ID K3VHL7_FUSPC Unreviewed; 885 AA.
AC K3VHL7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=FPSE_05893 {ECO:0000313|EMBL:EKJ73932.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ73932.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ73932.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ73932.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ73932.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFNW01000125; EKJ73932.1; -; Genomic_DNA.
DR RefSeq; XP_009257286.1; XM_009259011.1.
DR AlphaFoldDB; K3VHL7; -.
DR EnsemblFungi; EKJ73932; EKJ73932; FPSE_05893.
DR GeneID; 20364511; -.
DR KEGG; fpu:FPSE_05893; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000007978; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:EnsemblFungi.
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:0005980; P:glycogen catabolic process; IEA:EnsemblFungi.
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:UP000007978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..48
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; 100614 MW; ACCCB4CE052F52D4 CRC64;
MATEQQRLPT RERRPSTSAP IVDIQGAVGP TGISRPKHTR TATGFGPSEI KNFEASIPEP
QREAWKRNQS RGFTGKDGFE QEVVRHVETT LARSVLNCDE NAAYAATSLA FRDRLILDWN
RTQQRQTYRD SKRVYYFSLE FLMGRALDNA MLNVGQKDIA KAGLSELGFR IEDIITQEND
AALGNGGLGR LAACFLDSLA SLNYPAWGYG LRYRYGIFKQ EIVDGYQVEV PDYWLDFNPW
EFPRHDVVVD IQFFGHVRKT TDSNGKSVAI WEGGEIVQAV AYDVPIPGYD TPTTNNLRLW
SSKASGGEFD FQKFNNGDYE SSVADQQRAE TISAVLYPND NLDRGKELRL KQQYFWVAAS
LYDIVRRFKK SSRPWREFPD QVAIQLNDTH PTLAIVELQR ILIDIEHLEW DLAWDIVVKT
FSYTNHTVLP EALEKWPVGL IQHLLPRHLQ IIYDINLFFL QKVEKAFPND RDILGRVSII
EESQTKMVRM AFLAIVGSHK VNGVAELHSD LIKTTIFKDF VEIYGPDKFI NVTNGITPRR
WLHQANPRLS ELIASKVGGN GFLKDLTNLN QLEKYAEDKE FRKEWSEIKY ANKVRLAKLI
KSLVGVTVNP SALFDVQVKR IHEYKRQQLN IFGVIHRYLY LKSLAPEERK KVVPRVSIFG
GKAAPGYWMA KQIIHLVNAV GSVVNNDEDI GDLLKVIFLP DYNVSKAEII TPASDLSEHI
STAGTEASGT SNMKFVLNGG LIIGTCDGAN IEITREIGEN NIFLFGNLAE DVEDLRHNHQ
YGSHEIDPDL QKVFAEIEKG TFGSVHDFSA LVAAVRDHGD YYLVSDDFHS YNETHKLVDE
AYQNQEEWIK KTITSVSRMG FFSSDRCIDE YAESIWNTEP LVIHD
//
