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 P40390

Entry ID Method Resolution Chain Position Source
AF-P40390-F1 Predicted AlphaFoldDB

No variants for P40390

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P40390

No associated diseases with P40390

5 regional properties for P40390

Type Name Position InterPro Accession
active_site Thiolase, active site 374 - 387 IPR020610
conserved_site Thiolase, conserved site 339 - 355 IPR020613
active_site Thiolase, acyl-enzyme intermediate active site 84 - 102 IPR020615
domain Thiolase, N-terminal 4 - 262 IPR020616
domain Thiolase, C-terminal 270 - 392 IPR020617

Functions

Description
EC Number 5.4.2.2 Phosphotransferases (phosphomutases)
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphoglucomutase activity Catalysis of the reaction: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.

1 GO annotations of biological process

Name Definition
glucose metabolic process The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASITRDIFK AYDIRGIVGK TLTDDAAYFI GRAIAAKAAE KGIARIALGR DGRLSGPELM
70 80 90 100 110 120
EHIQRGLTDS GISVLNVGMV TTPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT
130 140 150 160 170 180
LAGEAIQELL AIVEKDGFVA ADKQGSVTEK DISGAYHDHI VGHVKLKRPI NIAIDAGNGV
190 200 210 220 230 240
GGAFAGKLYK GLGNEVTELF CEVDGNFPNH HPDPSKPENL QDLIAALKNG DAEIGLAFDG
250 260 270 280 290 300
DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGEAIM
310 320 330 340 350 360
EKTGHSFIKS AMKKTGALVA GEMSGHVFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL
370 380 390 400 410 420
DNLPQSISTP ELNISLPEGS NGHQVIEELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA
430 440 450
SNTTPILVLR FEADTQAAIE RIQNRFKAVI ESNPHLIWPL