Reviewed, UniProtKB/Swiss-Prot P53537 (PHSH_VICFA)

Names and origin

Protein names	Recommended name:     Alpha-glucan phosphorylase, H isozyme     EC=2.4.1.1 Alternative name(s):     Starch phosphorylase H
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	842 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 H isoform exhibits higher affinity for branched polyglucans such as soluble starch or glycogen.
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	Cytoplasm.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
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	cytoplasm 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
	Chain	1 – 842	842	Alpha-glucan phosphorylase, H isozyme		PRO_0000188544
Amino acid modifications
	Modified residue	688	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53537-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6EA0C09069DC63B4	FASTA	842	95,924
	10 20 30 40 50 60 MGFKVETNGG DGSLVSAKVP PLANPLAEKP DEIASNISYH AQYTPHFSPF KFQLQQAYYA 70 80 90 100 110 120 TAESVRDRLI QQWNETYLHF HKVDPKQTYY LSMEFLQGRA LTNAIGNLNI QDAYADALRK 130 140 150 160 170 180 FGLELEEITE QEKDAALGNG GLGRLASCFL DSMATLNLPA WGYGLRYRYG LFKQIITKEG 190 200 210 220 230 240 QEEVAEDWLE KFSPWEIVRH DVLYPIRFFG QVEVNPDGSR QWIGGEVIQA LAYDVPIPGY 250 260 270 280 290 300 QTKNTISLRL WEAKACADDF DLFLFNDGQL ESASVLHSRA QQICSVLYPG DATEGGKLLR 310 320 330 340 350 360 LKQQYFLCSA SLQDIISRFK ERRQGPWNWS EFPTKVAVQL NDTHPTLSIP ELMRLLMDDE 370 380 390 400 410 420 GLGWDEAWAV TSKTVAYTNH TVLPEALEKW SQPVMWKLLP RHMEIIEEID RRFVALISKT 430 440 450 460 470 480 RLDLEDEVSN MRILDNNLQK PVVRMANLCV VSSHTVNGVA QLHSDILKSE LFASYVSIWP 490 500 510 520 530 540 TKFQNKTNGI TPRRWINFCS PELSRIITKW LKTDKWVTNL DLLTGLREFA DNEDLQAEWL 550 560 570 580 590 600 SAKRANKQRL AQYVLQVTGE NIDPDSLFDI QVKRIHEYKR QLLNILGVIY RYKKLKEMSP 610 620 630 640 650 660 EERKSTTART VMIGGKAFAT YTNAKRIVKL VDDVGSVVNS DPEVNSYLKV VFVPNYNVSV 670 680 690 700 710 720 AEVLIPGSEL SQHISTAGME ASGTSNMKFA LNRVLIIGTL DGANVEIREE IGEENFFLFG 730 740 750 760 770 780 ATADEVPRLR KERENGLFKP DPRFEEAKKF IRSGVFGSYD YNPLLDSLEG NSGYGRGDYF 790 800 810 820 830 840 LVGYDFPSYM DAQEKVDEAY RDKKRWLKMS ILSTAGSGKF SSDRTIAQYA KEIWNIEECR VP

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	Z35117 mRNA. Translation: CAA84494.1.
PIR	T12091.
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

PHSH_VICFA

Accession

Primary (citable) accession number: P53537

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)