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 P48776

Entry ID Method Resolution Chain Position Source
AF-P48776-F1 Predicted AlphaFoldDB

33 variants for P48776

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388635445 3 G>E No EVA
rs3388636725 4 C>* No EVA
rs3388639373 5 P>R No EVA
rs3388638448 5 P>S No EVA
rs3388638489 6 F>L No EVA
rs32660985 18 V>L No EVA
rs241866018 39 G>E No EVA
rs3393301835 103 R>G No EVA
rs3393256476 147 L>Q No EVA
rs3393052588 151 S>A No EVA
rs3393196826 153 F>* No EVA
rs3393261337 153 F>* No EVA
rs3393271715 160 L>M No EVA
rs3393261320 160 L>N No EVA
rs3393289397 176 N>H No EVA
rs3393065144 176 N>K No EVA
rs3393272088 177 R>S No EVA
rs3393301724 178 K>* No EVA
rs3393196860 178 K>N No EVA
rs3393052607 180 Y>D No EVA
rs3392873850 181 R>S No EVA
rs32653061 182 D>A No EVA
rs240582100 218 N>H No EVA
rs3388635424 229 N>I No EVA
rs226657256 245 T>N No EVA
rs3388632277 302 P>S No EVA
rs3393065110 371 Y>S No EVA
rs3393052574 375 R>S No EVA
rs3393146994 376 H>D No EVA
rs3393052617 376 H>L No EVA
rs3392873837 378 V>E No EVA
rs3388636712 399 Y>D No EVA
rs3388629813 399 Y>F No EVA

No associated diseases with P48776

No regional properties for P48776

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P48776

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

6 GO annotations of molecular function

Name Definition
amino acid binding Binding to an amino acid, organic acids containing one or more amino substituents.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
oxygen binding Binding to oxygen (O2).
tryptophan 2,3-dioxygenase activity Catalysis of the reaction: L-tryptophan + O2 = N-formyl-L-kynurenine.

5 GO annotations of biological process

Name Definition
protein homotetramerization The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
response to nitroglycerin Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitroglycerin stimulus.
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.
tryptophan metabolic process The chemical reactions and pathways involving tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P48775 TDO2 Tryptophan 2,3-dioxygenase Homo sapiens (Human) PR
P21643 Tdo2 Tryptophan 2,3-dioxygenase Rattus norvegicus (Rat) PR
Q5EBG2 tdo2 Tryptophan 2,3-dioxygenase Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
A7MBU6 tdo2a Tryptophan 2,3-dioxygenase A Danio rerio (Zebrafish) (Brachydanio rerio) PR
Q7SY53 tdo2b Tryptophan 2,3-dioxygenase B Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSGCPFAGNS VGYTLKNVSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE
70 80 90 100 110 120
VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV
130 140 150 160 170 180
IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY
190 200 210 220 230 240
RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKNI LKGLEEEFLR
250 260 270 280 290 300
IQAKTDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE
310 320 330 340 350 360
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK
370 380 390 400
VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD