ID N4VDR8_COLOR Unreviewed; 886 AA.
AC N4VDR8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=GPH1 {ECO:0000313|EMBL:TDZ25760.1};
GN ORFNames=Cob_v000879 {ECO:0000313|EMBL:TDZ25760.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ25760.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ25760.1}.
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DR EMBL; AMCV02000001; TDZ25760.1; -; Genomic_DNA.
DR AlphaFoldDB; N4VDR8; -.
DR STRING; 1213857.N4VDR8; -.
DR EnsemblFungi; ENH80485; ENH80485; Cob_10546.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
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:UP000014480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 735
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 886 AA; 100093 MW; C8D5BC9EB1EC60BB CRC64;
MSGATEQRLP TRERRPSVGA PIVDIQGSVG PAGISRPKHK RTFTGFGAGE IKSVEASIPE
PQREAWNKAR AGPFTTKDDF EKDVVRHVET TLARSMFNCD ETAAYSAASL AFRDRLVKEW
NKTQQRQTLA DGKRVYYLSL EFLMGRALDN AMLNVGLKDV AKAGLDDLGF RIEDVIEQEH
DAALGNGGLG RLAACFLDSL ASLNFPAWGY GLRYRYGIFK QEIIDGYQVE VPDYWLDFNP
WEFPRHDVTV DIQFYGHVQK STDSNGKSTA SWEGGDTVTA VAYDVPIPGY ATPSTNNLRL
WSSKAASGEF DFQKFNSGDY ENSVADQQRA ETISAVLYPN DNLERGKELR LKQQYFWVAA
SLYDIVRRFK KSKRPWREFP DQVAIQLNDT HPTLAIVELQ RILVDLEKLE WDEAWNLVTA
TFGYTNHTVL PEALEKWPVG LVQHLLPRHL QIIYDINLFF LQSVEKMFPK DRDILGRVSI
IEESQPKMVR MAFLAIVGSH KVNGVAELHS DLIKTTIFKD FVSIYGPDKF TNVTNGITPR
RWLHQANPRL SDLIASKTGG HEFLKDLTQL NKLELSVNDK EFRKEWAEIK YANKVRLAKY
IKTTTGVSVN PAALFDVQVK RIHEYKRQQM NIFGVIHRYL TLKAMSPDER KKVAPRVSIF
GGKAAPGYWM AKQIIHLVNN VGAVVNNDED IGDLLKVIFL EDYNVSKAEM IIPASDLSEH
ISTAGTEASG TSNMKFVLNG GLIIGTCDGA NIEITREIGE NNIFLFGTLA EDVEDLRHAH
TYGSHTIDEN LAKVFKAIED GTFGSVSDFH ALISAVRDHG DYYLVSDDFN SYIETHHLVD
EAYKNQEEWI TKSITSVARM GFFSSDRCIN EYAEEIWNVE PLRIEE
//
