ID A0A093ZCJ2_9PEZI Unreviewed; 886 AA.
AC A0A093ZCJ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=V491_05795 {ECO:0000313|EMBL:KFY15071.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY15071.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY15071.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY15071.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY15071.1}.
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DR EMBL; JPJT01003610; KFY15071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZCJ2; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR Proteomes; UP000029338; 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:UP000029338};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..33
FT /note="Disordered"
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 886 AA; 100353 MW; BF0A3A07AC3440E3 CRC64;
MATSTRPPRE RRPSTGSPIS DLKGPVGPPG FIRPKHKRTL TGFGAGEIKS VEASIPENQR
TAWKKYHAHP FTTVEDFEKE VVRHVETTLA RSMFNCDETA AYAAASLAFR NRLITEWNST
QQRQTFADGK RVYYLSLEFL MGRALDNAML NVGLKNVAKE GLADLGFRIE DIIEQEHDAA
LGNGGLGRLA ACFLDSLASL NYPAWGYGLR YRYGIFKQEI VDGYQVEVPD YWLDFNPWEF
PRHDVVVDIQ FYGEVRKYHD ENGKSRAEWE GGEIVKATAY DVPIPGYSTG VVNNLRLWSS
KAASGEFDFQ KFNSGDYESA VADEQRAETI SAVLYPNDNL ERGKELRLKQ QYFWVAASLY
DIVRRFKKSK RPWKEFPDQV AIQLNDTHPT LAIVELQRIL IDLEGLEWED AWSIVTKTFG
YTNHTVLPEA LEKWSVPLFQ NLLPRHLQII YDINLFFLQA VERKFPKERE LLSRVSIIEE
SSPKMIRMAY LAIVGSHKVN GVAELHSDLI KTTIFKDFVK IFGADRFTNV TNGITPRRWL
HQANPRLSEL IASKTGGFGF LKDLTLLNKL EDFVDDKEFK KEWAEIKHAN KVRLARHIKD
TTGVIVNPNA LFDIQVKRIH EYKRQQMNIF GVIHRYITIK SLSPEERKKL APRVSIFGGK
AAPGYWMAKS IIHLINSVGA VVNNDKDVGD LLKVIFIEDY NVSKAEIIIP ASDVSEHIST
AGTEASGTSN MKFVLNGGLI IGTCDGANIE ITREIGEQNI FLFGNLAEDV DDLRHTHTYS
SPPPDPDLAS VFSYIRNNTF GPSDDFAALI SAVEDHGDYY LVSDDFKSYI QTQELVDQAY
KEKDEWVGKC ITAVARMGFF SSDRCISEYA ESIWNVEPME ALAGDE
//
