ID B5AMJ9_MAIZE Unreviewed; 849 AA.
AC B5AMJ9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 13-SEP-2023, entry version 73.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=ZEAMMB73_Zm00001d034074 {ECO:0000313|EMBL:ONM09509.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF94692.1};
RN [1] {ECO:0000313|EMBL:ACF94692.1}
RP NUCLEOTIDE SEQUENCE.
RA Yan H., Jiang H., Wu G.;
RT "Compare of the starch synthesis correlative genes between rice and maize:
RT copies, chromosome location and function.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ONM09509.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM09509.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU857640; ACF94692.1; -; mRNA.
DR EMBL; CM007647; ONM09509.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM09512.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM09520.1; -; Genomic_DNA.
DR AlphaFoldDB; B5AMJ9; -.
DR SMR; B5AMJ9; -.
DR ExpressionAtlas; B5AMJ9; baseline and differential.
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; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 2: Evidence at transcript level;
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 406..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 695
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 849 AA; 96004 MW; C2D8BF9798E46793 CRC64;
MNVKQAYYLS MEFLQGRALT NAIGNLEITG EYAEALKQLG QNLEDVASQE PDAALGNGGL
GRLASCFLDS LATLNYPAWG YGLRYEYGLF KQIITKDGQE EIAENWLEMG YPWEVVRNDV
SYPVKFYGKV VEGTDGRKHW IGGENIKAVA HDVPIPGYKT RTTNNLRLWS TTVPAQDFDL
AAFNSGDHTK AYEAHLNAKK ICHILYPGDE SLEGKVLRLK QQYTLCSASL QDIIARFESR
AGESLNWEDF PSKVAVQMND THPTLCIPEL MRILMDVKGL SWSEAWSITE RTVAYTNHTV
LPEALEKWSL DIMQKLLPRH VEIIETIDEE LINNIVSKYG TTDTELLKKK LKEMRILDNV
DLPASISQLF VKPKDKKESP AKSKQKLLVK SLETIVDVEE KTELEEEAEV LSEIEEEKLE
SEEVEAEEES SEDELDPFVK SDPKLPRVVR MANLCVVGGH SVNGVAEIHS EIVKQDVFNS
FYEMWPTKFQ NKTNGVTPRR WIRFCNPALS ALISKWIGSD DWVLNTDKLA ELKKFADNED
LHSEWRAAKK ANKMKVVSLI REKTGYIVSP DAMFDVQVKR IHEYKRQLLN ILGIVYRYKK
MKEMSTEERA KSFVPRVCIF GGKAFATYIQ AKRIVKFITD VAATVNHDSD IGDLLKVVFV
PDYNVSVAEA LIPASELSQH ISTAGMEASG TSNMKFAMNG CILIGTLDGA NVEIREEVGE
ENFFLFGAEA HEIAGLRKER AEGKFVPDPR FEEVKEFVRS GVFGTYSYDE LMGSLEGNEG
YGRADYFLVG KDFPSYIECQ EKVDEAYRDQ KLWTRMSILN TAGSSKFSSD RTIHEYAKDI
WDISPAILP
//
