Entry	Entry name	Gene names	Protein names	EC number	Function [CC]	Pathway	Keywords	Protein existence	Gene ontology (GO)	Protein families	Taxonomic lineage (SUPERKINGDOM)	Taxonomic lineage (PHYLUM)	Taxonomic lineage (CLASS)	Taxonomic lineage (ORDER)	Taxonomic lineage (FAMILY)	Taxonomic lineage (GENUS)	Taxonomic lineage IDs (GENUS)	Taxonomic lineage (SPECIES)	Taxonomic lineage IDs (SPECIES)	Cross-reference (BioCyc)	Cross-reference (BRENDA)	Cross-reference (CDD)	Cross-reference (eggNOG)	Ensembl transcript	Cross-reference (InterPro)	Cross-reference (KEGG)	Cross-reference (Pfam)	Cross-reference (Reactome)	Cross-reference (RefSeq)	Cross-reference (UniPathway)
A0A1H6AD45	A0A1H6AD45_9GAMM	B7O88_11480	DLH domain-containing protein				3D-structure;Signal	Evidence at protein level	hydrolase activity [GO:0016787]		Bacteria	Proteobacteria	Gammaproteobacteria	Pseudomonadales	Pseudomonadaceae	Halopseudomonas	2901189.0	Halopseudomonas aestusnigri							IPR029058;IPR002925;		PF01738;			
O22443	O22443_SOYBN	Ep 548068 GLYMA_09G022300	Peroxidase (EC 1.11.1.7)	1.11.1.7	FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}.		3D-structure;Calcium;Disulfide bond;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal	Evidence at protein level	extracellular region [GO:0005576]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]	Peroxidase family, Ascorbate peroxidase subfamily; Peroxidase family, Classical plant (class III) peroxidase subfamily	Eukaryota	Streptophyta	Magnoliopsida	Fabales	Fabaceae	Glycine	3846.0	Glycine max (Soybean) (Glycine hispida)			1.11.1.7;	cd00693;	ENOG502QVXS;		IPR002016;IPR010255;IPR000823;IPR019794;IPR019793;IPR033905;	gmx:548068;	PF00141;		NP_001238315.1;	
Q9HTK9	RURE_PSEAE	alkT PA5349	Rubredoxin-NAD(+) reductase (RdxR) (EC 1.18.1.1)	1.18.1.1	FUNCTION: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. {ECO:0000269|PubMed:12730186, ECO:0000269|PubMed:14574114}.	PATHWAY: Hydrocarbon metabolism; alkane degradation.	3D-structure;Cytoplasm;FAD;Flavoprotein;NAD;Oxidoreductase;Reference proteome	Evidence at protein level	cytoplasm [GO:0005737]; flavin adenine dinucleotide binding [GO:0050660]; rubredoxin-NAD+ reductase activity [GO:0015044]; rubredoxin-NADP+ reductase activity [GO:0015046]; alkane catabolic process [GO:0043448]	FAD-dependent oxidoreductase family	Bacteria	Proteobacteria	Gammaproteobacteria	Pseudomonadales	Pseudomonadaceae	Pseudomonas	286.0	Pseudomonas aeruginosa	287.0		1.18.1.1;				IPR036188;IPR023753;IPR041364;	pae:PA5349;	PF07992;PF18113;		NP_254036.1;WP_003114369.1;	UPA00191
G9BY57	PETH_UNKP		Leaf-branch compost cutinase (LC-cutinase) (LCC) (EC 3.1.1.74) (PET-digesting enzyme) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101)	3.1.1.74; 3.1.1.101	FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:22194294). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters), with a preference for short-chain substrates (C4 substrate at most) (PubMed:22194294, PubMed:24593046). Cannot hydrolyze olive oil (PubMed:22194294). Is also able to degrade poly(ethylene terephthalate), the most abundant polyester plastic in the world (PubMed:22194294, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:22194294). {ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:24593046, ECO:0000269|PubMed:32269349}.		3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal	Evidence at protein level	extracellular region [GO:0005576]; acetylesterase activity [GO:0008126]; cutinase activity [GO:0050525]	AB hydrolase superfamily	Bacteria							Unknown prokaryotic organism							IPR029058;IPR029059;		PF12695;			
Q02567	PEM1_PHACH	MNP1	Manganese peroxidase 1 (MnP-1) (MnP1) (EC 1.11.1.13) (Manganese peroxidase isozyme 1) (Peroxidase manganese-dependent 1) (Peroxidase manganese-dependent I)	1.11.1.13	FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.		3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Manganese;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Signal	Evidence at protein level	extracellular region [GO:0005576]; heme binding [GO:0020037]; manganese peroxidase activity [GO:0016689]; metal ion binding [GO:0046872]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lignin catabolic process [GO:0046274]	Peroxidase family, Ligninase subfamily	Eukaryota	Basidiomycota	Agaricomycetes	Polyporales	Phanerochaetaceae	Phanerodontia	2492674.0	Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)			1.11.1.13;	cd00692;			IPR044831;IPR002016;IPR010255;IPR001621;IPR024589;IPR019794;IPR019793;		PF00141;PF11895;			
