Q9XTL9 (PYG_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase
EC=2.4.1.1

Gene names

Name:	GlyP
Synonyms:	Glp1
ORF Names:	CG7254

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	844 AA.
Sequence status	Complete.
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.
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	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	flight Inferred from mutant phenotype PubMed 17159148. Source: FlyBase glycogen catabolic process Inferred from mutant phenotype Ref.1. Source: FlyBase
Molecular_function	glycogen phosphorylase activity Inferred from direct assay PubMed 3093145. Source: FlyBase pyridoxal phosphate binding Inferred from direct assay PubMed 3093145. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 844	844	Glycogen phosphorylase		PRO_0000188540
Sites
	Binding site	76	1	AMP By similarity
Amino acid modifications
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A By similarity
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity
Natural variations
	Natural variant	642	1	K → N in strain: Canton-S.

Sequences

	Sequence		Length	Mass (Da)
	Q9XTL9 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 0A65C5B9DCA060ED	FASTA	844	96,997
	10 20 30 40 50 60 MSKPQSDADR RKQISVRGIA EVGNVTEVKK NFNRHLHYTL VKDRNVSTLR DYYFALANTV 70 80 90 100 110 120 KDNMVGRWIR TQQHYYEKDP KRVYYLSLEY YMGRSLTNTM INLGIQSECE EAMYQLGLDI 130 140 150 160 170 180 ENLEEMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFAQK IKNGEQVEEP 190 200 210 220 230 240 DDWLRYGNPW EKARPEFMLP VNFYGRVIDT PEGKKWVDTQ RVFAMPYDNP IPGYNNNHVN 250 260 270 280 290 300 TLRLWSAKSP IDFNLKFFND GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFM 310 320 330 340 350 360 CAATLQDIIR RYKASKFGSR EAVRNTFDHF PDKVAIQLND THPSLAIPEL MRILVDEEHL 370 380 390 400 410 420 TWEKAWDITV RSCAYTNHTV LPEALERWPV SLLESILPRH LQIIYHINFL HMENVKKKFP 430 440 450 460 470 480 DDLDRMRRMS MVEEDGEKRI NMAHLSIVGS HAVNGVAAIH SQILKDSLFH DFYEMEPQKF 490 500 510 520 530 540 QNKTNGITPR RWLLLCNPGL SDLIAEKIGD EWPVHLDQLV ALKKWAKDPN FQRNVARVKQ 550 560 570 580 590 600 ENKLKLAAIL EKDYGVKINP SSMFDIQVKR IHEYKRQLLN CLHIITLYNR IKKDPTANFT 610 620 630 640 650 660 PRTIMIGGKA APGYYVAKQI IKLICAVGNV VNNDPIVGDK LKVIFLENYR VTLAEKIMPA 670 680 690 700 710 720 ADLSEQISTA GTEASGTGNM KFQLNGALTI GTLDGANVEM AEEMGLDNIF IFGMTVDEVE 730 740 750 760 770 780 ALKKKGYNAY DYYNANPEVK QVIDQIQGGF FSPGNPNEFK NIADILLKYD HYYLLADYDA 790 800 810 820 830 840 YIKAQDLVSK TYQNQAKWLE MSINNIASSG KFSSDRTIAE YAREIWGVEP TWEKLPAPED QPQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and functional characterization of the Drosophila glycogen phosphorylase gene." Tick G., Cserpan I., Dombradi V., Mechler B.M., Toeroek I., Kiss I. Biochem. Biophys. Res. Commun. 257:34-43(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila complementary DNA resource." Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A. Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF073177 Genomic DNA. Translation: AAD41649.1. AF073178 mRNA. Translation: AAD27759.1. AF073179 mRNA. Translation: AAD27760.1. AE014134 Genomic DNA. Translation: AAF51303.1. AF160947 mRNA. Translation: AAD46887.1.
RefSeq	NP_001027219.1. NM_001032048.2. NP_722762.1. NM_164453.4.
UniGene	Dm.6829.
3D structure databases
ProteinModelPortal	Q9XTL9.
SMR	Q9XTL9. Positions 24-831.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-22585N.
IntAct	Q9XTL9. 1 interaction.
MINT	MINT-1625105.
STRING	7227.FBpp0099923.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Proteomic databases
PaxDb	Q9XTL9.
PRIDE	Q9XTL9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077828; FBpp0077501; FBgn0004507. FBtr0100485; FBpp0099923; FBgn0004507.
GeneID	33386.
KEGG	dme:Dmel_CG7254.
Organism-specific databases
CTD	33386.
FlyBase	FBgn0004507. GlyP.
Phylogenomic databases
eggNOG	COG0058.
GeneTree	ENSGT00390000016886.
InParanoid	Q9XTL9.
KO	K00688.
OMA	LMKETVF.
OrthoDB	EOG4B2RC2.
PhylomeDB	Q9XTL9.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17099.
Gene expression databases
Bgee	Q9XTL9.
GermOnline	CG7254. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. PTHR11468. 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...
Other
ChiTaRS	GlyP. drosophila.
GenomeRNAi	33386.
NextBio	783293.

Entry information

Entry name

PYG_DROME

Accession

Primary (citable) accession number: Q9XTL9
Secondary accession number(s): Q9V467

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	July 11, 2001
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project