ID   A0A0B7MX58_9FUNG        Unreviewed;       881 AA.
AC   A0A0B7MX58;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=PARPA_01159.1 scaffold 1359 {ECO:0000313|EMBL:CEP07850.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP07850.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP07850.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP07850.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LN719426; CEP07850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7MX58; -.
DR   STRING; 35722.A0A0B7MX58; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000054107; 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:UP000054107};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   REGION          30..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         730
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   881 AA;  100660 MW;  B3E6FE70FE589599 CRC64;
     MSTTPTSSRP RRLSMPKLTR RLTNVVIHVD DNDNVEPVTP TSVPSRPSTR EELDEKAKSN
     WKKHMLPEKN DTDSIEQDIV HHTITTLCRG VYNIDKLAMY QATAHSVRDR LLEDWNCTQE
     ALHKENPKRC YYMSMEFLIG RALDNALNCL KVKKNYKESV NNLGFSLEDL LVEEKDAALG
     NGGLGRLAAC YMDSTATLDY PTWGYGLRYQ YGIFKQIIKD GYQNEMPDYW LNFDNPWEFP
     RTDIRYEVRF HGYVATKMNE KGESRMSWEG GDKVQAMAYD VPIPGFDTKG CGNIRLWSSK
     PLNTFDFDSF NAGDYERSVS EQTNAQNLTS VLYPNDNHLV GKELRLKQEY FFVSASLQDI
     IHRFKRAKCP WKDFPDKVAV QMNDTHPTLA VPELQRILVD VEGLEWDDAW DIVTRTFAFT
     NHTVLPEALE CWSVPMMEKI LPRHMQIIYD INLFFLQKVE RDFSPDRELL KRISIIEETS
     PQQVRMAYLA VVGSHTVNGV AALHSDLIRK NLFNDFVKYY GPEKFINITN GITPRRWLYQ
     SNPALRDLIT KTLGSEDWAT HLDLLQGLKK YADDAAFQDA WADVKLQNKK RLADWIKTNM
     NITVNPHALF DIQVKRIHEY KRQFMNILSV IYRYKSLKKM SAEDLEQQVP RVVIFGGKAA
     PGYYIAKLVI KLINSAADVI NNDVSIKDML KVVFIPDYNV SLAEIIVPAS DISQHISTAG
     TEASGTSNMK FVLNGGLILG TVDGANIEIC EQIGKENIFM FGVLADAVDD IRHNQKYHGL
     FIDASLQVVI DAIQGGEFGD PSVFGPLINT LTYGGDYYLI STDFKSYLQE HTVVDDTFRD
     RAVWNKKSIM CTAGMGFFSS DRAVRTYAEK IWKLKPFKVG V
//