ID A0A498HCN5_MALDO Unreviewed; 960 AA.
AC A0A498HCN5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=DVH24_037012 {ECO:0000313|EMBL:RXH69228.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH69228.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH69228.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH69228.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-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|ARBA:ARBA00001275,
CC 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:RXH69228.1}.
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DR EMBL; RDQH01000343; RXH69228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HCN5; -.
DR STRING; 3750.A0A498HCN5; -.
DR Proteomes; UP000290289; Chromosome 17.
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:SF28; ALPHA-GLUCAN PHOSPHORYLASE 1; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 2.
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:UP000290289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 516..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 806
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 960 AA; 108881 MW; BAD9082FC097825D CRC64;
MAASQFSATR SGPEAVWHCK SQSKLIDFCS RKNKSKLLFT RTSNRRRSFS FSVKNVLDKP
HELKDPIIEQ DAASAFSSFT PDTASIASSI KYHAEFTPLF SAEQFELPKA FYATAQSVRD
ALIVNWNATN NYYEKLNAKQ AYYLSMEFLQ GRALLNAVGN LELDGAYAEA LSKLGHKLEN
VANQEPDAAL GNGGLGRLAS CFLDSLATLN YPAWGYGLRY KYGLFKQQIT KDGQEEVAED
WLEMGNPWEI VRNDVSYPIK FYGKVVTGSD GKRHWIGGED IDAVAYDVPI PGYKTKTTIN
LRLWSTKASS QDFDLYAFNS GEHTKASEAL ANAEKICYVL YPGDESMEGK TLRLKQQYTL
CSASLQDIVA RFERRSGANV KWQEFPEKVA VQMNDTHPTL CIPELMRILI DLKGLDWKEA
WNITQRTVAY TNHTVLPEAL EKWSLELMEK LLPRHVQILE MIDEELIQTI ISEYGTADYD
LIDKKLKEMR ILENVDLPAK FADLIVKPKK SSIAVPSEEI EDSKEEDESA DESADEENVP
VKKHEEEKKK KVVVEPPKLV RMANLCVVGG HAVNGVAEIH SEIVKDEVFN SFYKLWPNKF
QNKTNGVTPR RWIRFCNPDL SNIITKWIGT EDWVLDTEKL AELRKFADDQ DLQTQWREAK
RNNKLKVVSL IKERTGYSVN PDAMFDIQVK RIHEYKRQLM NIMGIVYRYK KMKEMSASER
KSKFVPRVCM FGGKAFATYV QAKRIVKFIT DVGATVNCDP SIGDLLKVVF VPDYNVSVAE
QLIPASELSQ HISTAGMEAS GTSNMKFAMN GCILIGTLDG ANVEIREEVG EDNFFLFGAE
AHEIAGLRKE RAEGKFVPDP RFEEVKEFVK SGVFGSDNYD ELIGSLEGNE GFGRADYFLV
GKDFPSYIEC QEKVDEAYRD QKRWTRMSIL NTAGSYKFSS DRTIHEYAND IWNINPVELP
//