Reviewed, UniProtKB/Swiss-Prot Q00766 (PHS1_DICDI)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase 1
      Short name=GP1
    EC=2.4.1.1

Gene names

Name:	glpV
ORF Names:	DDB_G0281383

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	853 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May provide energy to overcome environmental stresses.
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor	Pyridoxal phosphate.
Enzyme regulation	During logarithmic growth and early developmental phases, the activity of GP1 is dependent on 5'AMP. It then seems to convert to an AMP independent type. This alteration in activity coincides with phosphorylation of GP1. Ref.1
Developmental stage	Present throughout cellular differentiation. Ref.1
Miscellaneous	In D.discoideum glycogen phosphorylase exists as 2 developmentally regulated forms, GP1 and GP2, which are the products of separate genes.
Sequence similarities	Belongs to the glycogen phosphorylase family.
Sequence caution	The sequence CAA44069.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycogen catabolic process Inferred from direct assay. Source: dictyBase
Cellular component	intracellular Inferred from direct assay. Source: dictyBase
Molecular function	glycogen phosphorylase activity Inferred from direct assay. Source: dictyBase nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 853	853	Glycogen phosphorylase 1		PRO_0000188546
Sites
	Binding site	91	1	AMP By similarity
	Site	159	1	Involved in the association of subunits By similarity
	Site	174	1	May be involved in allosteric control By similarity
Amino acid modifications
	Modified residue	27	1	Phosphoserine By similarity
	Modified residue	75	1	Phosphoserine By similarity
	Modified residue	697	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	59	1	T → R in CAA44069. Ref.1
	Sequence conflict	264	1	L → I in CAA44069. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q00766-1 [UniParc]. Last modified December 4, 2007. Version 3. Checksum: F1505B7E15946368	FASTA	853	98,277
	10 20 30 40 50 60 MSTTIPLKHT ARTTTGVVPP TEKKKGSKLF ALKTDFLKND EDSIQKDILD HVEYTLARTK 70 80 90 100 110 120 YNFDSFSAYQ GSAYSVRDRL IERWNETQQY YTERDPKRVY YLSMEFLMGR SLQNAIYNMN 130 140 150 160 170 180 LKDEYHNALL ELGFEMEDLY EEEKDAALGN GGLGRLAACF MDSLATLKYP AWGYGLRYNY 190 200 210 220 230 240 GMFEQGIYDG YQTEVPDYWL VAGNPWEIER LDVQYTVRFY GQVTEKKSSD GSKFEWDHGE 250 260 270 280 290 300 LVQAIAYDTP VPGYHTTNTN NIRLWSSKPH KEFDLDAFNG GNYLSAVEAK QRSENITSVL 310 320 330 340 350 360 YPNDNTYSGK ELRLKQQYFF VAATLCDVIR RFKKSHQNWQ DFPNKVAIQL NDTHPTIGVV 370 380 390 400 410 420 ELFRKLIDEE GLQWEEAWDI VTKTFAYTNH TILPEALEMW PVSLIEDLLP RHMQLIYGIN 430 440 450 460 470 480 HRFLIQVTQK WPGDIGKMRG LSIIQEGEEK RVRMAHLAIV GSHCVNGVAA MHSELVKHKV 490 500 510 520 530 540 FPDFFCLWPE KFQNKTNGVT PRRWIEQANP GLSAIFTKWL GTDKWTTNLE LVKGIKEHMD 550 560 570 580 590 600 NPELIAEWKY VKQGNKQRLA EFILKHCGIH VNPNALFDVH IKRIHEYKRQ LLNILSVIYR 610 620 630 640 650 660 YLSIKKMSPK DRAQVVPRVV IFAGKAAPGY VMAKRHIKLI NSVAEVINRD KEVDQYLKVV 670 680 690 700 710 720 FIANYNVSIA QVIVPASDIN QQISTAGTEA SGTSNMKFTM NGSLIIGTLD GANVEIAEEV 730 740 750 760 770 780 GQENMFIFGL RTSEVEAARE KMTNKEVNID PRLQEVFLNI ELGTFGPPDV FRPILDSLIF 790 800 810 820 830 840 SDFYLSIQDF PLYLDSQASV DELWKDQSAW VKKSIINSAS TYFFSSDRAM NEYAEQIWDI 850 KPCEVETTLN RRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and cloning of glycogen phosphorylase 1 from Dictyostelium discoideum." Rogers P.V., Luo S., Sucic J.F., Rutherford C.L. Biochim. Biophys. Acta 1129:262-272(1992) [PubMed: 1536877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, ENZYME REGULATION, DEVELOPMENTAL STAGE. Strain: AX3.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62142 Genomic DNA. Translation: CAA44069.1. Sequence problems. AAFI02000041 Genomic DNA. Translation: EAL66673.1.
PIR	S20595.
RefSeq	XP_640695.1.
3D structure databases
SMR	Q00766. Positions 11-843.
ModBase	Search...
Protein-protein interaction databases
STRING	Q00766.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Genome annotation databases
GeneID	8623081.
KEGG	ddi:DDB_0215010.
Organism-specific databases
dictyBase	DDB_G0281383. glpV.
Phylogenomic databases
eggNOG	KOG2099.
HOGENOM	HBG444050.
OMA	ERLDVQY.
PhylomeDB	Q00766.
Enzyme and pathway databases
BRENDA	2.4.1.1. 424.
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

PHS1_DICDI

Accession

Primary (citable) accession number: Q00766
Secondary accession number(s): Q54TW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	December 4, 2007
Last modified:	February 9, 2010
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)