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 B0B998

Entry ID Method Resolution Chain Position Source
AF-B0B998-F1 Predicted AlphaFoldDB

No variants for B0B998

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0B998

No associated diseases with B0B998

5 regional properties for B0B998

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 2.4.1.18 Hexosyltransferases
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

4 GO annotations of molecular function

Name Definition
1,4-alpha-glucan branching enzyme activity Catalysis of the transfer of a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxyl group in a similar glucan chain.
1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) Catalysis of the reaction: a glucosylated glycogenin = a glycogen.
cation binding Binding to a cation, a charged atom or group of atoms with a net positive charge.
hydrolase activity, hydrolyzing O-glycosyl compounds Catalysis of the hydrolysis of any O-glycosyl bond.

1 GO annotations of biological process

Name Definition
glycogen biosynthetic process The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDPFFLNTQH VELLVSGKQS SPQDLLGIVS ESLNQDRIVL FRPGAETVFV ELRGKIQQAE
70 80 90 100 110 120
SHHSGIFSLP VMKGISPQDY RVYHQNGLLA HDPYAFPLLW GEIDSFLFHE GTHQRIYERM
130 140 150 160 170 180
GAIPCEIDGV PGVRFIVWAP HAQRVSVIGD FNGWHGLVNP LHKVSDQGVW ELFVPGLTAG
190 200 210 220 230 240
ACYKWEMVTE SGQVLIKSDP YGKFFGPPPR SVSVVIDDSY EWNDSEWLEE RIKKTEGPMN
250 260 270 280 290 300
IYEVHVGSWQ WQEGQPLNYK ELADQLALYC KQMHYTHVEL LPVTEHPLNE SWGYQTTGYY
310 320 330 340 350 360
APTSRYGSFE DLQYFIDTMH QHGIGVILDW VPGHFPIDSF AMSGFDGTPL YEYTRNPSPL
370 380 390 400 410 420
HPHWHTYTFD YAKPEVCNFL LGSALFWIDK MHVDGIRVDA VSSMLYLDYG RYAGEWVPNR
430 440 450 460 470 480
YGGRENLDAI RFLQQFNTVI HEKYPGVLTF AEESTTFPKI TVSVEEGGLG FDYKWNMGWM
490 500 510 520 530 540
HDTLHYFEKD FPYRPYHQSD LTFPQWYAFS ERFLLPFSHD EVVHGKRSLI GKMPGDAWRQ
550 560 570 580 590 600
FAQLRLLLGY QICQPGKKLL FMGGEFGQGR EWSPGRELDW ELLDISYHQG VHLCSQELNA
610 620 630 640 650 660
LYVQSPQLWQ ADHLPSSFRW VDFSDVRNGV VAYLRFADAD AKKALLCVHH FGVGYFPHYL
670 680 690 700 710 720
LPILPLESCD LLMNTDNTRF GGSGKGFREP EILTPEIARQ EREAAGLIEA DDESGPDCWG
730
LDIELPPSAT LIFSVTLQ