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 Q88S87

Entry ID Method Resolution Chain Position Source
AF-Q88S87-F1 Predicted AlphaFoldDB

No variants for Q88S87

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q88S87

No associated diseases with Q88S87

4 regional properties for Q88S87

Type Name Position InterPro Accession
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal 594 - 792 IPR018969
domain Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal 14 - 374 IPR018970
binding_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site 162 - 180 IPR019789
conserved_site Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site 149 - 155 IPR019790

Functions

Description
EC Number
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
aldehyde-lyase activity Catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone.

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
MSEAIKSKTV DYSSDEYLKR VDEYWRAANY ISVGQLYLLN NPLLREPLKA TDVKVHPIGH
70 80 90 100 110 120
WGTIAGQNFI YAHLNRAINK YGLNMFYIEG PGHGGQVMVS NSYLDGTYTE TYPKITQDKA
130 140 150 160 170 180
GMKRLFKQFS FPGGVASHAD PKTPGSIHEG GELGYSILHG AGAVLDNPGL IAATVVGDGE
190 200 210 220 230 240
SETGPLATSW QVNKFLNPIT DGTVLPILNL NGFKISNPTV LSRESHEELE DYFKGLGWDP
250 260 270 280 290 300
HFVEGTDPAK MHKIMAEELD KVIEEIHAIR KNAKDNNDES RPKWPMIVFR APKGWTGPKS
310 320 330 340 350 360
WDGEPIEGSF RAHQIPIPVD RNHMEHADKL VDWLKSYKPE ELFDENGTLK PEIAAIIPEG
370 380 390 400 410 420
QARMAANPVT NGGKLTKDLI TPNIDDYALD NKSHGKEDGS DMTELGKYIR DLIELNKDNK
430 440 450 460 470 480
NFRGWGPDET LSNKLGAAFE DTKRQWMEPI HEPNDALLAP QGRIIDSMLS EHMDEGMLEA
490 500 510 520 530 540
YNLTGRYGFF ASYESFLRVV DSMLTQHFKW LRNSHEETPW RADVPSLNVI ASSTAFQQDH
550 560 570 580 590 600
NGYSHQDPGI ISHLAEKKTE YVRAYLPGDA NTLIATFDKA IQSKQLINLI IASKHPRPQW
610 620 630 640 650 660
FTMDEAKRLV RDGLGVVDWA STDHGEEPDV VFATAGSEPT TESLAAVSIL HARFPEMKIR
670 680 690 700 710 720
FINVVDLLKL KKDDPRGLSD AEFDAFFTKD KPVIFAYHAY DDLVKTIFFD RHNHNLHVHG
730 740 750 760 770 780
YREEGDITTP FDMRVRNELD RFHLVKAALL ATPAYAEKGA HVIQEMNSIL DKHHDYIRAE
790
GTDIPEVENW KWTALK