ID F9G3H5_FUSOF Unreviewed; 885 AA.
AC F9G3H5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=FOXB_13207 {ECO:0000313|EMBL:EGU76307.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU76307.1};
RN [1] {ECO:0000313|EMBL:EGU76307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU76307.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(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:EGU76307.1}.
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DR EMBL; AFQF01003306; EGU76307.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G3H5; -.
DR STRING; 660025.F9G3H5; -.
DR PaxDb; 5507-FOXG_06319P0; -.
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; 100468 MW; 7E925BF7F8CF6B69 CRC64;
MASEQQRLPT RERRPSTSAP IVDIQGAVGP AGISRPKHTR TATGFGPSEI KSFEASIPEP
QREAWKRNQS SGFTGKDGFE KEVVRHVETT LARSVFNCDE HAAYSATSLA FRDRLILDWN
RTQQRQTYRD SKRVYYFSLE FLMGRALDNA MLNVGQKDTA KAGLAELGFR IEDIITQEND
AALGNGGLGR LAACFLDSLA SLNYPAWGYG LRYRYGIFKQ EIVDGYQVEV PDYWLDFNPW
EFPRHDVTVD IQFFGHVRKT TDENGKSVAI WEGGEIVQAV AYDVPIPGYD TPTTNNLRLW
SSKASGGEFD FQKFNNGDYE SSVADQQRAE TISAVLYPND NLERGKELRL KQQYFWVAAS
LYDIVRRFKK SNRPWKEFPD QVAIQLNDTH PTLAIVELQR ILIDIEHLEW DLAWEIVVNT
FGYTNHTVLP EALEKWPVGL IQHLLPRHLQ IIYDINLFFL QKVEKAFPND RDILRRVSII
EESQTKMVRM AYLAIVGSHK VNGVAELHSD LIKTTIFKDF VEIYGPDKFT NVTNGITPRR
WLHQANPRLS ELIASKVGGN GFLKDLTTLN QLEKYADDKE FRKEWSEIKY ANKVRLAKLI
KSAVGVTVNP AALFDVQVKR IHEYKRQQLN IFGVIHRYLH LKSLSPEERK KVVPRVSIFG
GKAAPGYWMA KQIIHLVNAV GSVVNNDEDI GDLLKVIFLP DYNVSKAEII TPASDLSEHI
STAGTEASGT SNMKFVLNGG LIIGTCDGAN IEITREIGEN NIFLFGNLAE DVEDLRHSHQ
YGSHEIDPDL QKVFAEIEKG TFGSVHDFSA LVAAVRDHGD YYLVSDDFHS YNETHKLVDE
AYQNQEEWIK KSITSVSRMG FFSSDRCIDE YAESIWNAEP LVVHD
//
