ID   W9S7B1_9ROSA            Unreviewed;       892 AA.
AC   W9S7B1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=L484_015061 {ECO:0000313|EMBL:EXC30569.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC30569.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) 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}.
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DR   EMBL; KE346210; EXC30569.1; -; Genomic_DNA.
DR   RefSeq; XP_010111178.1; XM_010112876.1.
DR   AlphaFoldDB; W9S7B1; -.
DR   STRING; 981085.W9S7B1; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   Proteomes; UP000030645; 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: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; 3.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468:SF30; ALPHA-1,4 GLUCAN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 2.
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:UP000030645};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         743
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   892 AA;  101689 MW;  263B7370B23FDC31 CRC64;
     MERSRRGPPP AKPRRRVPNS DSDESTLFVI RARTRIGLLQ VVARVFGVLG LRIDRASVEF
     EGDFFVKKFF VTDSRGKKID DAESLERIRS ALIEAIDGDG DVSVGPATRG VVVRRLGLGT
     GSEERRAKAE RMFEMMDRFL KNDPISLQKD ILNHVEYTVA RSRFNFDDFE AYQGLSHCVR
     DRLIERWHDT QLHFKRKDPK RIYFLSLEYL MGRSLSNSVI NLGIRDECAE ALSQLGFEFE
     VLAEQEGDAA LGNGGLARLS ACQIDSLATM DYPAWGYGLR YQYGLFRQII LDGFQHEQPD
     HWLNFGNPWE IERIHVTYPV KVEAVAYDNP IPGYGTRNTI TLRLWAAKPS DHHDMESFNT
     GDYINAVVNR QKAETISSVL YPDDRSYQGK ELRLKQQYFF VSASIQDIIR RFKDSHDNFD
     VFPEKVALQL NDTHPSLAIA EVMRVLVDEE NIDWDRAWDI IIYDINFNFV DELKKKIGLD
     YDRLSRMSIV EEGAVKSIRS ANLSIVCSHT INGVSSVHFE LLKTKVFKDF YELWPQKFQY
     KTNGVSQRRW IVVSNPSLCA LISKWLGTEA WIRNSDLLTG LREHAADTNL QQEWQMVRKV
     NKMRLAEYIE AMSGLKVSLD AMFDVQIKRI HEYKRQLLNI LTIIHRYDCI KNMKESDRRK
     VVPRVCILGG KAAPGYEIAK KIIKLCHAVA EKINDDSDIG DLLKLVFIPD YNVSVAELVI
     PGADLSQHIS TAGHEASGTG SMKFAMNGCL LLATADGSTV EIIEEIGAEN MFLFGAKVNE
     VPALREKFSD VKVNLQFARV VRMVRDGYFG FQDYFKSLCD SVEGGNDFYL LGSDFESYLK
     AQAAADKAFV DKEKWTRMSI LSTAGSGRFS SDRTIEEYAE KSWGIEPCRC PF
//