ID A0A445FBI3_GLYSO Unreviewed; 981 AA.
AC A0A445FBI3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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_050288 {ECO:0000313|EMBL:RZB46212.1};
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:RZB46212.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB46212.1, 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:RZB46212.1};
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|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:RZB46212.1}.
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DR EMBL; QZWG01000019; RZB46212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445FBI3; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000289340; Chromosome 19.
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:UP000289340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 526..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 827
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 981 AA; 110373 MW; 6861F4ABB2E85160 CRC64;
MASSSTTMRF SAASTGAEAA LPRRSSVAGF IGVAARSSAK SRLRFIGRNA NLSLRMRRMS
SFSVVKCVSG SEAKVQDTVA KQQEATTSLS SFTPDASSIA SSIKYHAEFT PLFSPENFDL
PQAFLATAQS VRDSLIINWN ATYDYYEKLN VKQAYYLSME FLQGRALLNA IGNLELTGPY
AEALSKLGHK LESVAYQEPD AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ
RITKDGQEEV AEDWLEMGNP WEIIRNDVSY PVKFYGKVVS GSDGKKHWIG GEDIKAVAHD
VPIPGYKTKT TINLRLWSTK AASEEFDLSA FNAGRHTEAS EALANAEKIC YILYPGDEPI
EGKILRLKQQ YTLCSASLQD IIARFERRSG ANVNWEEFPE KVAVQMNDTH PTLCIPELMR
ILIDVKGLNW KDAWNITQRT VAYTNHTVLP EALEKWSLDL MQKLLPRHIE IIEMIDEELV
RTIIAEYGTE NSDLLEKKLK EMRILENVEL TAEFADILVK SKEAIDIPSE EQQSSEQAEA
EDEKDDDEVE AVAKKNGTDE SSIEDEKEEL PEPVPEPPKL VRMANLCVVG GHAVNGVAEI
HSEIVKDDVF NAFYKLWPEK FQNKTNGVTP RRWIRFCNPD LSKIITEWIG TEDWVLNTGK
LAELRKFVDN EDLQVQWREA KRSNKVKVAA FIREKTGYSV SPDAMFDIQV KRIHEYKRQL
MNIFGIVYRY KKMKEMSAAE REANFVPRVC IFGGKAFATY VQAKRIVKFI TDVGATVNHD
PEIGDLLKVV FVPDYNVSVA EMLIPASELS QHISTAGMEA SGTSNMKFAM NGCILIGTLD
GANVEIREEV GADNFFLFGA KAHEIAGLRK ERAEGKFVPD PRFEEVKEFV RSGVFGSYNY
DELMGSLEGN EGFGRADYFL VGKDFPSYIE CQEKVDEAYR DQTKWTRMSI LNTAGSYKFS
SDRTIHEYAR EIWNIEPVQL P
//
