ID A0A1V6R154_9EURO Unreviewed; 894 AA.
AC A0A1V6R154;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, 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=PENSOL_c021G03835 {ECO:0000313|EMBL:OQD95195.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD95195.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD95195.1}.
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DR EMBL; MDYO01000021; OQD95195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R154; -.
DR STRING; 60172.A0A1V6R154; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000191612; 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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 743
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 894 AA; 101948 MW; E89C27428D250213 CRC64;
MSTIPDAVAP TEPIEPTQPR RERRLSVGAP IGDLQGPVGP GFSRPKHKRT FTGLGPAEIK
NVEASIPEPL REAWRKHSAT EFTTKDEFEK DLVRHIETTL ARSLYNCDEL AAYSGTALAF
RDRLIIEWNR TQQRQTFTDQ KRVYYLSLEF LMGRTLDNAM LNVGLKDVAR DGLSDLGFRV
EDVINQEYDA ALGNGGLGRL AACFLDSMAT LNYPAWGYGL RYRYGIFKQE IVNGYQVEIP
DYWLDNNPWE FPRHDITVDI QFYGNVKKYQ DENGRLSHSW EDGEIVQAVA YDVPIPGYGT
KTTNNLRLWS SKASTGEFDF QKFNAGDYES AVADQQRAET ISAVLYPNDN LERGKELRLK
QQYFWCAASL FDIVRRFKKT KRAWGEFPDQ IAIQLNDTHP TLAIVELQRI LIDKEGLEWD
EAWSIVTKTF GYTNHTVLPE ALEKWSVPLM QNLLPRHLQI IYEINLFFLQ SVEKRFPNDR
DILSRVSIIE ESHPKMVRMA YLAIIGSHKV NGVAELHSDL LKTTLFKDFV KIYGPDRFTN
VTNGITPRRW LHQANPRLSA LIAEKLGSHD FLKDLTLLDK IEAFVDDKAF REEWAVIKRE
NKLRLAKHIK ATTGFDVNPN ALFDVQVKRI HEYKRQQLNI FGVIHRYLSI KAMSSEEKKK
VVPRVSIFGG KAAPGYWMAK TIIHLINKVA DVVNKDPEIG DLLKVIFIAD YNVSKAEIIC
PASDISEHIS TAGTEGSGTS NMKFVLNGGL IIGTCDGANI EITREIGEQN IFLFGNLAED
VEDLRHRHFY GDFKLDPQLE RVFDAIKDNV FGDKADFSAL ISSIEEHGDY YLVSDDFNSY
ITTHGMVDEA FQNQEEWLAK SITSVARMGF FSMDRVTNEY ADSIWNVEPL DVTD
//
