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 B0UU89

Entry ID Method Resolution Chain Position Source
AF-B0UU89-F1 Predicted AlphaFoldDB

No variants for B0UU89

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0UU89

No associated diseases with B0UU89

4 regional properties for B0UU89

Type Name Position InterPro Accession
domain Glycoside hydrolase, family 13, N-terminal 125 - 207 IPR004193
domain Glycosyl hydrolase, family 13, catalytic domain 247 - 606 IPR006047
domain Alpha-amylase/branching enzyme, C-terminal all beta 630 - 727 IPR006048
domain Glycogen branching enzyme GlgB, N-terminal Early set domain 118 - 220 IPR044143

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
MNKFVSQSTI DTFFDGEHAD PFSVLGMHET SNGIEVRVLL PDAEKVFVLS KETKNVLCEL
70 80 90 100 110 120
LRVDERGFFA GVVPNTHSFF AYQLEVYWGN EAQVIEDPYA FHPMINELDN WLLAEGSHKR
130 140 150 160 170 180
PYEILGAHFT ECDNVAGVNF RLWAPNAKRV SVVGDFNYWD GRRHPMRFHQ SSGIWELFLP
190 200 210 220 230 240
KVSLGQLYKF ELLDCHNQLR LKADPYAFSS QLRPDTASQI GALPEIVSMT EKRRKANQAD
250 260 270 280 290 300
QPISIYEVHL GSWRRNLENN FWLDYDQIAE ELIPYVKDMG FTHIELLPLS EFPFDGSWGY
310 320 330 340 350 360
QPIGLYSPTS RFGTAEGFKR LVNKAHKAGI NVILDWVPGH FPSDTHGLVA FDGTALYEHA
370 380 390 400 410 420
DPKEGYHQDW NTLIYNYGRH EVKNYLASNA LYWMERFGLD GIRVDAVASM IYRDYSREDG
430 440 450 460 470 480
QWIPNQYGGR ENLEAIEFLK QTNHLLGTEI PGVVSIAEES TSFAGVTHPP YEGGLGFHFK
490 500 510 520 530 540
WNMGWMNDTL SYMKKDPIYR QHHHSQMTFG MVYQYSENFI LPLSHDEVVH GKCSLLGKMP
550 560 570 580 590 600
GDAWQKFANL RAYYGYMWGY PGKKLLFMGN EFAQGREWNY QESLDWYLLD EFHGGGWHKA
610 620 630 640 650 660
IQDYVRDLNH IYQKNAPLFE LDTDPQGFEW LVVDDYQNSV FVFERRSKKD ERIIVVSNFT
670 680 690 700 710 720
PVLRQNYRFG VNIAGEYLEI LNSDAQQYMG SNSTNTSKIV TEDIESHNKA QSISIDIPPL
730 740 750 760 770 780
ATVYLKLHKV KKVRKMRKTS KVEDTAVKTE KKIAKGKTTR TKKTVADTVS EATEVKPKKT
790 800 810
VTKRAVVKKV KNEESAVFPN AEVIAESTSV ENNVS