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 Q65P47

Entry ID Method Resolution Chain Position Source
AF-Q65P47-F1 Predicted AlphaFoldDB

No variants for Q65P47

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q65P47

No associated diseases with Q65P47

5 regional properties for Q65P47

Type Name Position InterPro Accession
domain Alpha-D-phosphohexomutase, C-terminal 373 - 441 IPR005843
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain I 3 - 134 IPR005844
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain II 158 - 253 IPR005845
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain III 257 - 368 IPR005846
conserved_site Alpha-D-phosphohexomutase, conserved site 94 - 103 IPR016066

Functions

Description
EC Number 5.4.2.10 Phosphotransferases (phosphomutases)
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
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphoglucosamine mutase activity Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.

1 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKER PKVLIGRDTR ISGHMLEGAL
70 80 90 100 110 120
VAGLLSIGAE VMRLGVISTP GVAYLTKAMD AEAGVMISAS HNPVQDNGIK FFGGDGFKLS
130 140 150 160 170 180
DEQELEIERL MDQPEDHLPR PVGADLGMVN DYFEGGQKYL QFLKQSADED FTGIHVALDC
190 200 210 220 230 240
AHGATSSLAT HLFADLDADV STMGTSPNGL NINDGVGSTH PEALAEFVKE KGADVGMAFD
250 260 270 280 290 300
GDGDRLIAVD EKGNIVDGDQ IMYICAKYLK SEGRLTDNTV VSTVMSNLGF YKALEAEGIK
310 320 330 340 350 360
SVQTAVGDRY VVEAMKKGGF TLGGEQSGHL IFLDYNTTGD GLLSAIMLMN TIKMTGKPLS
370 380 390 400 410 420
ELAAEMQKFP QLLLNVKVTD KHKVTENEKV KAVIEEVEKE MNGDGRILVR PSGTEPLVRV
430 440
MAEAKTKELC EKYVGRIADV VKAEMGAE