ID A0A1Y1ULV8_9TREE Unreviewed; 924 AA.
AC A0A1Y1ULV8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BD324DRAFT_644771 {ECO:0000313|EMBL:ORX39038.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX39038.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX39038.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX39038.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) 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:ORX39038.1}.
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DR EMBL; NBSH01000003; ORX39038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1ULV8; -.
DR STRING; 4999.A0A1Y1ULV8; -.
DR InParanoid; A0A1Y1ULV8; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000193218; Unassembled WGS sequence.
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; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
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:UP000193218};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 768
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 924 AA; 104074 MW; 4AA30588B3EF3637 CRC64;
MSALTKDNLE KLPNAVPPGH RTPSLHQPTL SRRSSISAGH GQASGPTRDV DISQIGIPVH
TPRKERPSHQ RSLTGSYFPS TAHKVSDEDW PIGDKTTWQT AMQAEEVDPE NTQDVANSIV
RHVTTTLARQ AINVDTLAAY QATALSVRDQ LLKRWNETTG YHTARAPKRI YYLSIEWLLG
RSLDNAVLNL GMKNTYEDAT RKLGFNFEDL IDEERDAGLG NGGLGRLAAC YIDSMATLNL
PGWGYGLRYQ YGIFKQLLSN SGEQLEAPDP WLDRESPWEI PRLDVTYPIR FYGHVENVAN
SDRAIWSGGQ ECLAVAYDTP IPGYGTKNCA NIRLWKAVPQ AGFDLNSFNA GNYEASVAAS
SDVGNITQVL YPNDNMYQGK LLRLKQQALW TSASLQDILR RFSKLDRPWS ELPDYVCIQM
NDTHPTLAIP ELMRILIDEE DIPYSQAWKI VTKVFAYTNH TVLPEALEKW ELSLFENLLP
RHLQLIYKIN YEFMGQVAKR WPGDMDRLRR MSIIEEGTPK YVRMAYLAIV GSFKVNGVAE
LHSQLLQSTI FRDFVEFKGR DFFTNVTNGI TPRRWLLQCN PSLAALATHT LGSDHWLVES
KQLSKLIPMA DNPKFREAFR SIKQENKARL AEVLEKELGV SINVNSIFAA QIKRLHEYKR
QTLNVFGIIA RYLRIKKASP EERKKIQPWT FIFAGKAAPG YYIAKLVIRL INNVAKVVNN
DPAVGDLLRV CFIPDYSVSI AEVLIPAADI SVQISTAGTE ASGTSNMKLA LNGALLLGTV
DGANIEIAED SGEDQCFMFG HLAEQVQDVR YNNSYNPTSL EQRSPELYEV FKFIESGAFG
EGQIYEALLK TVYDHDYYLV SNDFGSYLEA QRLVDELWGS DQDEWTKKSI ITSFSMGDFS
SDRSVQDYAD GIWNVAAERV PDDQ
//
