ID A0A168MS14_ABSGL Unreviewed; 776 AA.
AC A0A168MS14;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=ABSGL_04662.1 scaffold 5760 {ECO:0000313|EMBL:SAL99081.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL99081.1};
RN [1] {ECO:0000313|EMBL:SAL99081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL99081.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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}.
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DR EMBL; LT552478; SAL99081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168MS14; -.
DR STRING; 4829.A0A168MS14; -.
DR InParanoid; A0A168MS14; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000078561; 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: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; 4.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 2.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
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:UP000078561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 626
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 776 AA; 87957 MW; 89E1204A5E0FD39E CRC64;
MASHTSRPVP QRRRSLPNVT SKRMMDVVIH GDVQPVAATE VPSRGLKYAP LHANALARWK
SLAPHDLATP EHIERSIVYH TTYTLCRHRY NVDKTALYTA TSYSVRDLLL QDWNATQEKL
HETNPKQCYY LSMEFLLGRA LDNALYCLST KKEYASSVKA LGFSLEDLLE EERDAALGNG
GLGRLAACYM DSVATLEYPV SGYGLRYQYG IFKQIINKEG YQDERPDYWL DSYNTKNCGN
IRLWESQPQH LFDFAAFNSG DYDKAVGEQK RAANLTAVLY PNDNHDSGKE LRLKQEYFWV
CASLQDIIRR FKRSKRPWKD FSHQVALQLN DTHPIMAIVE LQRLLVDVEG LSWDAAWDIV
TKTFAFTNHT VLPEALERWP VPLMERLLPR HMQIIYDINL FFLQKVEKAF PGDRDLLNRM
SIIEESNPQQ VRMAYLGVVG SSKVNGVAAL HSDLVKKDLF PDFVKYFGPD KFINITNGIT
PRRWLYQANP ALRDLITDTL GSEKWVCHLD ELIHEYKRQL LNILGVIHRY RELLDMTASE
RATVVPRVVI FGGKSAPGYH VAKMVIKLIN SVATVVNNDD SIGDLLKVVF IPDYKVSLAE
IITPASDISQ HISTAGTEAS GTSNMKFVLN GGLILGTVDG ANIEIRDEIG HDNIFMFGTL
ADKVPDIRHT QKFYGVLLDA NLQGVLDFIA TGAFGDGSVF NPLIDTLTYG GDYYLISEDF
DSYLKKQADV DNAFRDKTVW ARKSIMCTAG MGFFSSDRAV REYADKIWNM KPQPLE
//
