ID A0A0V0QLZ5_PSEPJ Unreviewed; 896 AA.
AC A0A0V0QLZ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PPERSA_09248 {ECO:0000313|EMBL:KRX03236.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03236.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03236.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03236.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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 Evidence={ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX03236.1}.
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DR EMBL; LDAU01000140; KRX03236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QLZ5; -.
DR EnsemblProtists; KRX03236; KRX03236; PPERSA_09248.
DR InParanoid; A0A0V0QLZ5; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 713
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 896 AA; 104525 MW; 751F3BBD39965884 CRC64;
MENRSYERKS SRRHSYWNKS GGQIQGYRAE FGSHTDLARN EKIWELMSQY IGTTKEDIQK
HIVTHVEHTL AKTRFDFTSF HCYQAVAVSI RDRLIELSND TQQHFIHNDV KFVYYLSLEF
LIGRYLQNAL INLDIEDLYK EAVKDLGYKL EALYEEEKDP ALGNGGLGRL AACFMDSLAT
LNYPAWGYGL RYSYGIFKQY IQDGYQCEVP DFWLDQGNPW EIERVDLNYR IRFYGHVSKV
KEGDQEVSVW EGGETVYARP YDNPLPGHGT FNTINLRLWR SIPGEEFHFQ HFNSGDYQRA
LEQRQRAEYI TSVLYPNDST YAGKELRLKQ QYLLVSASCQ DAIRRFMKKK PRDWKDWPEK
VAMQLNDTHP ALAIVELLRI LVDIERFSWE FAWNLVYKCF SYTNHTVLPE ALEKWGTDLM
KHLLPRHLEL IYMINHLFLE NISKRFPTDA LKLQRMSIIE EGHGQKVRMA NLCVIGSHAV
NGVAALHTEL VKKNLFNDFY QIKPKKFQNK TNGVTPRRWI RCCNPQLAEF YTIKLGGDEW
LFNMNELKDL VAIAEDEQAQ KEFAKIKRHN KEQLWWWVKH NLQIDLNIDS LFDIQVKRIH
EYKRQFMNIL YVIHRYLSII NTPPEERKRK FLPRSVLFGG KAAPGYINAK RIIKLINAVG
EKVNRDSAVG DLLKVVFLPN YNVSLAEIII PAAELSQHIS TAGMEASGTS NMKFVMNGSC
LIGTWDGANV EICEEVGVEN EFIFGARVEE IEALREKMRA TSPDKYFSEN LKKVLAAIEE
GVFGKSDDLV HLIDTIRHNN DYYLVGADFE SYCEAQQKVD DCYRNQKEWY KRIMLNAFKT
GKFSSDRTIH EYAKEIWKVE PFEIPIPALS MKERTKSFHD KQGIQMDQTA SESQIN
//
