ID   PHSL_VICFA              Reviewed;        1003 AA.
AC   P53536;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase L;
DE   Flags: Precursor;
GN   Name=PHO1;
OS   Vicia faba (Broad bean) (Faba vulgaris).
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; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fribo; TISSUE=Cotyledon;
RX   PubMed=8680306; DOI=10.1007/bf00196882;
RA   Buchner P., Borisjuk L., Wobus U.;
RT   "Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and
RT   expression patterns of cytosolic and plastidic forms in relation to
RT   starch.";
RL   Planta 199:64-73(1996).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in their
CC       regulatory mechanisms and in their natural substrates. However, all
CC       known phosphorylases share catalytic and structural properties.
CC   -!- FUNCTION: The L isoform exhibits higher affinity for unbranched
CC       substrates such as glucan-like amylose and maltodextrin.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC   -!- TISSUE SPECIFICITY: Found predominantly in cotyledons and early seed
CC       coat.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; Z36880; CAA85354.1; -; mRNA.
DR   PIR; S47243; S47243.
DR   AlphaFoldDB; P53536; -.
DR   SMR; P53536; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; P53536; -.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; PTHR11468; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Amyloplast; Carbohydrate metabolism; Chloroplast;
KW   Glycosyltransferase; Plastid; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..1003
FT                   /note="Alpha-1,4 glucan phosphorylase L isozyme,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000012294"
FT   REGION          71..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         849
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1003 AA;  113580 MW;  834E43BBED18535D CRC64;
     MASMTMRFHP NSTAVTESVP RRGSVYGFIG YRSSSLFVRT NVIKYRSVKR NLEFRRRSAF
     SVKCGSGNEA KQKVKDQEVQ QEAKTSPSSF APDTTSIVSS IKYHAEFTPL FSPEKFELPQ
     AFIATAQSVR DALIINWNAT YDYYEKLNVK QAYYLSMEFL QGRALLNAIG NLELTGPYAE
     ALSQLSYKLE DVAHQEPDAA LGNGGLGRLA SCFLDSLATL NYPAWGYGLR YKYGLFKQRI
     TKDGQEEVAE DWLEMGNPWE IVRNDVSYPV RFYGKVVSGS DGKKHWVGGE DIKAVAHDVP
     IPGYKTRSTI NLRLWSTKAA SEEFDLNAFN SGRHTEASEA LANAEKICYI LYPGDESIEG
     KTLRLKQQYT LCSASLQDII ARFERRSGAS VNWEDFPEKV AVQMNDTHPT LCIPELMRIL
     IDIKGLSWKD AWNITQRTVA YTNHTVLPEA LEKWSMDLME KLLPRHVEII EMIDEELIRT
     IIAEYGTADS DLLDKKLKEM RILENVELPA EFADILVKTK EATDISSEEV QISKEGGEEE
     ETSKEGGEEE EEKEVGGGRE EGDDGKEDEV EKAIAEKDGT VKSSIGDKKK KLPEPVPVPP
     KLVRMANLCV VGGHAVNGVA EIHSEIVKDD VFNAFYKLWP EKFQNKTNGV TPRRWIRFCN
     PDLSKIITQW IGTEDWILNT EKLAELRKFA DNEDLQTQWR EAKRNNKVKV AAFLRERTGY
     SVSPDSMFDI QVKRIHEYKR QLLNIFGIVY RYKKMKEMNA AERKENFVPR VCIFGGKAFA
     TYVQAKRIVK FITDVGATVN HDPEIGDLLK VIFVPDYNVS VAEMLIPASE LSQHISTAGM
     EASGTSNMKF AMNGCLQIGT LDGANVEIRE EVGADNFFLF GAKAREIVGL RKERARGKFV
     PDPRFEEVKK FVRSGVFGSY NYDELIGSLE GNEGFGRADY FLVGQDFPSY LECQEEVDKA
     YRDQKKWTRM SILNTAGSSK FSSDRTIHEY AREIWNIEPV KLE