ID S2J1B3_MUCC1 Unreviewed; 881 AA.
AC S2J1B3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HMPREF1544_09383 {ECO:0000313|EMBL:EPB83871.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB83871.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., 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 Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-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}.
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DR EMBL; KE124056; EPB83871.1; -; Genomic_DNA.
DR AlphaFoldDB; S2J1B3; -.
DR STRING; 1220926.S2J1B3; -.
DR VEuPathDB; FungiDB:HMPREF1544_09383; -.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; S2J1B3; -.
DR OMA; HCACSVA; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000014254; 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:UP000014254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 730
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 881 AA; 100718 MW; 39E0602131003576 CRC64;
MSTTPTSSRP RRLSMPKLTR RLTNVVIHVD KDDNVEPVTP ASVPSRPSKR EELDEKAKSN
WKKHMTPERN DTDAIEQDIV HHTITTLCRG VYNIDKLAMY QATAHSVRDR LLEDWNNTQE
ALHKENPKRC YYMSMEFLIG RALDNALNCL KVKKNYKESV DNLGFNLEDL LVEEKDAALG
NGGLGRLAAC YMDSAATLDY PTWGYGLRYQ YGIFKQIIKD GYQNEMPDYW LNFDNPWEFP
RADIRYEIRF HGYVATKMNE KGESRMSWEG GDKVQAMAYD VPIPGFDTKG CGNIRLWSSK
PLNTFDFDSF NAGDYDRSVS EQTNAQNLTS VLYPNDNHLV GKELRLKQEY FFVSASLQDI
IYRFKRAKCP WKDFPDKVAV QMNDTHPTLA VPELQRILVD VEGLEWDDAW DIVTRTFAFT
NHTVLPEALE CWSVPMMEKI LPRHMQIIYD INLFFLQKVE RDFSADRELL KRISIIEETS
PQQVRMAYLA VVGSHTVNGV AALHSDLIRK NLFNDFVKYY GPEKFINITN GITPRRWLYQ
SNPGLRDLIT KTLGSEKWAT HLDQLEGLKK YADDASFQDA WADVKLQNKK RLADWIKTNM
NITVNPHALF DIQVKRIHEY KRQYMNILSV IYRYKSLKKM SPEDLEQQVP RVVIFGGKAA
PGYYIAKLVI KLINSAAEVI NNDPSIKDML KVVFIPDYNV SLAEIIIPAS DISQHISTAG
TEASGTSNMK FVLNGGLILG TVDGANIEIG EQIGDENIFM FGVLADAVDD IRHNQKYHGL
FIDASLQVVI DAIQGGEFGD PSIFGPLINT LTYGGDYYLI STDFKSYLQK HTEVDDTYRD
KAAWNKKSIM CTAGMGFFSS DRAVHTYAEK IWKLKPFKVE A
//
