Detail Information for IndEnz0009000129
IED ID IndEnz0009000129
Enzyme Type ID chitinase000129
Protein Name Cellulose synthase A catalytic subunit 3
UDP-forming
AtCesA3
EC 2.4.1.12
Constitutive expression of VSP1 protein 1
Isoxaben-resistant protein 1
Ath-B
Protein ECTOPIC LIGNIN 1
Protein RADIALLY SWOLLEN 5
AtRSW5
Gene Name CESA3 ATHB CEV1 ELI1 IXR1 RSW5 At5g05170 K2A11.4
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MESEGETAGKPMKNIVPQTCQICSDNVGKTVDGDRFVACDICSFPVCRPCYEYERKDGNQSCPQCKTRYKRLKGSPAIPGDKDEDGLADEGTVEFNYPQKEKISERMLGWHLTRGKGEEMGEPQYDKEVSHNHLPRLTSRQDTSGEFSAASPERLSVSSTIAGGKRLPYSSDVNQSPNRRIVDPVGLGNVAWKERVDGWKMKQEKNTGPVSTQAASERGGVDIDASTDILADEALLNDEARQPLSRKVSIPSSRINPYRMVIMLRLVILCLFLHYRITNPVPNAFALWLVSVICEIWFALSWILDQFPKWFPVNRETYLDRLALRYDREGEPSQLAAVDIFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGAAMLSFESLAETSEFARKWVPFCKKYSIEPRAPEWYFAAKIDYLKDKVQTSFVKDRRAMKREYEEFKIRINALVSKALKCPEEGWVMQDGTPWPGNNTRDHPGMIQVFLGQNGGLDAEGNELPRLVYVSREKRPGFQHHKKAGAMNALVRVSAVLTNGPFILNLDCDHYINNSKALREAMCFLMDPNLGKQVCYVQFPQRFDGIDKNDRYANRNTVFFDINLRGLDGIQGPVYVGTGCVFNRTALYGYEPPIKVKHKKPSLLSKLCGGSRKKNSKAKKESDKKKSGRHTDSTVPVFNLDDIEEGVEGAGFDDEKALLMSQMSLEKRFGQSAVFVASTLMENGGVPPSATPENLLKEAIHVISCGYEDKSDWGMEIGWIYGSVTEDILTGFKMHARGWRSIYCMPKLPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGYNGRLKFLERFAYVNTTIYPITSIPLLMYCTLPAVCLFTNQFIIPQISNIASIWFLSLFLSIFATGILEMRWSGVGIDEWWRNEQFWVIGGVSAHLFAVFQGILKVLAGIDTNFTVTSKASDEDGDFAELYLFKWTTLLIPPTTLLIVNLVGVVAGVSYAINSGYQSWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVVWSVLLASIFSLLWVRIDPFTSRVTGPDILECGINC
Enzyme Length 1065
Uniprot Accession Number Q941L0
Absorption
Active Site ACT_SITE 379; /evidence=ECO:0000255; ACT_SITE 765; /evidence=ECO:0000255
Activity Regulation
Binding Site BINDING 545; /note=Substrate; /evidence=ECO:0000255; BINDING 547; /note=Substrate; /evidence=ECO:0000255
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
DNA Binding
EC Number 2.4.1.12
Enzyme Function FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation, especially in roots. {ECO:0000269|PubMed:11340179, ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12119374, ECO:0000269|PubMed:12713541, ECO:0000269|PubMed:17878302, ECO:0000269|PubMed:17878303}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
nucleotide Binding
Features Active site (2); Beta strand (16); Binding site (2); Chain (1); Coiled coil (1); Compositional bias (1); Glycosylation (1); Helix (12); Metal binding (8); Modified residue (4); Mutagenesis (6); Region (1); Sequence conflict (3); Topological domain (9); Transmembrane (8); Turn (4); Zinc finger (1)
Keywords 3D-structure;Cell membrane;Cell wall biogenesis/degradation;Cellulose biosynthesis;Coiled coil;Glycoprotein;Glycosyltransferase;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Zinc;Zinc-finger
Interact With Q94JQ6
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue MOD_RES 3; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:17427041, ECO:0007744|PubMed:15308754"; MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:17427041, ECO:0007744|PubMed:14506206, ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"; MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:17427041"; MOD_RES 216; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:17427041, ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 7CK1; 7CK2; 7CK3;
Mapped Pubmed ID 10330464; 10887094; 11842152; 15020435; 15940463; 16020787; 16159327; 16255250; 16453133; 16618929; 17041031; 17189328; 17317660; 17351116; 18393624; 18495638; 18650403; 19269997; 19376929; 19376932; 19645738; 20064062; 20377682; 20876662; 21798944; 22036185; 22272350; 22375033; 22514801; 22926318; 22995285; 23148892; 23299322; 23527628; 24194514; 24873912; 25122472; 25262226; 25352273; 25516570; 25926481; 26343580; 26391708; 26969722; 27543091; 27647923; 28150693; 28944540; 29388029; 29514326; 30171735; 30197649; 30277578; 31221729; 31557400; 32037093; 32524705; 33729990; 34524465; 9165747;
Motif
Gene Encoded By
Mass 119,683
Kinetics
Metal Binding METAL 20; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 23; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 39; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 42; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 47; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 50; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 62; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9SWW6; METAL 65; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9SWW6
Rhea ID RHEA:19929
Cross Reference Brenda 2.4.1.12;