Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P30359

Entry ID Method Resolution Chain Position Source
AF-P30359-F1 Predicted AlphaFoldDB

No variants for P30359

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P30359

No associated diseases with P30359

No regional properties for P30359

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P30359

Functions

Description
EC Number 1.1.1.195 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
cinnamyl-alcohol dehydrogenase activity Catalysis of the reaction: cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+.
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
sinapyl alcohol dehydrogenase activity Catalysis of the reaction: sinapaldehyde + NADPH + H+ = sinapyl-alcohol + NADP+.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
lignin biosynthetic process The chemical reactions and pathways resulting in the formation of lignins, a class of polymers formed by the dehydrogenetive radical polymerization of various phenylpropanoid monomers.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGGLEVEKTT IGWAARDPSG VLSPYTYTLR NTGPEDVEVK VLYCGLCHTD LHQVKNDLGM
70 80 90 100 110 120
SNYPLVPGHE VVGEVVEVGP DVSKFKVGDT VGVGLLVGSC RNCGPCKRDI EQYCNKKIWN
130 140 150 160 170 180
CNDVYTDGKP TQGGFAKSMV VDQKFVVKIP EGMAPEQAAP LLCAGITVYS PLNHFGFKQS
190 200 210 220 230 240
GLRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSNKKRQEA LEHLGADDYL VSSDTDKMQE
250 260 270 280 290 300
ASDSLDYIID TVPVGHPLEP YLSLLKIDGK LILMGVINTP LQFISPMVML GRKSITGSFI
310 320 330 340 350
GSMKETEEML DFCKEKGVTS QIEIVKMDYI NTAMERLEKN DVRYRFVVDV IGSKLDQ