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_000345	gene-LXL04_000345	KAL4587474.1	OH-1004	1	Q8L5A7	SOT15_ARATH	Swiss-Prot		Cytosolic sulfotransferase 15 OS=Arabidopsis thaliana OX=3702 GN=SOT15 PE=1 SV=1	Arabidopsis thaliana	SOT15	40.881	318	93.155	2.11e-85	265.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At5g07010	磺基转移酶，利用 3'-磷酸-5'-腺苷基硫酸盐 作为磺酸盐供体，特异性催化羟基茉莉酮酸酯的硫酸盐缀合，优先选择 12-羟基茉莉酮酸酯而不是 11-羟基茉莉酮酸酯。	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to specifically catalyze the sulfate conjugation of hydroxyjasmonates, with a preference for 12- hydroxyjasmonate over 11-hydroxyjasmonate.	"[{""pmid"":""12637544"",""title"":""Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana."",""doi"":""10.1074/jbc.m211943200"",""url"":""https://pubmed.ncbi.nlm.nih.gov/12637544/"",""year"":""2003"",""journal"":""The Journal of biological chemistry"",""authors"":""Gidda SK, Miersch O, Levitin A, Schmidt J, Wasternack C, Varin L."",""matched_aliases"":[""AtST2A""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false}]"
LXL04_000345	gene-LXL04_000345	KAL4587474.1	OH-1004	3	Q9ZPQ5	SOT13_ARATH	Swiss-Prot		Cytosolic sulfotransferase 13 OS=Arabidopsis thaliana OX=3702 GN=SOT13 PE=3 SV=1	Arabidopsis thaliana	SOT13	42.903	310	91.667	1.03e-80	251.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At2g03770	磺基转移酶利用 3'-磷酸-5'-腺苷基硫酸盐 (PAPS) 作为磺酸盐供体。	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor.	[]
LXL04_000345	gene-LXL04_000345	KAL4587474.1	OH-1004	4	Q8GZ53	SOT14_ARATH	Swiss-Prot		Cytosolic sulfotransferase 14 OS=Arabidopsis thaliana OX=3702 GN=SOT14 PE=2 SV=1	Arabidopsis thaliana	SOT14	39.157	332	96.726	6.11e-79	248.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At5g07000	磺基转移酶利用 3'-磷酸-5'-腺苷基硫酸盐 (PAPS) 作为磺酸盐供体。	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor.	[]
LXL04_000345	gene-LXL04_000345	KAL4587474.1	OH-1004	5	Q9C9D0	SOT16_ARATH	Swiss-Prot		Cytosolic sulfotransferase 16 OS=Arabidopsis thaliana OX=3702 GN=SOT16 PE=1 SV=1	Arabidopsis thaliana	SOT16	41.27	315	90.179	3.52e-78	245.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At1g74100	硫酸基转移酶，以3′-磷酸腺苷-5′-磷酸硫酸（PAPS）为供体，催化脱硫硫代葡萄糖苷（dsGS）的硫酸化，完成硫代葡萄糖苷核心结构生物合成的最后一步。	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure.	"[{""pmid"":""15358770"",""title"":""Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure."",""doi"":""10.1074/jbc.m407681200"",""url"":""https://pubmed.ncbi.nlm.nih.gov/15358770/"",""year"":""2004"",""journal"":""The Journal of biological chemistry"",""authors"":""Piotrowski M; Schemenewitz A; Lopukhina A; Müller A; Janowitz T; Weiler EW; Oecking C"",""matched_aliases"":[""AtST5A"",""CORI-7""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""16367753"",""title"":""The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed."",""doi"":""10.1111/j.1742-4658.2005.05048.x"",""url"":""https://pubmed.ncbi.nlm.nih.gov/16367753/"",""year"":""2006"",""journal"":""The FEBS journal"",""authors"":""Klein M; Reichelt M; Gershenzon J; Papenbrock J"",""matched_aliases"":[""AtSOT16""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""19077143"",""title"":""Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana."",""doi"":""10.1111/j.1399-3054.2008.01182.x"",""url"":""https://pubmed.ncbi.nlm.nih.gov/19077143/"",""year"":""2009"",""journal"":""Physiologia plantarum"",""authors"":""Klein M; Papenbrock J"",""matched_aliases"":[""AtSOT16""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""21281472"",""title"":""Modulation of sulfur metabolism enables efficient glucosinolate engineering."",""doi"":""10.1186/1472-6750-11-12"",""url"":""https://pubmed.ncbi.nlm.nih.gov/21281472/"",""year"":""2011"",""journal"":""BMC biotechnology"",""authors"":""Møldrup ME; Geu-Flores F; Olsen CE; Halkier BA"",""matched_aliases"":[""AtSOT16""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false}]"