P06738

PR
Gene name
GPH1 (YPR160W, P9584.1)
Protein name
Glycogen phosphorylase
Names
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YPR160W
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)

1-90 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for P06738

Entry ID Method Resolution Chain Position Source
1YGP X-ray 280 A A/B 24-902 PDB
AF-P06738-F1 Predicted AlphaFoldDB

10 variants for P06738

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-861419 40 S>A No SGRP
s16-861737 146 D>H No SGRP
s16-861767 156 K>E No SGRP
s16-861981 227 Y>C No SGRP
s16-862364 355 Q>E No SGRP
s16-863052 584 K>R No SGRP
s16-863225 642 V>I No SGRP
s16-863240 647 Y>H No SGRP
s16-863259 653 K>R No SGRP
s16-863729 810 V>I No SGRP

No associated diseases with P06738

1 regional properties for P06738

Type Name Position InterPro Accession
conserved_site Phosphorylase pyridoxal-phosphate attachment site 673 - 685 IPR035090

Functions

Description
EC Number 2.4.1.1 Hexosyltransferases
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.

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
Q0VCM4 PYGL Glycogen phosphorylase, liver form Bos taurus (Bovine) PR
P06737 PYGL Glycogen phosphorylase, liver form Homo sapiens (Human) PR
P11216 PYGB Glycogen phosphorylase, brain form Homo sapiens (Human) PR
P11217 PYGM Glycogen phosphorylase, muscle form Homo sapiens (Human) PR
Q9ET01 Pygl Glycogen phosphorylase, liver form Mus musculus (Mouse) PR
Q8CI94 Pygb Glycogen phosphorylase, brain form Mus musculus (Mouse) PR
Q9WUB3 Pygm Glycogen phosphorylase, muscle form Mus musculus (Mouse) PR
P32811 Alpha-glucan phosphorylase, H isozyme Solanum tuberosum (Potato) PR
P53535 STP-1 Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic Solanum tuberosum (Potato) PR
P04045 Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic 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
MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR ALWNKHQVKK
70 80 90 100 110 120
FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR DNLVIDWNKT QQKFTTRDPK
130 140 150 160 170 180
RVYYLSLEFL MGRALDNALI NMKIEDPEDP AASKGKPREM IKGALDDLGF KLEDVLDQEP
190 200 210 220 230 240
DAGLGNGGLG RLAACFVDSM ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN
250 260 270 280 290 300
PWEIERNEVQ IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL
310 320 330 340 350 360
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA
370 380 390 400 410 420
ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL QRVLVDLEKL DWHEAWDIVT
430 440 450 460 470 480
KTFAYTNHTV MQEALEKWPV GLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS
490 500 510 520 530 540
IIEENSPERQ IRMAFLAIVG SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT
550 560 570 580 590 600
PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR
610 620 630 640 650 660
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL AMKNMLKNGA
670 680 690 700 710 720
SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI VNNDESIEHL LKVVFVADYN
730 740 750 760 770 780
VSKAEIIIPA SDLSEHISTA GTEASGTSNM KFVMNGGLII GTVDGANVEI TREIGEDNVF
790 800 810 820 830 840
LFGNLSENVE ELRYNHQYHP QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY
850 860 870 880 890 900
YLVSDDFESY LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP
VT