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 O65979

Entry ID Method Resolution Chain Position Source
AF-O65979-F1 Predicted AlphaFoldDB

No variants for O65979

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O65979

No associated diseases with O65979

3 regional properties for O65979

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 6 - 286 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 141 - 155 IPR017958
domain Asn/Gln amidotransferase 325 - 471 IPR018027

Functions

Description
EC Number 2.4.1.213 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

1 GO annotations of molecular function

Name Definition
glucosylglycerol-phosphate synthase activity Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).

2 GO annotations of biological process

Name Definition
glucosylglycerol biosynthetic process The chemical reactions and pathways resulting in the formation of glucosylglycerol, alpha-D-glucopyranosyl-alpha-(1,2)-glycerol.
trehalose biosynthetic process The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKSSLVILYH REPYDEVREN GKTFYRDKTS PNGIMPTLKS FFANAEQSTW VAWKQISGKQ
70 80 90 100 110 120
QENFQAKMAF PGQENSVVHR IPLSADQVKN FYHITSKEAF WPILHSFPWQ FTYDSSDWEN
130 140 150 160 170 180
FKQINEMFAE AACEDADDDA LFWVHDYNLW LTPYFIRQKK PNAKIAFFHH TPFPSVDIFN
190 200 210 220 230 240
ILPWREAIVD SLLCCDLCGF HLPRYVQNFV AVARSLRKVE ITRQVPVDEH AFTAVGTALA
250 260 270 280 290 300
EPEITTQLKY KDHLVNLDAF PVGTNPTQIR AQVEKASTQE RIRKIREELG SNKLILSAGR
310 320 330 340 350 360
VDYVKGTKEM LVCYERLLER RPELQTKVNL VVAAAKAASG MRVYKNAQSE IERLVGRING
370 380 390 400 410 420
RFAKLNWTPI LLFTSALSYE ELLGFFGAAD IAWITPLRDG LNLVAKEYVV AHGCDDGVLI
430 440 450 460 470 480
LSEFAGSAVE LPDAILTNPY AAKRMDESID QALAMPVEEQ QRRMKSMYQA IQRYDVQQWA
490
NHMFREAKAT AVLGKEPTPV