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 Q6DDT1

Entry ID Method Resolution Chain Position Source
AF-Q6DDT1-F1 Predicted AlphaFoldDB

No variants for Q6DDT1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6DDT1

No associated diseases with Q6DDT1

1 regional properties for Q6DDT1

Type Name Position InterPro Accession
domain Myo-inositol-1-phosphate synthase, GAPDH-like 304 - 417 IPR013021

Functions

Description
EC Number 5.5.1.4 Intramolecular lyases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 GO annotations of molecular function

Name Definition
inositol-3-phosphate synthase activity Catalysis of the reaction: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate. This reaction requires NAD, which dehydrogenates the CHOH group to CO at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the aldehyde at C-1. Finally, the enzyme-bound NADH reconverts C-5 into the CHOH form.

2 GO annotations of biological process

Name Definition
inositol biosynthetic process The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAEMFKVESP HVRYLKDVIE ADYSYDTTQV YEEKGVTKVK PCSTKFTFHT ERKVPKLGVM
70 80 90 100 110 120
LVGWGGNNGT TVTAAVLANR LGLSWMTKTG KKVANYYGSL FQSSTVCLGR GSSGEVFVPF
130 140 150 160 170 180
RDLLPMVNPN DLVFDGWDIS SLNLADAMFR AEVLDWQLQE QLRPYMEKMK PRPSIYIPEF
190 200 210 220 230 240
IAANQEDRAD HTIHGTKAEQ VQKIREDIQD FKRTSGVDKV IVLWTANTER FCDIIPGVND
250 260 270 280 290 300
TADNLLKAIE NGLEVSPSTM FAVASILEGC AFINGSPQNT FVPGAIELAI RHNVFIGGDD
310 320 330 340 350 360
FKSGQTKIKS VLMDFLVSAG LKPVSIVSYN HLGNNDGKNL SAPQQFRSKE ISKSNVVDDM
370 380 390 400 410 420
VQSNPILYGP NEKPDHCVVI KYVPYVGDSK RAMDEYTSEI MMGGANTIVL HNTCEDSLLA
430 440 450 460 470 480
SPIFLDLVLL TELCQRITFR TETDQEFQTF HSVLSILSFL CKAPLVPAGT PVVNAFFRQR
490 500 510 520 530 540
NCIENILRAC LGLSPQNHMM LEHKMQRSFV SLKRPSVDCN AYPISSKKGN GVNGFHPPGI
550 560
SNGLSHSNGL GKTVISSDIE IEN