ID K7M1G7_SOYBN Unreviewed; 1002 AA.
AC K7M1G7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=100779066 {ECO:0000313|EnsemblPlants:KRH21364};
GN ORFNames=GLYMA_13G235600 {ECO:0000313|EMBL:KRH21364.1};
OS Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EMBL:KRH21364.1};
RN [1] {ECO:0000313|EMBL:KRH21364.1, ECO:0000313|EnsemblPlants:KRH21364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH21364};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH21364.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH21364}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH21364};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH21364.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH21364.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-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}.
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DR EMBL; CM000846; KRH21364.1; -; Genomic_DNA.
DR RefSeq; XP_006594571.1; XM_006594508.2.
DR AlphaFoldDB; K7M1G7; -.
DR SMR; K7M1G7; -.
DR STRING; 3847.K7M1G7; -.
DR PaxDb; 3847-GLYMA13G30920-2; -.
DR EnsemblPlants; KRH21364; KRH21364; GLYMA_13G235600.
DR GeneID; 100779066; -.
DR Gramene; KRH21364; KRH21364; GLYMA_13G235600.
DR KEGG; gmx:100779066; -.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; K7M1G7; -.
DR OMA; HGIKYEY; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR ExpressionAtlas; K7M1G7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR002912; ACT_dom.
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:SF30; ALPHA-1,4 GLUCAN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51671; ACT; 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|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT DOMAIN 73..154
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 1002 AA; 113533 MW; A97D85F1F7FA9C52 CRC64;
MQTIISFPHL TPFPNQLSPV PFPSLTHFSS LSIPRSLTVA HWRILLRAST SESISTSTST
IAVDNSDSAD STAFVIRARN QIGLLQVITR VFKVLGLTVD RATVEFEGDF FVKTFFVTDS
HGNKIEDSDS LQRIKRALAE AIAGEDDGGN GTISVTRSAA NRGIVVRRPG LAEAIGERRA
KAERMFSLMD GFLKNDPLTL QKDILNHVEY TVARSRFSFD DFEAYQALSH SVRDRLIERW
HDTHVYVKRT KPKRLYFLSL EFLMGRSLSN SVINLGIQDQ YAEALSQLGF EFEVVAEQEG
DAALGNGGLA RLSACQMDSL ATLDYPAWGY GLRYEYGLFR QIIVDGFQHE QPDYWLNYGN
PWEIERIHVT YEVKFYGTVE EVEMNGEKHQ VWVPGETVEA VAYDNPIPGY GTRNTINLRL
WAAKPSNKFD LEAYNTGDYI NSVVNRQRAE TISNVLYPDD RNHQGKELRL KQQYFFVSAS
LQDIIRRFKE AHNNFDELPD KVALHLNDTH PSLSIAEIMR ILVDEEHLVW NKAWDIACKV
FSFTTHTVVA EGLEKIPVDL LGSLLPRHLQ ILYEINFKFM EELKKKIGLD YNRLSRMSIV
EEGAVKSIRM ANLSIVGSHA VNGVSKLHLD TLKMNTFKDF YELWPEKFQY KTNGVTQRRW
IVVSNPSLCA LISKWLGTEA WIRNADLLTG LRDLVDNTDF HQEWKMVKKV NKMRLAEYIE
TMSGVKVSLD AMFDVQVKRI HEYKRQLLNI LGIIHRYDCI KNMDKNDRRK VVPRVCIIGG
KAAPGYEIAK KIIKLSHAVA EKINNDTDIG DLLKLVFIPD YNVSVAELVI PGADLSQHLS
TAGHEASGTG SMKFMMNGCL LLATADGSTI EIIEEIGSDN LFLFGAKVQE VAELREKGST
LKVPLQFARV LRMVRDGYFG HKDYFESLCD TVEIGNDFYL LGPDFGSYLE AQAAADKAFV
EPEKWIKMSI LSVAGSGRFS SDRTIQDYAE RTWKIDPCRC PL
//
