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 D7BMJ2

Entry ID Method Resolution Chain Position Source
AF-D7BMJ2-F1 Predicted AlphaFoldDB

No variants for D7BMJ2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D7BMJ2

No associated diseases with D7BMJ2

5 regional properties for D7BMJ2

Type Name Position InterPro Accession
domain Alpha-D-phosphohexomutase, C-terminal 373 - 443 IPR005843
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain I 3 - 134 IPR005844
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain II 166 - 253 IPR005845
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain III 257 - 366 IPR005846
conserved_site Alpha-D-phosphohexomutase, conserved site 95 - 104 IPR016066

Functions

Description
EC Number 2.4.99.16 Transferring other glycosyl groups
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
hexosyltransferase activity Catalysis of the transfer of a hexosyl group from one compound (donor) to another (acceptor).
hydrolase activity, hydrolyzing O-glycosyl compounds Catalysis of the hydrolysis of any O-glycosyl bond.

1 GO annotations of biological process

Name Definition
alpha-glucan biosynthetic process The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSTLQHKTSS ARRSSRRSVA APDFVAVSRI PIVEVSPQLL DGTAPVKSTV DESFPVQATI
70 80 90 100 110 120
FREGHDKFAA RAVLVDGAGH TVDSVPMCDV SPGLFRFEGW LTPRVPGPHR FFVEAWSDPY
130 140 150 160 170 180
ATWLHNAEIK VPAGIDVGLV FAEAEVLFKA ALKGTPVRSG ERAAIRDALT VISKRRALPE
190 200 210 220 230 240
VKLAAARSEE VRAAFAAYPV KELVSRSREY PVFVDRVRAL VGSWYELFPR SVGATRDSES
250 260 270 280 290 300
GEWTSGTLRT AATDLDRVAG MGFDVVYIPP VHPIGLTNRK GRNNSLTAVP GDPGSPYAIG
310 320 330 340 350 360
SDAAGGHDAI EPSLGTFEDF DVFVGRAHEL GMEVALDLAL QCSPDHPWVK EHPEWFTARP
370 380 390 400 410 420
DGTIAYAENP PKKYQDIYPL NFDNDPEGIY KEIKRVVELW VAHGVTIFRV DNPHTKPVGF
430 440 450 460 470 480
WQRLLAEFRV EHPEVIFLAE AFTNPPMMQT LGTVGFHQSY TYFTWRNERQ EIEEYLMEVS
490 500 510 520 530 540
HESSHRMRPA FWPTTHDILT PYIQRGGISA AAIRAILAAT GSPTWGIYNG YELIENIARP
550 560 570 580 590 600
GAEEHIDNEK YEFKPRNYAL AEQNGMATLL TMLNSIRSKH KALQRLRNVT INPTSNDKIV
610 620 630 640 650 660
SFTKVARPEE TADGVMDAVI VVVNLDPYAS RDATVYLDLS PFGISPRWDG GPIIEVTDEM
670 680 690
SGETYLWNEA PYVHLDPHGQ VAHVLSVKVL S