Reviewed, UniProtKB/Swiss-Prot P04045 (PHSL1_SOLTU)

Names and origin

Protein names	Recommended name:     Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic     EC=2.4.1.1 Alternative name(s):     Starch phosphorylase L-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	966 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	Tuber.
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 Direct protein sequencing
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	identical protein binding Inferred from physical interaction. Source: IntAct phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-780963,EBI-780963
STP-1	P53535	1	EBI-780963,EBI-780968

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 50	50	Chloroplast Ref.3 Ref.4
	Chain	51 – 966	916	Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic		PRO_0000012292
Amino acid modifications
	Modified residue	812	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	159	1	A → D in CAA36612. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P04045-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: A7758860A790793A	FASTA	966	109,506
	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

References

[1]	"Molecular cloning of cDNA encoding potato amyloplast alpha-glucan phosphorylase and the structure of its transit peptide." Nakano K., Mori H., Fukui T. J. Biochem. 106:691-695(1989) [PubMed: 2481677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Occurrence of a copia-like transposable element in one of the introns of the potato starch phosphorylase gene." Camirand A., St Pierre B., Marineau C., Brisson N. Mol. Gen. Genet. 224:33-39(1990) [PubMed: 1703627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Kennebec.
[3]	"The complete amino acid sequence of potato alpha-glucan phosphorylase." Nakano K., Fukui T. J. Biol. Chem. 261:8230-8236(1986) [PubMed: 3722153] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-966.
[4]	"Structural basis for the difference of the regulatory properties between potato and rabbit muscle phosphorylases. The NH2-terminal sequence of the potato enzyme." Nakano K., Fukui T., Matsubara H. J. Biol. Chem. 255:9255-9261(1980) [PubMed: 7410423] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-131.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00520 mRNA. Translation: BAA00407.1. X52385 mRNA. Translation: CAA36612.1.
PIR	PHPOAG. JU0130.
3D structure databases
HSSP	HSSP built from PDB template 1YGP based on UniProtKB P06738.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04045. 2 interactions.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Enzyme and pathway databases
BRENDA	2.4.1.1. 296.
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

PHSL1_SOLTU

Accession

Primary (citable) accession number: P04045

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)