ID A0A178B254_9PLEO Unreviewed; 886 AA.
AC A0A178B254;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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=IQ06DRAFT_272064 {ECO:0000313|EMBL:OAL03160.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL03160.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL03160.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL03160.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441709; OAL03160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B254; -.
DR STRING; 765868.A0A178B254; -.
DR InParanoid; A0A178B254; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000077206; 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:UP000077206};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 731
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 886 AA; 100638 MW; 0C9294215514EA2B CRC64;
MAAAAPSARE RRPSTSAPIA DLKGPVGPNF TRPKHKRTVT GFGPSEIKSV EASIPEPQRE
AWRKFMPKPF TTPEEFEKEA VRHIETTLAR SLFNCDESAA YAGTALAFRD RLVLDWNKTQ
QSQTFADQKR IYYLSLEFLM GRALDNAMLN VEQKDVASKG LSDLGFRMED VISQEHDAAL
GNGGLGRLAA CFLDSMASLN YPAWGYGLRY RYGIFKQEIV DGYQVEVPDY WLDFNPWEFQ
RHDIVVDVQF YGQVNRWQDD EGKQQCSWEG GEIVQAVAFD VPVPGYKTGT CNNLRLWGSK
AASGEFDFQK FNSGEYESSV ADQQRAETIS AVLYPNDNLE RGKELRLKQQ YFWCAASLYD
IVRRFKKSQK AWKEFPNSVA IQLNDTHPTL AIPELQRILV DIEGLEWDDA WNIVSKTFGY
TNHTVLPEAL EKWSVPLMQH LLPRHLQIIY EINLQFLQFV ERNFPKERDI LGRVSIIEES
QPKMVRMAYL ALIGSHKVNG VAELHSDLIK TTIFKDFVKI YGPDKFTNVT NGITPRRWLH
QANPRLSALI ASKLGGHEFL KDLTLLGKLE AFVDDKEFRK EFREIKYANK VRLAQHIKEH
QGITVNPAAL FDVQVKRIHE YKRQQLNIFG VIHRYLQIKA MSPEERSKLA PRVSIFGGKA
APGYWMAKTV IHLVNKVGDV VNNDKDVGDL LKVVFIEDYN VSKAEIICPA SDISEHISTA
GTEASGTSNM KFCLNGGLII GTCDGANIEI TREIGENNIF LFGNLAEDVE DLRHAHLYSH
YQLDPSLAKV FDSIHQGMFG DAERFSALLN GIVEHGDYYL VSDDFASYVK TQELIDESYK
NTEEWTTKCI TTVARMGFFS SDRCIDEYAE AIWNVEPLIP KDEPAP
//
