P53535

PR
Gene name
STP-1
Protein name
Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic
Names
Starch phosphorylase L-2
Species
Solanum tuberosum (Potato)
KEGG Pathway
sot:102603391
EC number
2.4.1.1: Hexosyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-99 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P53535

Entry ID Method Resolution Chain Position Source
AF-P53535-F1 Predicted AlphaFoldDB

No variants for P53535

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P53535

No associated diseases with P53535

1 regional properties for P53535

Type Name Position InterPro Accession
conserved_site Phosphorylase pyridoxal-phosphate attachment site 812 - 824 IPR035090

Functions

Description
EC Number 2.4.1.1 Hexosyltransferases
Subcellular Localization
  • Plastid, chloroplast
  • Plastid, amyloplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
amyloplast A plastid whose main function is to synthesize and store starch.
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
glycogen phosphorylase activity Catalysis of the reaction: glycogen + phosphate = maltodextrin + alpha-D-glucose 1-phosphate.
linear malto-oligosaccharide phosphorylase activity Catalysis of the reaction: hydrogenphosphate + a linear malto-oligosaccharide = alpha-D-glucose 1-phosphate + a linear malto-oligosaccharide.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
SHG alpha-glucan phosphorylase activity Catalysis of the reaction: hydrogenphosphate + a plant soluble heteroglycan = alpha-D-glucose 1-phosphate + a plant soluble heteroglycan.

1 GO annotations of biological process

Name Definition
glycogen catabolic process The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.

14 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P06738 GPH1 Glycogen phosphorylase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q0VCM4 PYGL Glycogen phosphorylase, liver form Bos taurus (Bovine) PR
P11216 PYGB Glycogen phosphorylase, brain form Homo sapiens (Human) PR
P06737 PYGL Glycogen phosphorylase, liver form Homo sapiens (Human) PR
P11217 PYGM Glycogen phosphorylase, muscle form Homo sapiens (Human) PR
Q8CI94 Pygb Glycogen phosphorylase, brain form Mus musculus (Mouse) PR
Q9ET01 Pygl Glycogen phosphorylase, liver form Mus musculus (Mouse) PR
Q9WUB3 Pygm Glycogen phosphorylase, muscle form Mus musculus (Mouse) PR
P04045 Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic Solanum tuberosum (Potato) PR
P32811 Alpha-glucan phosphorylase, H isozyme Solanum tuberosum (Potato) PR
P09811 Pygl Glycogen phosphorylase, liver form Rattus norvegicus (Rat) PR
P09812 Pygm Glycogen phosphorylase, muscle form Rattus norvegicus (Rat) PR
Q9SD76 PHS2 Alpha-glucan phosphorylase 2, cytosolic Arabidopsis thaliana (Mouse-ear cress) PR
Q9LIB2 PHS1 Alpha-glucan phosphorylase 1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MATFAVSGLN SISSISSFNN NFRSKNSNIL LSRRRILLFS FRRRRRSFSV SSVASDQKQK
70 80 90 100 110 120
TKDSSSDEGF TLDVFQPDST SVLSSIKYHA EFTPSFSPEK FELPKAYYAT AESVRDTLII
130 140 150 160 170 180
NWNATYEFYE KMNVKQAYYL SMEFLQGRAL LNAIGNLGLT GPYADALTKL GYSLEDVARQ
190 200 210 220 230 240
EPDAALGNGG LGRLASCFLD SMATLNYPAW GYGLRYQYGL FKQLITKDGQ EEVAENWLEM
250 260 270 280 290 300
GNPWEIVRND ISYPVKFYGK VIEGADGRKE WAGGEDITAV AYDVPIPGYK TKTTINLRLW
310 320 330 340 350 360
TTKLAAEAFD LYAFNNGDHA KAYEAQKKAE KICYVLYPGD ESLEGKTLRL KQQYTLCSAS
370 380 390 400 410 420
LQDIIARFEK RSGNAVNWDQ FPEKVAVQMN DTHPTLCIPE LLRILMDVKG LSWKQAWEIT
430 440 450 460 470 480
QRTVAYTNHT VLPEALEKWS FTLLGELLPR HVEIIAMIDE ELLHTILAEY GTEDLDLLQE
490 500 510 520 530 540
KLNQMRILDN VEIPSSVLEL LIKAEESAAD VEKAADEEQE EEGKDDSKDE ETEAVKAETT
550 560 570 580 590 600
NEEEETEVKK VEVEDSQAKI KRIFGPHPNK PQVVHMANLC VVSGHAVNGV AEIHSEIVKD
610 620 630 640 650 660
EVFNEFYKLW PEKFQNKTNG VTPRRWLSFC NPELSEIITK WTGSDDWLVN TEKLAELRKF
670 680 690 700 710 720
ADNEELQSEW RKAKGNNKMK IVSLIKEKTG YVVSPDAMFD VQIKRIHEYK RQLLNIFGIV
730 740 750 760 770 780
YRYKKMKEMS PEERKEKFVP RVCIFGGKAF ATYVQAKRIV KFITDVGETV NHDPEIGDLL
790 800 810 820 830 840
KVVFVPDYNV SVAEVLIPGS ELSQHISTAG MEASGTSNMK FSMNGCLLIG TLDGANVEIR
850 860 870 880 890 900
EEVGEDNFFL FGAQAHEIAG LRKERAEGKF VPDPRFEEVK AFIRTGVFGT YNYEELMGSL
910 920 930 940 950 960
EGNEGYGRAD YFLVGKDFPD YIECQDKVDE AYRDQKKWTK MSILNTAGSF KFSSDRTIHQ
970
YARDIWRIEP VELP