ID A0A0V0XM55_TRIPS Unreviewed; 599 AA.
AC A0A0V0XM55;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Flags: Fragment;
GN Name=GlyP {ECO:0000313|EMBL:KRX89026.1};
GN ORFNames=T4E_379 {ECO:0000313|EMBL:KRX89026.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX89026.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX89026.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX89026.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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|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:KRX89026.1}.
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DR EMBL; JYDU01000212; KRX89026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XM55; -.
DR Proteomes; UP000054815; 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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX89026.1"
SQ SEQUENCE 599 AA; 69241 MW; 87DBD29BAF1CD1EB CRC64;
LIFLGIVKER SIVVCVEVAI MLTDREKRKQ ISIRGIAQVE NVANMKKAFN RHLHFTMMKD
RNVATPRDYF YSLAHTVRDH LTSRWIRTQQ HYHEKDPKGV NAVDESNRAG RAAHHCQSDA
FLFCSVHQHS HDLDRIYYLS LEFYMGRTLS NTMLNLGIQA ACDESLYQLG LDIEELQELE
EDAGLGNGGL GRLAACFLDS MATLGLAAYG YGLRYEYGIF KQTIKNGYQV EEPDDWLRFG
NPWEKARPEY MLPVNFYGKV IHDDKGRAHW VDTQLMFAMP YDTPVPGYQN NVVNTLRLWS
AKAETHFNLT FFNDGDYIQA VLDRNAAENI TRVLYPNDNC FEGRELRLKQ EYFLVAATLQ
DIIRRYRASK LAVSSSPGKI FQHFPDKVAI QLNDTHPAMA IPEFMRIMVD LESMTWNEAW
DICVRTFAYT NHTVLPEALE RWSCRMLENL LPRHLEIIYE INQKFLDSIL RRWPGDVDRM
RRMSLVEEAD QFGEKRINMA HLCIVGSHAV NGVAAIHSEI LKKTIFRDFY EMWPEKFQNK
TNGITPRRWL LLSNPSLADI IAEKIGEGWI TDLSQLEQLK SLTTNAGFLE AIHRVKQAC
//
