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 Q1JH49

Entry ID Method Resolution Chain Position Source
AF-Q1JH49-F1 Predicted AlphaFoldDB

No variants for Q1JH49

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1JH49

No associated diseases with Q1JH49

4 regional properties for Q1JH49

Type Name Position InterPro Accession
domain Nucleotidyl transferase domain 16 - 283 IPR005835
conserved_site ADP-glucose pyrophosphorylase, conserved site 19 - 38 IPR005836-1
conserved_site ADP-glucose pyrophosphorylase, conserved site 106 - 114 IPR005836-2
conserved_site ADP-glucose pyrophosphorylase, conserved site 204 - 214 IPR005836-3

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 RGEANVELTP ELAFKLGRFG GYVLSQHETE RPKVFVARDT RISGEMLESA
70 80 90 100 110 120
LIAGLLSVGI EVYKLGVLAT PGVSYLVRTE KASAGVMISA SHNPALDNGI KFFGNDGFKL
130 140 150 160 170 180
ADDQELEIEA LLDAPEDTLP RPSAEGLGTL VDYPEGLRKY EKFLVTTGTD LSGMTVALDT
190 200 210 220 230 240
ANGAASVSAR DVFLDLNAEI AVIGEKPNGL NINDGVGSTH PEQLQELVKE TGADLGLAFD
250 260 270 280 290 300
GDSDRLIAVD ETGEIVDGDR IMFIIGKYLS EKGLLAHNTI VTTVMSNLGF HKALDKQGIN
310 320 330 340 350 360
KAITAVGDRY VVEEMRSSGY NLGGEQSGHV IIMDYNTTGD GQLTAIQLAK VMKETGKSLS
370 380 390 400 410 420
ELAAEVTIYP QKLVNIRVEN SMKDRAMEVP AIANIIAKME DEMAGNGRIL VRPSGTEPLL
430 440 450
RVMAEAPTDA EVDYYVDTIA DVVRTEIGCD N