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

2 structures for P17770

Entry ID Method Resolution Chain Position Source
6EEW X-ray 205 A A/B/C/D 1-500 PDB
AF-P17770-F1 Predicted AlphaFoldDB

No variants for P17770

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P17770

No associated diseases with P17770

1 regional properties for P17770

Type Name Position InterPro Accession
binding_site Pyridoxal-phosphate binding site 312 - 333 IPR021115

Functions

Description
EC Number 4.1.1.28 Carboxy-lyases
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

3 GO annotations of molecular function

Name Definition
5-hydroxy-L-tryptophan decarboxylase activity Catalysis of the reaction: 5-hydroxy-L-tryptophan + H+ = CO2 + serotonin.
L-tryptophan decarboxylase activity Catalysis of the reaction: L-tryptophan + H+ = CO2 + tryptamine.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

2 GO annotations of biological process

Name Definition
cellular amino acid metabolic process The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
organonitrogen compound biosynthetic process The chemical reactions and pathways resulting in the formation of organonitrogen compound.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGSIDSTNVA MSNSPVGEFK PLEAEEFRKQ AHRMVDFIAD YYKNVETYPV LSEVEPGYLR
70 80 90 100 110 120
KRIPETAPYL PEPLDDIMKD IQKDIIPGMT NWMSPNFYAF FPATVSSAAF LGEMLSTALN
130 140 150 160 170 180
SVGFTWVSSP AATELEMIVM DWLAQILKLP KSFMFSGTGG GVIQNTTSES ILCTIIAARE
190 200 210 220 230 240
RALEKLGPDS IGKLVCYGSD QTHTMFPKTC KLAGIYPNNI RLIPTTVETD FGISPQVLRK
250 260 270 280 290 300
MVEDDVAAGY VPLFLCATLG TTSTTATDPV DSLSEIANEF GIWIHVDAAY AGSACICPEF
310 320 330 340 350 360
RHYLDGIERV DSLSLSPHKW LLAYLDCTCL WVKQPHLLLR ALTTNPEYLK NKQSDLDKVV
370 380 390 400 410 420
DFKNWQIATG RKFRSLKLWL ILRSYGVVNL QSHIRSDVAM GKMFEEWVRS DSRFEIVVPR
430 440 450 460 470 480
NFSLVCFRLK PDVSSLHVEE VNKKLLDMLN STGRVYMTHT IVGGIYMLRL AVGSSLTEEH
490
HVRRVWDLIQ KLTDDLLKEA