ID A1CPG9_ASPCL Unreviewed; 881 AA.
AC A1CPG9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=ACLA_022540 {ECO:0000313|EMBL:EAW07540.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07540.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07540.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07540.1; -; Genomic_DNA.
DR RefSeq; XP_001268966.1; XM_001268965.1.
DR AlphaFoldDB; A1CPG9; -.
DR STRING; 344612.A1CPG9; -.
DR EnsemblFungi; EAW07540; EAW07540; ACLA_022540.
DR GeneID; 4700977; -.
DR KEGG; act:ACLA_022540; -.
DR VEuPathDB; FungiDB:ACLA_022540; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:EnsemblFungi.
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:0005980; P:glycogen catabolic process; IEA:EnsemblFungi.
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:UP000006701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 730
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 881 AA; 100329 MW; 22ECA211BD4BA88A CRC64;
MSAPSSPRRE RKPSVGAPIP LQGPVGPGFS RPKHKRTYTG FGPAEIKSVE ASIPEPLREA
WTKHSASGFA NKEEFERELV RHVETTLARS LYNCDELAAY SGTALAFRDR LIIEWNKTQQ
RQTFADQKRV YYLSLEFLMG RALDNAMLNV GMKDAAREGL KDLGFRVEDV INQEHDAALG
NGGLGRLAAC FLDSMATLNY PAWGYGLRYR YGIFKQEIVN GYQVEIPDYW LDFNPWEFPR
HDITVEIQFY GWVKTYQDDN GKTVHSWQDG EMVQAVAYDV PIPGYGTKTT NNLRLWSSKA
ASGEFDFQKF NAGDYESAVA DQQRAETISA VLYPNDNLER GKELRLKQQY FWCAASLFDI
VRRFKKTKRA WSEFPDQVAI QLNDTHPTLA IVELQRILVD QEGLEWDEAW RLVTKTFGYT
NHTVLPEALE KWSVPLMQNL LPRHLEIIYD INLFFLQSVE KRFPNDRAML SRVSIIEESH
PKMVRMAHIA IIGSHKVNGV AELHSDLIKT TIFKDFVEIY GPDKFTNVTN GITPRRWLHQ
ANPRLSDLIA SKLGGYEFLK DLTLLDQLEA YVDDKAFRAE WSEIKTANKL RLAKHIKDTT
GYSVNPKALF DVQVKRIHEY KRQQLNIFGV IHRYLTIKSM SKEDREKLVP RVSIFGGKAA
PGYWMAKTII HLINKVAAVV NNDPDVGDLL KVIFIEDYNV SKAEIICPAS DISEHISTAG
TEASGTSNMK FVLNGGLIIG TCDGANIEIT REIGEQNIFL FGTLAEDVEE LRHRHFYGEF
QLDPHLSKVF DAIRSDTFGD ASNFSALISS ITEHGDFYLV SDDFNSYITT QEIVDEAFKN
QDEWIAKSIT SVARMGFFST DRVISEYADS IWNIEPLDMK D
//
