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 Q8R9M7

Entry ID Method Resolution Chain Position Source
AF-Q8R9M7-F1 Predicted AlphaFoldDB

No variants for Q8R9M7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8R9M7

No associated diseases with Q8R9M7

2 regional properties for Q8R9M7

Type Name Position InterPro Accession
conserved_site Indole-3-glycerol phosphate synthase, conserved site 48 - 66 IPR001468
domain Indole-3-glycerol phosphate synthase domain 1 - 253 IPR013798

Functions

Description
EC Number 4.1.1.48 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

1 GO annotations of molecular function

Name Definition
indole-3-glycerol-phosphate synthase activity Catalysis of the reaction: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O.

1 GO annotations of biological process

Name Definition
tryptophan biosynthetic process The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MILEEIVNFK KEEVRKKKEL KPYNELLNVN AVYRGDFKNS LNKGKVAIIG EIKRASPSKG
70 80 90 100 110 120
IIREEFDLVE IAKTYEKAEV DAISVLTEKR FFKGEGGYIP QVKKLTTKPV LRKDFVIDEY
130 140 150 160 170 180
QIYESKFLGA DAVLLIVAIL EDKLKGFCDI AKQIGLDVLV EVHEEEELET ALKAGCDIIG
190 200 210 220 230 240
INNRDLKTFK VDIKTTERLI KNIPKDKIVV SESGIKTPED VLYLSSLGVK AVLIGESFMK
250
MDEGRIKEFV KKVRGG