Detail Information for IndEnz0005000817
IED ID IndEnz0005000817
Enzyme Type ID lipase000817
Protein Name Rhamnogalacturonan acetylesterase
RGAE
EC 3.1.1.86
Gene Name AN2528
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MKSIALTSLSLLPSALAQTIYLAGDSTMASSTPGWGDYIADSVSVEISNQAIGGRSARSYTREGRFQAIADVLQAGDYVVIEFGHNDGGSLSNDNGRTDCPGDGDETCETVYNGVAETVLTFPAYIENAALLFLEKGANVLISSQTPNNPWESGTFSYTPNRFVGYAELAAQRAGVDYVDHGAYTASIFEALGADTVNSFYPNDHTHTNAEGSSVVADAFLKAVVCSGVALNDVLTRTDFDGECL
Enzyme Length 245
Uniprot Accession Number Q5BAA2
Absorption
Active Site ACT_SITE 26; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 204; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 207; /evidence=ECO:0000250|UniProtKB:Q00017
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I.; EC=3.1.1.86; Evidence={ECO:0000269|PubMed:16844780};
DNA Binding
EC Number 3.1.1.86
Enzyme Function FUNCTION: Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Involved in degradation of pectin. {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:22589326}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1)
Keywords Disulfide bond;Hydrolase;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22589326}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 25,870
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda