P04045

PR
Gene name
Protein name
Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic
Names
Starch phosphorylase L-1
Species
Solanum tuberosum (Potato)
KEGG Pathway
sot:102596766
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)

25-99 (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 P04045

Entry ID Method Resolution Chain Position Source
AF-P04045-F1 Predicted AlphaFoldDB

No variants for P04045

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P04045

No associated diseases with P04045

1 regional properties for P04045

Type Name Position InterPro Accession
domain Amine oxidase 62 - 499 IPR002937

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.

5 GO annotations of molecular function

Name Definition
glycogen phosphorylase activity Catalysis of the reaction: glycogen + phosphate = maltodextrin + alpha-D-glucose 1-phosphate.
identical protein binding Binding to an identical protein or proteins.
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
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
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
P53535 STP-1 Alpha-1,4 glucan phosphorylase L-2 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
MATANGAHLF NHYSSNSRFI HFTSRNTSSK LFLTKTSHFR RPKRCFHVNN TLSEKIHHPI
70 80 90 100 110 120
TEQGGESDLS SFAPDAASIT SSIKYHAEFT PVFSPERFEL PKAFFATAQS VRDSLLINWN
130 140 150 160 170 180
ATYDIYEKLN MKQAYYLSME FLQGRALLNA IGNLELTGAF AEALKNLGHN LENVASQEPD
190 200 210 220 230 240
AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ RITKDGQEEV AEDWLEIGSP
250 260 270 280 290 300
WEVVRNDVSY PIKFYGKVST GSDGKRYWIG GEDIKAVAYD VPIPGYKTRT TISLRLWSTQ
310 320 330 340 350 360
VPSADFDLSA FNAGEHTKAC EAQANAEKIC YILYPGDESE EGKILRLKQQ YTLCSASLQD
370 380 390 400 410 420
IISRFERRSG DRIKWEEFPE KVAVQMNDTH PTLCIPELMR ILIDLKGLNW NEAWNITQRT
430 440 450 460 470 480
VAYTNHTVLP EALEKWSYEL MQKLLPRHVE IIEAIDEELV HEIVLKYGSM DLNKLEEKLT
490 500 510 520 530 540
TMRILENFDL PSSVAELFIK PEISVDDDTE TVEVHDKVEA SDKVVTNDED DTGKKTSVKI
550 560 570 580 590 600
EAAAEKDIDK KTPVSPEPAV IPPKKVRMAN LCVVGGHAVN GVAEIHSEIV KEEVFNDFYE
610 620 630 640 650 660
LWPEKFQNKT NGVTPRRWIR FCNPPLSAII TKWTGTEDWV LKTEKLAELQ KFADNEDLQN
670 680 690 700 710 720
EWREAKRSNK IKVVSFLKEK TGYSVVPDAM FDIQVKRIHE YKRQLLNIFG IVYRYKKMKE
730 740 750 760 770 780
MTAAERKTNF VPRVCIFGGK AFATYVQAKR IVKFITDVGA TINHDPEIGD LLKVVFVPDY
790 800 810 820 830 840
NVSVAELLIP ASDLSEHIST AGMEASGTSN MKFAMNGCIQ IGTLDGANVE IREEVGEENF
850 860 870 880 890 900
FLFGAQAHEI AGLRKERADG KFVPDERFEE VKEFVRSGAF GSYNYDDLIG SLEGNEGFGR
910 920 930 940 950 960
ADYFLVGKDF PSYIECQEKV DEAYRDQKRW TTMSILNTAG SYKFSSDRTI HEYAKDIWNI
EAVEIA