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 A9FU01

Entry ID Method Resolution Chain Position Source
AF-A9FU01-F1 Predicted AlphaFoldDB

No variants for A9FU01

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9FU01

No associated diseases with A9FU01

No regional properties for A9FU01

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A9FU01

Functions

Description
EC Number 1.13.11.11 With incorporation of two atoms of oxygen
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
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
tryptophan 2,3-dioxygenase activity Catalysis of the reaction: L-tryptophan + O2 = N-formyl-L-kynurenine.

1 GO annotations of biological process

Name Definition
tryptophan catabolic process to kynurenine The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including kynurenine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRPVPGPSVF WGAGSRLPAP LVARAHRLLR TRRANPARGA SRITKDMNYW DYIHVEELLA
70 80 90 100 110 120
LQGGFDDDEQ KVGNDEALFI VVHQIYELWF KLILRELTSA RELFRQNPVP DQKLASAARS
130 140 150 160 170 180
FRRVVTIFEQ AIEHFRVMET LTTRDYLDFR DRLIPASGFQ SAQLREIELL LGLDDALRIP
190 200 210 220 230 240
LGREGSYKEA LKTADGAPSA ATRRVEARLA SGPSLKHFLD EWLSRTPIDG SSEPEGVVGF
250 260 270 280 290 300
LRSYTRSMRQ ENERRVQMAI DKALTPPDVE RLRARYEAES AAAEAFLLAE DDPAADAATR
310 320 330 340 350 360
EKRRAVRAAI VFIESYRELP RLAWPREVLD RILEMEQAML IWRQRHARMV ERVIGRRTGT
370 380 390 400 410
GGSAGVDYLD QTALRYRVFG DLWTVRSLLL RKPSVPEIEH ASDYGFRVED SP