ID A0A366RWZ8_9HYPO Unreviewed; 885 AA.
AC A0A366RWZ8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=FIESC28_04867 {ECO:0000313|EMBL:RBR21599.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR21599.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR21599.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR21599.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) 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:RBR21599.1}.
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DR EMBL; QKXC01000100; RBR21599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366RWZ8; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000253153; 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..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 734
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 885 AA; 100533 MW; 310FF57ED5F08E0A CRC64;
MASEQQRLPT RERRPSTSAP IVDIQGAVGP AGISRPKHTR TATGFGPSEI KSFEASIPEP
QREAWKRNQS KGFTGKDGFE QEVVRHVETT LARSVFNCDE HAAYSATSLA FRDRLILDWN
RTQQRQTYRD SKRVYYFSLE FLMGRALDNA MLNVGQKDTA KAGLAELGFR IEDIITQEND
AALGNGGLGR LAACFLDSLA SLNYPAWGYG LRYRYGIFKQ EIVDGYQVEV PDYWLDFNPW
EFPRHDVTVD IQFFGHVRKT TDANGKSVAI WEGGEIVQAV AYDVPIPGYD TPTTNNLRLW
SSKASGGEFD FQKFNNGDYE SSVADQQRAE TISAVLYPND NLERGKELRL KQQYFWVAAS
LYDIVRRFKK SNRPWKEFPE QVAIQLNDTH PTLAIVELQR ILIDIEHLEW DLAWDIVVNT
FGYTNHTVLP EALEKWPVGL IQHLLPRHLQ IIYDINLFFL QKVEKAFPND RDILRRVSII
EESQTKMVRM AFLAIVGSHK VNGVAELHSD LIKTTIFKDF VEIYGPDKFT NVTNGITPRR
WLHQANPRLS ELIASKVGGN GFLKDLTTLN QLEKYAEDKE FRKEWSEIKY ANKVRLAKLI
KSAVGVTVNP SALFDVQVKR IHEYKRQQLN IFGVIHRYLY LKSLSPEERR KVVPRVSIFG
GKAAPGYWMA KQIIHLVNAV GSVVNNDEDI GDLLKVIFLP DYNVSKAEII TPASDLSEHI
STAGTEASGT SNMKFVLNGG LIIGTCDGAN IEITREIGEN NIFLFGNLAE DVEDLRHSHQ
YGSHEIDPDL QKVFAEIEKG TFGSVHDFSA LVAAVRDHGD YYLVSDDFHS YNETHKLVDE
AYQNQEEWIK KTITSVSRMG FFSSDRCIDE YAESIWNAEP LVVHD
//
