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 O77457

Entry ID Method Resolution Chain Position Source
AF-O77457-F1 Predicted AlphaFoldDB

No variants for O77457

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O77457

No associated diseases with O77457

No regional properties for O77457

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O77457

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.

3 GO annotations of biological process

Name Definition
ommochrome biosynthetic process The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.
tryptophan catabolic process to acetyl-CoA The chemical reactions and pathways resulting in the breakdown of tryptophan into other compounds, including acetyl-CoA.
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
MSCPMRSGFV DSVQGGHHLG SEAGMLYGEY LMLDKVLSAQ RMLSVEGKKP VHDEHLFIVT
70 80 90 100 110 120
HQAYELWFKQ IIFELDSIRD LFSTEHIEES RTLEILKRLN RIVMILKLLV DQVPILETMT
130 140 150 160 170 180
PLDFMDFRDY LSPASGFQSL QFRLLENKLG VKSEHRVKYN QKYTEVFASD PGAIERIGTT
190 200 210 220 230 240
ETEPSLADLV QKWLERTPGL EQDGFNFWGK FQESVEQLLA EQEASAMSEE HENVREYRLM
250 260 270 280 290 300
DIDKRREVYK SIFDAQVHDA LVARGERRFT HKALQGAIMI TFYRDEPRFS QPHQLLMLLM
310 320 330 340 350 360
DIDSLITKWR YNHVIMVQRM IGSQQLGTGG SSGYQYLRST LSDRYKVFLD LFNLSTFLIP
370 380 390
RQSIPPLTNE MQKALNLAWG SPAHFARNGS LH