Reviewed, UniProtKB/Swiss-Prot P27598 (PHSL_IPOBA)

Names and origin

Protein names	Recommended name:     Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic     EC=2.4.1.1 Alternative name(s):     Starch phosphorylase L
Organism	Ipomoea batatas (Sweet potato) (Batate)
Taxonomic identifier	4120 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea

Protein attributes

Sequence length	955 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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 pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Chloroplast Potential
	Chain	44 – 955	912	Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic		PRO_0000012291
Amino acid modifications
	Modified residue	801	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27598-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: CCDB7CD5628A662A	FASTA	955	108,520
	10 20 30 40 50 60 MSRLSGITPR ARDDRSQFQN PRLEIAVPDR TAGLQRTKRT LLVKCVLDET KQTIQHVVTE 70 80 90 100 110 120 KNEGTLLDAA SIASSIKYHA EFSPAFSPER FELPKAYFAT AQSVRDALIV NWNATYDYYE 130 140 150 160 170 180 KLNMKQAYYL SMEFLQGRAL LNAIGNLELT GEYAEALNKL GHNLENVASK EPDAALGNGG 190 200 210 220 230 240 LGRLASCFLD SLATLNYPAW GYGLRYKYGL FKQRITKDGQ EEVAEDWLEL GNPWEIIRMD 250 260 270 280 290 300 VSYPVKFFGK VITGSDGKKH WIGGEDILAV AYDVPIPGYK TRTTISLRLW STKVPSEDFD 310 320 330 340 350 360 LYSFNAGEHT KACEAQANAE KICYILYPGD ESIEGKILRL KQQYTLCSAS LQDIIARFER 370 380 390 400 410 420 RSGEYVKWEE FPEKVAVQMN DTHPTLCIPE LIRILIDLKG LSWKEAWNIT QRTVAYTNHT 430 440 450 460 470 480 VLPEALEKWS YELMEKLLPR HIEIIEMIDE QLINEIVSEY GTSDLDMLEK KLNDMRILEN 490 500 510 520 530 540 FDIPSSIANL FTKPKETSIV DPSEEVEVSG KVVTESVEVS DKVVTESEKD ELEEKDTELE 550 560 570 580 590 600 KDEDPVPAPI PPKMVRMANL CVVGGHAVNG VAEIHSDIVK EDVFNDFYQL WPEKFQNKTN 610 620 630 640 650 660 GVTPRRWIRF CNPALSNIIT KWIGTEDWVL NTEKLAELRK FADNEDLQIE WRAAKRSNKV 670 680 690 700 710 720 KVASFLKERT GYSVSPNAMF DIQVKRIHEY KRQLLNILGI VYRYKQMKEM SAREREAKFV 730 740 750 760 770 780 PRVCIFGGKA FATYVQAKRI AKFITDVGAT INHDPEIGDL LKVIFVPDYN VSAAELLIPA 790 800 810 820 830 840 SGLSQHISTA GMEASGQSNM KFAMNGCILI GTLDGANVEI RQEVGEENFF LFGAEAHEIA 850 860 870 880 890 900 GLRKERAEGK FVPDERFEEV KEFIKRGVFG SNTYDELLGS LEGNEGFGRG DYFLVGKDFP 910 920 930 940 950 SYIECQEKVD EAYRDQKIWT RMSILNTAGS YKFSSDRTIH EYAKDIWNIQ PVVFP

References

[1]	"Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence." Lin C.T., Yeh K.W., Lee P.D., Su J.C. Plant Physiol. 95:1250-1253(1991) [PubMed: 16668119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64362 mRNA. Translation: AAA63271.1.
PIR	T10947.
3D structure databases
HSSP	HSSP built from PDB template 1YGP based on UniProtKB P06738.
ModBase	Search...
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Enzyme and pathway databases
BRENDA	2.4.1.1. 21210.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. Glyco_trans_35. 1 hit.
Pfam	PF00343. Phosphorylase. 1 hit. [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

PHSL_IPOBA

Accession

Primary (citable) accession number: P27598

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)