ID A0A445F036_GLYSO Unreviewed; 955 AA.
AC A0A445F036;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=D0Y65_052925 {ECO:0000313|EMBL:RZB42146.1};
OS Glycine soja (Wild soybean).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB42146.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB42146.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB42146.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-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|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:RZB42146.1}.
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DR EMBL; QZWG01000020; RZB42146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445F036; -.
DR Proteomes; UP000289340; Chromosome 20.
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:SF27; ALPHA-1,4 GLUCAN PHOSPHORYLASE L-2 ISOZYME, CHLOROPLASTIC_AMYLOPLASTIC; 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; 2.
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:UP000289340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 514..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..556
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 824
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 955 AA; 109157 MW; 1B400B782318B8D8 CRC64;
MAALPFSTTC RHSNSPLHHN SKTSFIGFSQ RNNIWQLFVI TKSNSRRAIR KLCVKNVTSD
KKQELEEPLN EQDTFNEFVP DSASIASSIK FHAEFTSPFS PEKFELNKAF FATAESVRDS
LIINWNATND YYERMNVKQA YYMSMEYLQG RALLNAIGNL QLSGPYAEAL RKLGHNLEDV
ANKEPDAALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK YGLFKQHITK DGQVEVAENW
LEMGNPWEIL KNDVSYPVKF YGEVISGPNG SKQWVGGENI LAVAYDVPIP GYKTRTTINL
RLWSTKVSPE EFDLQAYNSG DHAKAYAVMK NAEKICYVLY PGDESIDGKT LRLKQQYTLC
SASLQDIFAR FERRLGKRVN WDTLPDKVVV QMNDTHPTLC IPEIIRILVD VKGLSWEKAW
NITKRTVAYT NHTILPEALE KWSLTLLQDL LPRHMEIIRK IDEELINEII SEYGIDDLDL
FQQRLKKMRI LENIELPNSV MELLSITEET PAVDPVKEID VDDTDVKATE KEDGDDDDDY
EVVEEEQEED NEEPSVEEDT SNKIELKFKV DPKLPMMVRM ANLCVVGGFS VNGVAEIHSK
IVKEEVFDEF YKLWPEKFQN KTNGVTPRRW IRFCNPDLSK IITKWIGTED WVTDLEKLAI
LRKFADNEDL QLEWIEAKRR NKIRVASFLK EKTGYVVNPN AMFDVQVKRI HEYKRQLLNI
LGIVYRYKKM KELSAEERKD MFVPRVCIFG GKAFATYVQA KRIVKFITDV GATINSDPEI
GDLLKVVFVP DYNVSVAEML IPGSELSQHI STAGMEASGT SNMKFAMNGC IVIGTLDGAN
VEIREEVGED NFFLFGARAQ EIVGLRKERV EGKFVPDPRF EEVKAYVRSG VFGPYNYEEL
MGSLEGNEGY GRADYFLVGK DFPSYLECQE EVDKAYHDQK VNVISLLRNK TYIFI
//
