ID M3B738_SPHMS Unreviewed; 892 AA.
AC M3B738;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SEPMUDRAFT_147477 {ECO:0000313|EMBL:EMF15652.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF15652.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF15652.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF15652.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456261; EMF15652.1; -; Genomic_DNA.
DR RefSeq; XP_016763773.1; XM_016904321.1.
DR AlphaFoldDB; M3B738; -.
DR STRING; 692275.M3B738; -.
DR GeneID; 27901458; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_0_1; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000016931; 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:UP000016931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 738
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 892 AA; 101782 MW; 0305A57A19CAB8AE CRC64;
MPINMATTNE TPAPRERRPS TNAPITDFQG PIGPAGISRP KHKRTVTGFG AQEIKSVEAS
IPEPQREAWR KYSASEFKSK DEFDRDVVRH IETTLARSLF NCDEAAAYSG TALAFRDRLI
IEWNRTQQQQ TYADPKRVYY LSLEFLMGRA LDNAMLNTGM KDIAKEGLHD LGFRMEDIIS
QERDAALGNG GLGRLAACFL DSMATLNYPA WGYALRYRYG IFKQEIIDGY QVEIPDYWLD
MNPWEFPRHD VTVDVQFYGS VRKYTDDNGK QVSVWENGEL VTAVAYDAPI PGYGTSTTNN
LRLWSSKASG GEFDFTKFNS GEYEASVADQ QRAETISAVL YPNDSLDRGK ELRLKQQYFW
CAASLFDIVR RFKKSKKAWK EFPNQVAIQL NDTHPTLAIP ELQRILIDQE GLDWDEAWSI
VQKTFGYTNH TVLPEALEKW SVPLVQHLLP RHLQIIYEIN LNFLQYVERT FPKDRDMLAR
VSIIEESQPK MVRMAYLAVI GSHKVNGVAE LHSDLIKTTI FKDFVKLYGP DKFTNVTNGI
TPRRWLHQAN PRLSELIASK LGGYDFLRDL TLLNKIESYV DDKSFRKEFQ EIKYANKVRL
AKYIKDANGI TVNPASLFDI QVKRMHEYKR QQLNIFGVIN HYLEIKDMSP EERKKVQPRV
SIFGGKAAPG YWMAKTIIHL INQVSKVVNN DKDIGDLLKV VFLEDYNVSK AEIICPASDI
SEHISTAGTE ASGTSNMKFV LNGGLIIGTC DGANIEITRE IGEDNIFLFG NLAEDVEDLR
HAHFYSEFHL DPMLERVFKT IQQGVFGDAG QFSALVNSIV EHGDYYLVSD DFKSYVDTQK
LIDEAYKNQE EWLTKTITSV ARMGFFSSDR CIDEYAEMIW NVEPLPPKSQ NA
//
