ID A0A074XN49_AURPU Unreviewed; 885 AA.
AC A0A074XN49;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 08-OCT-2025, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=M438DRAFT_346381 {ECO:0000313|EMBL:KEQ83427.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ83427.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ83427.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ83427.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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|ARBA:ARBA00001275,
CC 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; KL584984; KEQ83427.1; -; Genomic_DNA.
DR RefSeq; XP_029759614.1; XM_029905663.1.
DR AlphaFoldDB; A0A074XN49; -.
DR STRING; 1043002.A0A074XN49; -.
DR GeneID; 40747969; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OrthoDB; 9215500at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:TreeGrafter.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000002; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000003; Alpha-1,4 glucan 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, LIVER FORM; 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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:UP000030706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 732
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 885 AA; 100374 MW; 6DA58A19BA76110E CRC64;
MATTTTPSRS RRPSTSAPVA ELSGPIGPAG ITRPKHKRTI TGFGASDIKS VEAEIPDEQK
TAWKKHSASG FKNKEDFESA AIRHIETTLA RSLYNCDEGA AYGGTALAFR DRLIIDWNKT
QQSHTFADQK RVYYLSLEFL MGRALDNAML NVGLKDVARD GLADLGFRME DVIGIERDAA
LGNGGLGRLA ACFLDSLASL DYPAWGYGLR YRYGIFKQEI INGYQVEVPD YWLDFNPWEF
PRHDVTVDIQ FYGHVRKYND ENGRQVSVWE NGEIVTANAY DVPIPGYNTP TTNNLRLWSS
KAASGEFDFQ KFNSGEYEQS VHDQMRAETI SAVLYPNDNL DRGKELRLKQ QYFWCAASLH
DIVRRFKKSK KAWKEFPNQI AIQLNDTHPT LAIPELQRIL VDEEGLDWDT AWSIVVNTFG
YTNHTVMAEA LEKWSVPLIQ HLLPRHLEII YEINLHFLQY VERTFPKDRD MLSRVSIVEE
SNPKMIRMAF LAIVGSHKVN GVAELHSDLI KTTIFKDFVK IYGQDKFTNV TNGITPRRWL
HQANPKLSEL IASKLGGYDF LKDLTLLHKI EAYADDKQFR KAFQDIKYAN KTRLANYIKD
TTGVKVNPAA LFDIQVKRIH EYKRQQLNIF GVIHRYLALK AMSPEERKKM QPRVSIFGGK
AAPGYWMAKC IIHLVNEVGR VVNNDPEIGD ALKVIFIEDY NVSKCEIIAP ASDISEHIST
AGTEASGTSN MKFVLNGGLI IGTCDGANIE ITREIGEDNI FLFGNLAEDV EDIRHQHTYE
GVLIDDGLQK VFDAIHNGMF GHSDEFSALT NTVVNHDHWL TSADFEAYCK TQDSIDVAFK
DQESWLHKTI ISVARMGFFT ADRCIEEYAE MIWNVEPQKM KQNGA
//
