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 Q9AEM9

Entry ID Method Resolution Chain Position Source
AF-Q9AEM9-F1 Predicted AlphaFoldDB

No variants for Q9AEM9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9AEM9

No associated diseases with Q9AEM9

4 regional properties for Q9AEM9

Type Name Position InterPro Accession
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal 605 - 802 IPR018969
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal 17 - 381 IPR018970
binding_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site 166 - 184 IPR019789
conserved_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site 153 - 159 IPR019790

Functions

Description
EC Number 4.1.2.9 Aldehyde-lyases
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
fructose-6-phosphate phosphoketolase activity Catalysis of the reaction: D-fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H2O.
phosphoketolase activity Catalysis of the reaction: D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O.

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
MTNPVIGTPW QKLDRPVSEE AIEGMDKYWR VANYMSIGQI YLRSNPLMKE PFTRDDVKHR
70 80 90 100 110 120
LVGHWGTTPG LNFLLAHINR LIADHQQNTV FIMGPGHGGP AGTAQSYIDG TYTEYYPNIT
130 140 150 160 170 180
KDEAGLQKFF RQFSYPGGIP SHFAPETPGS IHEGGELGYA LSHAYGAIMD NPSLFVPCII
190 200 210 220 230 240
GDGEAETGPL ATGWQSNKLV NPRTDGIVLP ILHLNGYKIA NPTILARISD EELHDFFRGM
250 260 270 280 290 300
GYHPYEFVAG FDNEDHLSIH RRFAELFETI FDEICDIKAA AQTDDMTRPF YPMLIFRTPK
310 320 330 340 350 360
GWTCPKFIDG KKTEGSWRAH QVPLASARDT EAHFEVLKGW MESYKPEELF NADGSIKEDV
370 380 390 400 410 420
TAFMPKGELR IGANPNANGG RIREDLKLPE LDQYEITGVK EYGHGWGQVE APRSLGAYCR
430 440 450 460 470 480
DIIKNNPDSF RVFGPDETAS NRLNATYEVT KKQWDNGYLS ALVDENMAVT GQVVEQLSEH
490 500 510 520 530 540
QCEGFLEAYL LTGRHGIWSS YESFVHVIDS MLNQHAKWLE ATVREIPWRK PISSVNLLVS
550 560 570 580 590 600
SHVWRQDHNG FSHQDPGVTS VLLNKTFNND HVTNIYFATD ANMLLAIAEK CFKSTNKINA
610 620 630 640 650 660
IFAGKQPAAT WITLDEVRAE LEAGAAEWKW ASNAKSNDEV QVVLAAAGDV PTQEIMAASD
670 680 690 700 710 720
ALNKMGIKFK VVNVVDLIKL QSSKENDEAM SDEDFADLFT ADKPVLFAYH SYAQDVRGLI
730 740 750 760 770 780
YDRPNHDNFT VVGYKEQGST TTPFDMVRVN DMDRYALQAK ALELIDADKY ADKINELNEF
790 800 810 820
RKTAFQFAVD NGYDIPEFTD WVYPDVKVDE TSMLSATAAT AGDNE