PHS1_DICDI
ID PHS1_DICDI Reviewed; 853 AA.
AC Q00766; Q54TW6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycogen phosphorylase 1;
DE Short=GP1;
DE EC=2.4.1.1;
GN Name=glpV; ORFNames=DDB_G0281383;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, ACTIVITY
RP REGULATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=1536877; DOI=10.1016/0167-4781(92)90502-q;
RA Rogers P.V., Luo S., Sucic J.F., Rutherford C.L.;
RT "Characterization and cloning of glycogen phosphorylase 1 from
RT Dictyostelium discoideum.";
RL Biochim. Biophys. Acta 1129:262-272(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May provide energy to overcome environmental stresses.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: During logarithmic growth and early developmental
CC phases, the activity of GP1 is dependent on 5'AMP. It then seems to
CC convert to an AMP independent type. This alteration in activity
CC coincides with phosphorylation of GP1. {ECO:0000269|PubMed:1536877}.
CC -!- DEVELOPMENTAL STAGE: Present throughout cellular differentiation.
CC {ECO:0000269|PubMed:1536877}.
CC -!- MISCELLANEOUS: In D.discoideum glycogen phosphorylase exists as 2
CC developmentally regulated forms, GP1 and GP2, which are the products of
CC separate genes.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X62142; CAA44069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAFI02000041; EAL66673.1; -; Genomic_DNA.
DR PIR; S20595; S20595.
DR RefSeq; XP_640695.1; XM_635603.1.
DR AlphaFoldDB; Q00766; -.
DR SMR; Q00766; -.
DR STRING; 44689.DDB0215010; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; Q00766; -.
DR EnsemblProtists; EAL66673; EAL66673; DDB_G0281383.
DR GeneID; 8623081; -.
DR KEGG; ddi:DDB_G0281383; -.
DR dictyBase; DDB_G0281383; glpV.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q00766; -.
DR OMA; KHKRTFT; -.
DR PhylomeDB; Q00766; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:Q00766; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:dictyBase.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Carbohydrate metabolism; Direct protein sequencing;
KW Glycogen metabolism; Glycosyltransferase; Nucleotide-binding;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..853
FT /note="Glycogen phosphorylase 1"
FT /id="PRO_0000188546"
FT BINDING 91
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="T -> R (in Ref. 1; CAA44069)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> I (in Ref. 1; CAA44069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 98277 MW; F1505B7E15946368 CRC64;
MSTTIPLKHT ARTTTGVVPP TEKKKGSKLF ALKTDFLKND EDSIQKDILD HVEYTLARTK
YNFDSFSAYQ GSAYSVRDRL IERWNETQQY YTERDPKRVY YLSMEFLMGR SLQNAIYNMN
LKDEYHNALL ELGFEMEDLY EEEKDAALGN GGLGRLAACF MDSLATLKYP AWGYGLRYNY
GMFEQGIYDG YQTEVPDYWL VAGNPWEIER LDVQYTVRFY GQVTEKKSSD GSKFEWDHGE
LVQAIAYDTP VPGYHTTNTN NIRLWSSKPH KEFDLDAFNG GNYLSAVEAK QRSENITSVL
YPNDNTYSGK ELRLKQQYFF VAATLCDVIR RFKKSHQNWQ DFPNKVAIQL NDTHPTIGVV
ELFRKLIDEE GLQWEEAWDI VTKTFAYTNH TILPEALEMW PVSLIEDLLP RHMQLIYGIN
HRFLIQVTQK WPGDIGKMRG LSIIQEGEEK RVRMAHLAIV GSHCVNGVAA MHSELVKHKV
FPDFFCLWPE KFQNKTNGVT PRRWIEQANP GLSAIFTKWL GTDKWTTNLE LVKGIKEHMD
NPELIAEWKY VKQGNKQRLA EFILKHCGIH VNPNALFDVH IKRIHEYKRQ LLNILSVIYR
YLSIKKMSPK DRAQVVPRVV IFAGKAAPGY VMAKRHIKLI NSVAEVINRD KEVDQYLKVV
FIANYNVSIA QVIVPASDIN QQISTAGTEA SGTSNMKFTM NGSLIIGTLD GANVEIAEEV
GQENMFIFGL RTSEVEAARE KMTNKEVNID PRLQEVFLNI ELGTFGPPDV FRPILDSLIF
SDFYLSIQDF PLYLDSQASV DELWKDQSAW VKKSIINSAS TYFFSSDRAM NEYAEQIWDI
KPCEVETTLN RRY
