P23315

PR
Gene name
trpE
Protein name
Anthranilate synthase component 1
Names
AS, ASI
Species
Acinetobacter calcoaceticus
KEGG Pathway
EC number
4.1.3.27: Oxo-acid-lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

173-247 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P23315

Entry ID Method Resolution Chain Position Source
AF-P23315-F1 Predicted AlphaFoldDB

No variants for P23315

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P23315

No associated diseases with P23315

2 regional properties for P23315

Type Name Position InterPro Accession
domain Anthranilate synthase component I, N-terminal 27 - 173 IPR006805
domain Chorismate-utilising enzyme, C-terminal 221 - 480 IPR015890

Functions

Description
EC Number 4.1.3.27 Oxo-acid-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

2 GO annotations of molecular function

Name Definition
anthranilate synthase activity Catalysis of the reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
metal ion binding Binding to a metal ion.

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
MTSLTQFEQL KTAGYNTIPV YRQRLADTDT PLSVFARLKD YTQAYLFESV EGGENWARYS
70 80 90 100 110 120
IIGLGESTVF SCNAGQLTIK NAQGNITTQS CADPFQYIRD YQSQFKVPPH ALIPDLPQFT
130 140 150 160 170 180
GGLVGYFGYD AVRYIEPRLS NVPEADPVGL PDIWMMLSKT VIIFDNLKDT LFLIVHANTT
190 200 210 220 230 240
DEEAYQRAQN QLDYLERLLA TPVSLQAKKH KAPHFESLTG KEKFLESVET VKEYIRAGDV
250 260 270 280 290 300
MQVVPGHRMV SDFDGDPLQV YRALRHLNPS PYLFLVQGHT LTDNTPFHIV GSSPEILSRL
310 320 330 340 350 360
EDGIATVRPL AGTRPRGKTK EEDLALEQEL LADEKEIAEH LMLIDLGRND VGRVSKIGKV
370 380 390 400 410 420
QVTDRMVIER YSHVMHIVSN VQGEVRDDID ALDVFKATFP AGTLSGAPKI RAMEIIDEVE
430 440 450 460 470 480
PVKRGIFGGA VGYLGWHGEM DMSIAIRTCV IRENKVYVQA GAGLVADSNP ESEWNETQIK
490
ARAVIKAVEL SSNGLIL