ID A0A139H445_9PEZI Unreviewed; 892 AA.
AC A0A139H445;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=AC578_31 {ECO:0000313|EMBL:KXS97260.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS97260.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS97260.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS97260.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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}.
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:KXS97260.1}.
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DR EMBL; LFZN01000148; KXS97260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H445; -.
DR STRING; 321146.A0A139H445; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000070133; 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:UP000070133};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 736
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 892 AA; 101859 MW; C4F8B167C69152AF CRC64;
MATATSTNSS TPRERKPSTS APITDFQGPV GPHGITRPKH KRTVTGFGPQ EIKAVEASIP
EHLREAWKKY SANEFTSKED FDKEVVRHIE TTLARSLFNC DEAAAYAGTA LAFRDRLVIE
WNRTQQNQTY HDPKRVYYLS LEFLMGRALD NAMLNTGMKD IASEGVKDLG FRMEDLIAQE
RDAALGNGGL GRLAACFLDS LATLNYPAWG YALRYRYGIF KQEIVDGYQV EIPDYWLDFN
PWEFPRHDVT VDIQFYGNVR KYTDDSGKQV SVWENGEIVT AVAYDAPVPG YGTKTTNNLR
LWSSKASHGE FDFTKFNSGE YEASVADQQR AETISAVLYP NDSLERGKEL RLKQQYFWCA
ASLFDIVRRF KKSKKAWKEF PNQVAIQLND THPTLAIPEL QRILIDQEGL EWDEAWSIVQ
KTFGYTNHTV LPEALEKWSV GLIQHLLPRH LQIIYDINLN FLQYVERTFP KERDMLSRVS
IIEESQPKMV RMAYLAVIGS HKVNGVAELH SDLIKTTIFK DFVKIYGPDK FTNVTNGITP
RRWLHQANPR LSELIASKLG GYDFLRDLTL LHKIEAYVDD KDFRKEFQEI KYANKVRLAK
YIKDTQGFTV NPASLFDIQV KRMHEYKRQQ LNIFGVIHRY LELKDMSPEE RKKVQPRVNI
FGGKAAPGYW MAKTIIHLIN QVAKVVNQDK DIGDLLKVIF LEDYNVSKAE MIVPASDISE
HISTAGTEAS GTSNMKFVLN GGLIIGTCDG ANIEITREVG EDNIFLFGNL AEDVEDLRHS
HFYGEFKIDP LLERVFKTIR EGTFGDAGQF SALVNSIVDH GDYYLCSDDF KSYVDTQRLI
DEAYKNQEEW LTKTITSVAR MGFFSSDRCI DEYAEMIWNV EPLPPPKSNG VA
//
