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 O35078

Entry ID Method Resolution Chain Position Source
AF-O35078-F1 Predicted AlphaFoldDB

2 variants for O35078

Variant ID(s) Position Change Description Diseaes Association Provenance
rs197829043 215 T>S No EVA
rs3322217825 275 M>V No EVA

No associated diseases with O35078

2 regional properties for O35078

Type Name Position InterPro Accession
domain FAD dependent oxidoreductase 2 - 328 IPR006076
conserved_site D-amino acid oxidase, conserved site 304 - 322 IPR006181

Functions

Description
EC Number
Subcellular Localization
  • Peroxisome matrix
  • Cytoplasm, cytosol
  • Presynaptic active zone
  • Secreted
  • Transiently present in the cytosol before being delivered to the peroxisomes (By similarity)
  • In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (PubMed:21700703)
  • Secreted into the lumen of the small intestine (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrial outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

3 GO annotations of molecular function

Name Definition
D-amino-acid oxidase activity Catalysis of the reaction: a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + hydrogen peroxide.
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
identical protein binding Binding to an identical protein or proteins.

7 GO annotations of biological process

Name Definition
D-alanine catabolic process The chemical reactions and pathways resulting in the breakdown of D-alanine, the D-enantiomer of the amino acid alanine.
D-amino acid catabolic process The chemical reactions and pathways resulting in the breakdown of D-amino acids, the D-enantiomers of amino acids.
D-serine catabolic process The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
D-serine metabolic process The chemical reactions and pathways involving D-serine, the D-enantiomer of serine, i.e. (2R)-2-amino-3-hydroxypropanoic acid.
dopamine biosynthetic process The chemical reactions and pathways resulting in the formation of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
leucine metabolic process The chemical reactions and pathways involving leucine, 2-amino-4-methylpentanoic acid.
proline catabolic process The chemical reactions and pathways resulting in the breakdown of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31228 DDO D-aspartate oxidase Bos taurus (Bovine) PR
P14920 DAO D-amino-acid oxidase Homo sapiens (Human) PR
10 20 30 40 50 60
MRVAVIGAGV IGLSTALCIH ERYHPAQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN
70 80 90 100 110 120
PQEAEWNQQT FDHLQSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKSTV LGFRKLTPSE
130 140 150 160 170 180
LDMFPDYSYG WFNTSLLLEG KSYLSWLTER LTERGVKFIH RKVASFEEVV RGGVDVIINC
190 200 210 220 230 240
TGVWAGALQA DASLQPGRGQ IIQVEAPWIK HFILTHDPSL GIYNSPYIIP GSKTVTLGGV
250 260 270 280 290 300
FQLGNWSELN SVHDHNTIWK SCCQLEPTLK NARIMGELTG FRPVRPQVRL ERERLRFGSS
310 320 330 340
SAEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKNLSR MPPSHL