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 P23669

Entry ID Method Resolution Chain Position Source
AF-P23669-F1 Predicted AlphaFoldDB

No variants for P23669

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P23669

No associated diseases with P23669

3 regional properties for P23669

Type Name Position InterPro Accession
binding_site Serine/threonine dehydratase, pyridoxal-phosphate-binding site 108 - 122 IPR000634
domain Tryptophan synthase beta chain-like, PALP domain 99 - 338 IPR001926
domain Threonine synthase, N-terminal 3 - 84 IPR029144

Functions

Description
EC Number 4.2.3.1 Acting on phosphates
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
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
threonine synthase activity Catalysis of the reaction: O-phospho-L-homoserine + H2O = L-threonine + phosphate.

1 GO annotations of biological process

Name Definition
threonine biosynthetic process The chemical reactions and pathways resulting in the formation of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDYISTRDAS RTPARFSDIL LGGLAPDGGL YLPATYPQLD DAQLSKWREV LANEGYAALA
70 80 90 100 110 120
AEVISLFVDD IPVEDIKAIT ARAYTYPKFN SEDIVPVTEL EDNIYLGHLS EGPTAAFKDM
130 140 150 160 170 180
AMQLLGELFE YELRRRNETI NILGATSGDT GSSAEYAMRG REGIRVFMLT PAGRMTPFQQ
190 200 210 220 230 240
AQMFGLDDPN IFNIALDGVF DDCQDVVKAV SADAEFKKDN RIGAVNSINW ARLMAQVVYY
250 260 270 280 290 300
VSSWIRTTTS NDQKVSFSVP TGNFGDICAG HIARQMGLPI DRLIVATNEN DVLDEFFRTG
310 320 330 340 350 360
DYRVRSSADT HETSSPSMDI SRASNFERFI FDLLGRDATR VNDLFGTQVR QGGFSLADDA
370 380 390 400 410 420
NFEKAAAEYG FASGRSTHAD RVATIADVHS RLDVLIDPHT ADGVHVARQW RDEVNTPIIV
430 440 450 460 470 480
LETALPVKFA DTIVEAIGEA PQTPERFAAI MDAPFKVSDL PNDTDAVKQY IVDAIANTSV
K