Reviewed, UniProtKB/Swiss-Prot Q8HXW4 (PYGM_MACFA)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase, muscle form
    EC=2.4.1.1
Alternative name(s):
    Myophosphorylase

Gene names

Name:	PYGM
ORF Names:	QccE-10224

Organism

Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	842 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 By similarity.
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A By similarity.
Post-translational modification	Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A By similarity.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 842	841	Glycogen phosphorylase, muscle form		PRO_0000188530
Sites
	Binding site	76	1	AMP By similarity
	Site	109	1	Involved in the association of subunits By similarity
	Site	143	1	Involved in the association of subunits By similarity
	Site	156	1	May be involved in allosteric control By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A By similarity
	Modified residue	316	1	N6-acetyllysine By similarity
	Modified residue	473	1	Phosphotyrosine By similarity
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8HXW4-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F1EFAD31EDAD2424	FASTA	842	97,150
	10 20 30 40 50 60 MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 190 200 210 220 230 240 DVWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 250 260 270 280 290 300 TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENIPRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM 370 380 390 400 410 420 DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAATFP 430 440 450 460 470 480 GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 490 500 510 520 530 540 QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ 550 560 570 580 590 600 ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV 610 620 630 640 650 660 PRTVMIGGKA APGHHMAKMI IRLITAIGDV VNHDPTVGDR LRVIFLENYR VSLSEKVIPA 670 680 690 700 710 720 ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD 730 740 750 760 770 780 KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED 790 800 810 820 830 840 YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE AI

References

[1]	"Isolation and characterization of cDNA for macaque neurological disease genes." Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB083327 mRNA. Translation: BAC20606.1.
3D structure databases
HSSP	HSSP built from PDB template 1PYG based on UniProtKB P00489.
SMR	Q8HXW4. Positions 13-841.
ModBase	Search...
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Phylogenomic databases
HOVERGEN	Q8HXW4.
Enzyme and pathway databases
BRENDA	2.4.1.1. 3438.
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

PYGM_MACFA

Accession

Primary (citable) accession number: Q8HXW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 39 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)