ID W9YQD2_9EURO Unreviewed; 896 AA.
AC W9YQD2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=A1O1_00256 {ECO:0000313|EMBL:EXJ95137.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ95137.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ95137.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ95137.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ95137.1}.
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DR EMBL; AMWN01000001; EXJ95137.1; -; Genomic_DNA.
DR RefSeq; XP_007719366.1; XM_007721176.1.
DR AlphaFoldDB; W9YQD2; -.
DR STRING; 1182541.W9YQD2; -.
DR GeneID; 19155165; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_0_1; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000019484; 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:UP000019484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 733
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 896 AA; 101634 MW; 94E78E0C8133893A CRC64;
MAAAVSSSPS RERKPSVGAP ISTLQGPVGP GFSRPKHKRT ATGFAAGDIK AVESSIPEHM
REAWRKFSPA GFTTKDEFEA ECVRHVETTL ARSLYNCDEL AAYSGTALAF RDRLIIDWNK
TQQRQTFVDQ KRIYYLSLEF LMGRTLDNAM LNVGLKKVAQ EGLGDLGFRI EDVVNQEHDA
ALGNGGLGRL AACFLDSLAS LNYPAWGYGL RYRYGIFKQE IENGYQVEIP DYWLDFNPWE
FARHDVTVDV QFYGWVNKYT NDEGKQVVSW QDGELVTAVA YDVPIPGYGT STVNNLRLWS
SKASSGEFDF SKFNSGDYES AVADQQRAET ISAVLYPNDN LERGKELRLK QQYFWCAASL
HDIVRRFKKT QRKWSEFPDQ VAIQLNDTHP TLAIVELQRI LVDKEGLEWD VAWGIVTKTF
GYTNHTVLPE ALEKWSVPLM QNLLPRHLSI IYDINLFWLQ SVERRFPKDR DMLARVSIIE
ESQPKMVRMA YLAIVGSHKV NGVAELHSDL IKTTIFKDFV KVYGPDKFTN VTNGITPRRW
LHQANPRLSE LIASKLGGYD FLKDLTLLNK LEPFIDDKEF KKEWAEIKYA NKVRLAQHIL
KTTGVSVNPK SMFDVQVKRI HEYKRQQLNI FGVIRRYLAI KAMTPEERKK LLPRVSIFGG
KAAPGYWMAK TIIHLINKVG EVVNKDPDVG DLLKVIFIED YNVSKAEIIC PASDISEHIS
TAGTEASGTS NMKFVLNGGL IIGTLDGANI EITREIGEQN VFLFGNLAED VEDLRHNHYY
GHYTLDPELA KVFDCIKSGT FGKEGGFDSL ISAIADNGDY YLVSDDFHSY CKTQDLIDES
YRNQEEWLSK SILSVARMGF FTSDRCINEY ADSIWNIEPL EVKDEDEVRA RTGLGN
//
