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 C0ZIM8

Entry ID Method Resolution Chain Position Source
AF-C0ZIM8-F1 Predicted AlphaFoldDB

No variants for C0ZIM8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C0ZIM8

No associated diseases with C0ZIM8

5 regional properties for C0ZIM8

Type Name Position InterPro Accession
domain Alpha-D-phosphohexomutase, C-terminal 375 - 443 IPR005843
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain I 3 - 137 IPR005844
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain II 160 - 255 IPR005845
domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain III 259 - 370 IPR005846
conserved_site Alpha-D-phosphohexomutase, conserved site 96 - 105 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 RGVANTQLTP ELAFKIGRVG GYVLTRHKQE GKPKVVIGRD TRISGQMLEN
70 80 90 100 110 120
ALLAGLLSVG AEVVRLGVIS TSGVAYLTRA LGADAGVMIS ASHNPFPDNG IKFFGSNGFK
130 140 150 160 170 180
LSDEVEAEVE QYLDAAEDTM PRPTGEQIGT VLEFLEGGQK YLSHLKSTVS ERFDGLKVVL
190 200 210 220 230 240
DCANGAVSSL AARLFADVDA EVITIGANPN GININDQCGS THPERLVEEV LKHKADLGLS
250 260 270 280 290 300
FDGDADRCIA VDNNGEIIDG DYIMAICARA LKAKGKLNNN TVVTTVMANM GFFKGMEECS
310 320 330 340 350 360
INTTKTAVGD RYVVEEMLRG GYNLGGEQSG HIVFLDYNTT GDGLLTGLQL LNIIKESGKP
370 380 390 400 410 420
LSELKQVMVK YPQLLINVRV EDKSKLNGNE AIAQAIREVE EDLAGNGRVL VRPSGTEPIV
430 440
RVMAEGPDAA QLEGLVNRIV DVVKQQLV