ID A0A444X8G9_ARAHY Unreviewed; 980 AA.
AC A0A444X8G9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, 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=Ahy_B10g105641 {ECO:0000313|EMBL:RYQ85988.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ85988.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ85988.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ85988.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYQ85988.1}.
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DR EMBL; SDMP01000020; RYQ85988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444X8G9; -.
DR STRING; 3818.A0A444X8G9; -.
DR Proteomes; UP000289738; Chromosome b10.
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:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 826
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 980 AA; 110727 MW; 13B46C19029BDF39 CRC64;
MASPSPMRLS SATAGSMRTQ GLLGCSSVSG IIGAASRSSR SKLLMMRNTA KLNLTMMRNR
RSSFTLVKCV SSSEAPQKLQ EQDPLSHEHE TTTSLGSFTP DATSIASSIK YHAEFTPLFS
PENFELPQAF CATAQSVRDA LIINWNATYD YYEKLNVKQA YYLSMEFLQG RALLNAIGNL
ELTGSYAEAL SKLGYKLEDV AGQEPDAALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK
YGLFKQRITK DGQEEVAEDW LEMGNPWEIV RNDVSYPVKF YGQIVSGSDG KKHWIGGEDI
LAVAHDVPIP GYKTKSTINL RLWSTKAASE EFDLYAFNAG KHTEANEALA NAEKICYILY
PGDESIEGKT LRLKQQYTLC SASLQDIITR FERRSGATVN WEEFPEKVAV QMNDTHPTLC
IPELMRILID IKDLSWEDAW NITQRTVAYT NHTVLPEALE KWSLDLMQKL LPRHVEIIEM
IDHELIRTII TEYGTSDSKL LEKKLKEMRI LDNVELPVEF ADVLVKPDET IEPHDELENP
EQEVEKDNNE EAKEAGEEII AKEDEKEALL QPVPELPKLV RMANLCVVGG HAVNGVAEIH
SEIVKDEVFN SFYQLWPEKF QNKTNGVTPR RWIRFCNPAL SKIITKWIGT EDWVLNTEKL
AELRKFADNE DLQKQWREAK RANKMKVAAL IRERTGYSVS ADAMFDIQVK RIHEYKRQLL
NILGIVYRYK KMKEMTPKER KANFVPRVCI FGGKAFATYV QAKRIVKFIT DVGATVNHDP
EIGDLLKVIF VPDYNVSVAE MLIPASELSQ HISTAGMEAS GTSNMKFAMN GCILIGTLDG
ANVEIREEVG EDNFFLFGAK AHEIAGLRKE RAEGKFVPDP RFEEVKKFVR SGVFGPYNYD
ELMGSLEGNE GFGRADYFLV GKDFPSYIEC QEKVDKAYQD QKTWTRMSIL NTAGSHKFSS
DRTIHEYARD IWNIEPVELP
//
