent_identity	alignment_length	query_coverage	evalue	bitscore	confidence	evidence_type	source_db	reference_gene_id	reference_function_zh	reference_function_en	reference_papers_json
LXL04_035063	gene-LXL04_035063	KAL4556897.1	OH-1004	1	F4K2A1	FPGS1_ARATH	Swiss-Prot		Folylpolyglutamate synthase OS=Arabidopsis thaliana OX=3702 GN=FPGS1 PE=1 SV=1	Arabidopsis thaliana	FPGS1	66.3	454	90.269	0.0	602.0	strong_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At5g05980	催化叶酸转化为多谷氨酸衍生物，使叶酸化合物在细胞内浓缩，并保持这些辅因子在细胞内的滞留，它们是大多数参与嘌呤、嘧啶和氨基酸合成中一碳转移反应的叶酸依赖酶的重要底物。	Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.	"[{""pmid"":""21070407"",""title"":""Functional analysis of folate polyglutamylation and its essential role in plant metabolism and development."",""doi"":""10.1111/j.1365-313x.2010.04336.x"",""url"":""https://pubmed.ncbi.nlm.nih.gov/21070407/"",""year"":""2010"",""journal"":""The Plant journal : for cell and molecular biology"",""authors"":""Mehrshahi P; Gonzalez-Jorge S; Akhtar TA; Ward JL; Santoyo-Castelazo A; Marcus SE; Lara-Núñez A; Ravanel S; Hawkins ND; Beale MH; Barrett DA; Knox JP; Gregory JF; Hanson AD; Bennett MJ; Dellapenna D"",""matched_aliases"":[""FPGS1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""21233333"",""title"":""The folylpolyglutamate synthetase plastidial isoform is required for postembryonic root development in Arabidopsis."",""doi"":""10.1104/pp.110.168278"",""url"":""https://pubmed.ncbi.nlm.nih.gov/21233333/"",""year"":""2011"",""journal"":""Plant physiology"",""authors"":""Srivastava AC; Ramos-Parra PA; Bedair M; Robledo-Hernández AL; Tang Y; Sumner LW; Díaz de la Garza RI; Blancaflor EB"",""matched_aliases"":[""ATDFB""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false}]"
LXL04_035063	gene-LXL04_035063	KAL4556897.1	OH-1004	2	Q8W035	FPGS3_ARATH	Swiss-Prot		Folylpolyglutamate synthase OS=Arabidopsis thaliana OX=3702 GN=FPGS3 PE=1 SV=1	Arabidopsis thaliana	FPGS3	60.46	435	90.062	0.0	535.0	strong_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g55630	催化叶酸转化为多谷氨酸衍生物，使叶酸化合物在细胞内浓缩，并保持这些辅因子在细胞内的滞留，它们是大多数参与嘌呤、嘧啶和氨基酸合成中一碳转移反应的叶酸依赖酶的重要底物。	Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.	[]
LXL04_035063	gene-LXL04_035063	KAL4556897.1	OH-1004	3	F4J2K2	FPGS2_ARATH	Swiss-Prot		Folylpolyglutamate synthase OS=Arabidopsis thaliana OX=3702 GN=FPGS2 PE=1 SV=1	Arabidopsis thaliana	FPGS2	56.29	469	90.476	1.46e-172	502.0	strong_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g10160	催化叶酸转化为多谷氨酸衍生物，使叶酸化合物在细胞内浓缩，并保持这些辅因子在细胞内的滞留，它们是大多数参与嘌呤、嘧啶和氨基酸合成中一碳转移反应的叶酸依赖酶的重要底物。	Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.	[]