Reviewed, UniProtKB/Swiss-Prot P53536 (PHSL_VICFA)

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

Gene names

Name:

PHO1

Organism

Vicia faba (Broad bean)

Taxonomic identifier

3906 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Vicia

Protein attributes

Sequence length	1003 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. The L isoform exhibits higher affinity for unbranched substrates such as glucan-like amylose and maltodextrin.
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	Found predominantly in cotyledons and early seed coat.
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 – 64	64	Chloroplast Potential
	Chain	65 – 1003	939	Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic		PRO_0000012294
Amino acid modifications
	Modified residue	849	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53536-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 834E43BBED18535D	FASTA	1,003	113,580
	10 20 30 40 50 60 MASMTMRFHP NSTAVTESVP RRGSVYGFIG YRSSSLFVRT NVIKYRSVKR NLEFRRRSAF 70 80 90 100 110 120 SVKCGSGNEA KQKVKDQEVQ QEAKTSPSSF APDTTSIVSS IKYHAEFTPL FSPEKFELPQ 130 140 150 160 170 180 AFIATAQSVR DALIINWNAT YDYYEKLNVK QAYYLSMEFL QGRALLNAIG NLELTGPYAE 190 200 210 220 230 240 ALSQLSYKLE DVAHQEPDAA LGNGGLGRLA SCFLDSLATL NYPAWGYGLR YKYGLFKQRI 250 260 270 280 290 300 TKDGQEEVAE DWLEMGNPWE IVRNDVSYPV RFYGKVVSGS DGKKHWVGGE DIKAVAHDVP 310 320 330 340 350 360 IPGYKTRSTI NLRLWSTKAA SEEFDLNAFN SGRHTEASEA LANAEKICYI LYPGDESIEG 370 380 390 400 410 420 KTLRLKQQYT LCSASLQDII ARFERRSGAS VNWEDFPEKV AVQMNDTHPT LCIPELMRIL 430 440 450 460 470 480 IDIKGLSWKD AWNITQRTVA YTNHTVLPEA LEKWSMDLME KLLPRHVEII EMIDEELIRT 490 500 510 520 530 540 IIAEYGTADS DLLDKKLKEM RILENVELPA EFADILVKTK EATDISSEEV QISKEGGEEE 550 560 570 580 590 600 ETSKEGGEEE EEKEVGGGRE EGDDGKEDEV EKAIAEKDGT VKSSIGDKKK KLPEPVPVPP 610 620 630 640 650 660 KLVRMANLCV VGGHAVNGVA EIHSEIVKDD VFNAFYKLWP EKFQNKTNGV TPRRWIRFCN 670 680 690 700 710 720 PDLSKIITQW IGTEDWILNT EKLAELRKFA DNEDLQTQWR EAKRNNKVKV AAFLRERTGY 730 740 750 760 770 780 SVSPDSMFDI QVKRIHEYKR QLLNIFGIVY RYKKMKEMNA AERKENFVPR VCIFGGKAFA 790 800 810 820 830 840 TYVQAKRIVK FITDVGATVN HDPEIGDLLK VIFVPDYNVS VAEMLIPASE LSQHISTAGM 850 860 870 880 890 900 EASGTSNMKF AMNGCLQIGT LDGANVEIRE EVGADNFFLF GAKAREIVGL RKERARGKFV 910 920 930 940 950 960 PDPRFEEVKK FVRSGVFGSY NYDELIGSLE GNEGFGRADY FLVGQDFPSY LECQEEVDKA 970 980 990 1000 YRDQKKWTRM SILNTAGSSK FSSDRTIHEY AREIWNIEPV KLE

References

[1]

"Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch." Buchner P., Borisjuk L., Wobus U. Planta 199:64-73(1996) [PubMed: 8680306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Fribo. Tissue: Cotyledon.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z36880 mRNA. Translation: CAA85354.1.
PIR	S47243.
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. 30.
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_VICFA

Accession

Primary (citable) accession number: P53536

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)