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Database: UniProt
Entry: A0A498HCN5_MALDO
LinkDB: A0A498HCN5_MALDO
Original site: A0A498HCN5_MALDO 
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
//
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