ID A0A094GGZ4_9PEZI Unreviewed; 747 AA.
AC A0A094GGZ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Flags: Fragment;
GN ORFNames=V498_03411 {ECO:0000313|EMBL:KFY95315.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY95315.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY95315.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFY95315.1}.
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DR EMBL; JPKA01000593; KFY95315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094GGZ4; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR Proteomes; UP000029270; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..38
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"
FT NON_TER 747
FT /evidence="ECO:0000313|EMBL:KFY95315.1"
SQ SEQUENCE 747 AA; 84553 MW; 05BB801395E04CCD CRC64;
MATPSSPPRE RRPSTGSPIS DLKGPIGPGF TRPKHKRTLT GFGASEIKSV EASIPENQRT
AWNKYHTKPF TNVEDFEKEV VRHVETTLAR SMFNCDETAA YAAASLAFRN RLITEWNSTQ
QRQTFADGKR VYYLSLEFLM GRALDNAMLN VGLKDVAKEG LADLGFRIED IIEQEHDAAL
GNGGLGRLAA CFLDSLASLN YPAWGYGLRY RYGIFKQEIV DGYQVEVPDY WLDFNPWEFP
RHDVVVDIQF YGEVRKYHDE DGKSHAEWEG GEIVKATAYD VPIPGFDTAV VNNLRLWSSK
AASGEFDFQK FNSGDYESAV ADEQRAETIS AVLYPNDNLD RGKELRLKQQ YFWVAASLYD
IVRRFKKSKR AWKEFPDQVA IQLNDTHPTL AIVELQRILI DLEGLEWDDA WSIVTKTFGY
TNHTVLPEAL EKWSVPLFQN LLPRHLQIIY DINLLFLQAV ERKFPKEREL LARVSIIEES
TPKMVRMAYL AIVGSHKVNG VAELHSDLIK TTIFKDFVKI FGEDRFTNVT NGITPRRWLH
QANPRLSELI ASKTGGIGFL KDLTLLNKLE EFVDDKEFKK EWAEIKLANK VRLARHIKDT
TGVVVNPHAL FDIQVKRIHE YKRQQMNIFG VIHRYITIKS LSPEERKKCA PRVSIFGGKA
APGYWMAKSI IHLINSVGAV VNNDKDVGDL LKVIFIEDYN VSKAEIIIPA SDVSEHISTA
GTEASGTSNM KFVLNGGLII GTCDGAN
//
