ID B0DQT6_LACBS Unreviewed; 891 AA.
AC B0DQT6;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 08-NOV-2023, entry version 64.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=LACBIDRAFT_307719 {ECO:0000313|EMBL:EDR03173.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR03173.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547126; EDR03173.1; -; Genomic_DNA.
DR RefSeq; XP_001886314.1; XM_001886279.1.
DR AlphaFoldDB; B0DQT6; -.
DR STRING; 486041.B0DQT6; -.
DR GeneID; 6081860; -.
DR KEGG; lbc:LACBIDRAFT_307719; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; B0DQT6; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000001194; 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:UP000001194};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 861..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 710
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 891 AA; 100149 MW; C81318CF778BCC01 CRC64;
MTSTIDPKSI GKVVRPRRHV RTLTGFIPET DETGKEKWPK GDEKAWRDGM RSVDKGISDV
TRSVVNHVQT SLARQPYNLD DFGAYQASAL SVRDDLLVNW NETQMNYTRK APKRAYYLSL
EFLMGRTLDN ALLNLGLKDL YKDGLKNLGF NMEDLLEKER DAALGNGGLG RLAACYLDSS
ASQELPVWGY GLRYKYGIFQ QLISQDGEQL EAPDPWLENQ NPWELPRLDV TYQVRFYGNA
DRMADGSGRA IWQGGQEVLA VAYDVMIPGY GTKTTNNLRL WESKPKRGFD LNSFNAGNYE
GAVEASNSAD AITSVLYPND HTSFGKELRL KQQYFWTAAS LADILRRFKN TGKPIKEFSD
HVAIQLNDTH PTLAIPELMR ILIDDEDLHW NQAWEIVTNT FFYTNHTVLP EALEKWPVPL
LEHVLPRHLQ IIYDINLFFL QAVEKKYPGD RDRLARMSLI EEGTPKQVRM AFLACVGSRK
VNGVAELHSE LVRTTILKDF VEFEGISKFG NVTNGITPRR WLDQCNPELS ALISKTLQLS
PGAWLKELTK LEGLLPYAES KTFRAEWAAI KQRNKERLAH HVEVTLGLKV RTDAMYDVQI
KRQTLNILGV IHRYLTLKSL KPAERAKANR KVVFFAGKAA PAYYIAKLTI RLIVNVARVI
NADPETNEYL QLYFLPDYSV SLAEVLIPAS DISQHISTAG TEASGTSNMK FCLNGGLLLG
TVDGANIEIA EEVGESNVFF FGHLTPAVED LRYQHVYHPV PIEQKCPALA QVLDQISGGL
FGGDGVYEPL LNTIRQGDYY LLTDDFDSYI AALAMVDEAY LDKEEWTKKS IKTTAKMGKF
SSDRAINEYA ESYWNIEATP VPAEKPASSK PAKEATPVPA DIPASSKPAK K
//
