PHS2_DICDI
ID PHS2_DICDI Reviewed; 993 AA.
AC P34114; Q54F21;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Glycogen phosphorylase 2;
DE Short=GP2;
DE EC=2.4.1.1;
GN Name=glpD; ORFNames=DDB_G0291123;
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], PROTEIN SEQUENCE, SUBUNIT, PROTEOLYTIC
RP PROCESSING, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=1310312; DOI=10.1016/s0021-9258(18)45877-2;
RA Rutherford C.L., Peery R.B., Sucic J.F., Yin Y., Rogers P.V., Luo S.,
RA Selmin O.;
RT "Cloning, structural analysis, and expression of the glycogen
RT phosphorylase-2 gene in Dictyostelium.";
RL J. Biol. Chem. 267:2294-2302(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: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1310312}.
CC -!- DEVELOPMENTAL STAGE: Appears during cell differentiation; absent in
CC amoebae and early stages of development, reaches a maximum level of
CC expression at the slug stage and then decreases.
CC {ECO:0000269|PubMed:1310312}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Enzyme activity requires processing of the 113 kDa peptide to an
CC enzymatically active 106 kDa form of the protein. Processing would
CC occur near the middle of the Gln-rich repetitive element.
CC {ECO:0000269|PubMed:1310312}.
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}.
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DR EMBL; M77492; AAA33211.1; -; Genomic_DNA.
DR EMBL; AAFI02000175; EAL61845.1; -; Genomic_DNA.
DR PIR; A42318; A42318.
DR RefSeq; XP_635369.1; XM_630277.1.
DR AlphaFoldDB; P34114; -.
DR SMR; P34114; -.
DR STRING; 44689.DDB0191397; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; P34114; -.
DR PRIDE; P34114; -.
DR EnsemblProtists; EAL61845; EAL61845; DDB_G0291123.
DR GeneID; 8628017; -.
DR KEGG; ddi:DDB_G0291123; -.
DR dictyBase; DDB_G0291123; glpD.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; P34114; -.
DR OMA; IYDINWR; -.
DR PhylomeDB; P34114; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P34114; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
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:0060359; P:response to ammonium ion; IDA:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; 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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..993
FT /note="Glycogen phosphorylase 2"
FT /id="PRO_0000188547"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 229
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 242
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250"
FT MOD_RES 763
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="R -> T (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="Y -> L (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="V -> I (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..415
FT /note="HN -> T (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="R -> V (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="S -> A (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="I -> V (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="N -> S (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="N -> S (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..574
FT /note="RR -> SS (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="Q -> E (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..623
FT /note="EIK -> TIN (in Ref. 1; AAA33211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 993 AA; 113104 MW; 3DD37DBFEE4F2871 CRC64;
MEEKRSTNSP GFDKPKLNRS GSITSATSHP PRSNSNPKLV AKHQQQLYEE SKNKRNQEQQ
NQQPQQQQQK QTSNQSEDPA TQLSSLKFES DKEKEQALLW AFLASYLPED KGSLQKEFVK
HVEYTLAQTK SECTDFSSFQ ALSYCTRDRL IERWKDTKLF FKQKNVKQVN YMSLEFLLGR
SLQNSLSALG LVGKYSDALM DLGFKLEDLY DEERDAGLGN GGLGRLAACF MDSLATCNFP
GYGYGLRYKF GMFYQTLVDG EQVELPDYWL NYGSPWEIER LDVSYPINFY GKVSEVEDEN
GKKVMKWDQG EQMLAVAYDY PIPGFKTYNT VAIRLWSSKP SDEFNLDSFN RGDYLGAIEE
KEKSENITNV LYPNDNTMQG KELRLKQQYL FVSATIQDII SQFKETGKPF SEFHNFHAIQ
LNDTHPTLGI PELMRILIDE EKKSWDEAWD ITTKTFSYTN HTVLPEALEK WSVSMVENVL
PRHIMIIYEI NERFLKLVDQ KWPGDMSKRR ALSIIDESDG KFIRMAFLAI VGSHTINGVA
YLHSELVKHD VFPLFYEIWP NKFQNKTNGV TPRRWIQQSN PQLAELITRS LNSDRWLVNL
DIIKDLVHLA DNSSFQKEWM EIKRNNKIRL AKYIEKRCDI QVNVDVLFDV QVKRFHEYKR
QLLNVLSVIN RYLDIKEGKK VAPRVVIFGG KAAPGYYMAK LIIKLINSVA DVVNNDPKVG
DLLKVVFIPN YCVSNAEIII PASDISQHIS TAGTEASGTS NMKFSMNGGL IIGTLDGANI
EIRDAIGHEN MYIFGARSEE VNKVKKIIHD GKFTPDTRWA RVLTAIKEDT FGPHEQFQDI
INSVSGGNDH YILSYDFGSY LDIQNSIDQD FKDRAKWAKK SIMASVCCGK FSSDRTIKEY
AQQIWGIEEW KRPGPVPVSN EEARSLLVPP PSGSPNDINA ISIERLSPLT FVKQTSASPL
SVISGGDKTN NTLKPKQTTK GFNIGGQPGN PTN
