P53535 (PHSL2_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic
EC=2.4.1.1

Alternative name(s):
Starch phosphorylase L-2

Gene names

Name:

STP-1

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	974 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor	Pyridoxal phosphate.
Subcellular location	Plastid › chloroplast. Plastid › amyloplast.
Tissue specificity	Leaves.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Amyloplast Chloroplast Plastid
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphorylase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P04045	2	EBI-780968,EBI-780963

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 81	81	Chloroplast Potential
	Chain	82 – 974	893	Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic		PRO_0000012293
Amino acid modifications
	Modified residue	820	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53535 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5EF8A23C237463D8	FASTA	974	110,700
	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

References

[1]	"A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis." Sonnewald U., Basner A., Greve B., Steup M. Plant Mol. Biol. 27:567-576(1995) [PubMed: 7894019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73684 mRNA. Translation: CAA52036.1.
PIR	S34189. S53489.
3D structure databases
ProteinModelPortal	P53535.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53535. 2 interactions.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. Glyco_trans_35. 1 hit.
Pfam	PF00343. Phosphorylase. 2 hits. [Graphical view]
PIRSF	PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMs	TIGR02093. P_ylase. 1 hit.
PROSITE	PS00102. PHOSPHORYLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHSL2_SOLTU

Accession

Primary (citable) accession number: P53535

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program