ID   A0A1S2Y6P1_CICAR        Unreviewed;       841 AA.
AC   A0A1S2Y6P1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=LOC101510928 {ECO:0000313|RefSeq:XP_004500220.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004500220.1};
RN   [1] {ECO:0000313|RefSeq:XP_004500220.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004500220.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_004500220.1; XM_004500163.3.
DR   AlphaFoldDB; A0A1S2Y6P1; -.
DR   GeneID; 101510928; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca5.
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:SF4; ALPHA-GLUCAN PHOSPHORYLASE 2, CYTOSOLIC; 1.
DR   PANTHER; PTHR11468; 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:UP000087171};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         687
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   841 AA;  95528 MW;  236578E44D6A67CB CRC64;
     MGSKVETNGG GSLVAAKVAA VANPLAEKPD EIASNISYHS QYSPHFSPFK FELEQAYYAT
     AESVRDRLIQ QWNETYLHFH KVDPKQTYYL SMEFLQGRAL TNAIGNLNIQ DAYADALRKF
     GLELEEITEQ EKDAALGNGG LGRLASCFLD SMATLNLPAW GYGLRYRYGL FKQIIAKEGQ
     EEVAEDWLEK FSPWEIVRHD ILYPVKFFGQ VEVNPDGSRK WVGGEVVQAL AYDVPIPGYK
     TKNTISLRLW EAKAHADDFD LFLFNDGQLE SASVLHSRAQ QICSVLYPGD ATEGGKLLRL
     KQQYFLCSAS LQDIISRFKE RRQGPWNWSE FPTKVAVQLN DTHPTLSIPE LMRLLMDDEG
     LGWDEAWEVT TKTIAYTNHT VLPEALEKWS QPVMWKLLPR HMEIIQEIDK RFATLISKTR
     LDLESELSTM RILDNNPQKP VVRMANLCVV SAHTVNGVAQ LHSDILKSEL FANYVSIWPT
     KFQNKTNGIT PRRWISFCSP ELSRIITKWL KTDQWVTNLD LLTGLRQFAD NEELQAEWLA
     AKMANKQRLA QYVLQVTGES IDPDSLFDIQ VKRIHEYKRQ LLNILGVIYR YKKLKEMSPE
     ERKSTTPRTV MFGGKAFATY TNAKRIVKLV DDVGAVVNID PEVNSYLKVV FVPNYNVSVA
     EVLIPGSELS QHISTAGMEA SGTSNMKFAL NGCLIIGTLD GANVEIREEI GEENFFLFGA
     TAEDVPRLRK EREDGLFKPD PRFEEAKKFI RSGVFGSYDY NPLLESLEGN SGYGRGDYFL
     VGYDFASYMD AQEKVDEAYR DKKRWLKMSI LSTAGSGKFS SDRTIAQYAK EIWNIEECRV
     P
//