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 Q6MM37

Entry ID Method Resolution Chain Position Source
AF-Q6MM37-F1 Predicted AlphaFoldDB

No variants for Q6MM37

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6MM37

No associated diseases with Q6MM37

5 regional properties for Q6MM37

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 162 - 501 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 68 - 146 IPR004365
domain Aminoacyl-tRNA synthetase, class II 184 - 503 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 177 - 503 IPR018149
domain Lysine-tRNA ligase, class II, N-terminal 67 - 174 IPR044136

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
MKYPPVHYHD YLGLNPLLNA QHPKSTEYGK PAHDELLFII VHQTYELWFK QILFELDSVL
70 80 90 100 110 120
STFQKPTVAE SEMGIASARL ERIVSILKLI IGQVDVLETM TPLDFLDFRD MLYPASGFQS
130 140 150 160 170 180
YQWRLIETKL GLRIGDRLAY NQSPFYKSLS ESQQGEMLNI MNQPSLHDSV EKWLERTPFL
190 200 210 220 230 240
QGENFNFWDS YKEAVNKMFQ DDITTVKNNP RLPDEEKAKT VAGLEQTLKS FDALFDEEAF
250 260 270 280 290 300
NKLRAEGQFR LSYKAMHAAL LIQLHRDQPI LQTPFRIIRA LLDIDETMTT WRYRHALMAM
310 320 330 340 350
RMLGQKIGTG GSSGHKYLAD ATAKHKIFGD FFNLTTFFIP RSQVPPLPKA IADRMSFHY