ID   A0A0N5C7L3_STREA        Unreviewed;       846 AA.
AC   A0A0N5C7L3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001392500.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001392500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0N5C7L3; -.
DR   STRING; 174720.A0A0N5C7L3; -.
DR   WBParaSite; SPAL_0001392500.1; SPAL_0001392500.1; SPAL_0001392500.
DR   Proteomes; UP000046392; Unplaced.
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   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   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; 1.
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|PIRSR:PIRSR000460-1,
KW   ECO:0000256|RuleBase:RU000587};
KW   Transferase {ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         682
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   846 AA;  97421 MW;  6C672D13E3ED3C04 CRC64;
     MQSDHEKRKQ ISVHGIAQVE NVSNIKNSFN RHLHFSVIKD RNVSTPRDYF NALALTVRDH
     LVSRWIRTQQ YYYEKDPKRI YYLSLEFYMG RTLSNTMINL GMQAACDEAL YQLGLDIEDL
     QEIEEDAGLG NGGLGRLAAC FLDSMATLGI PAYGYGLRYE YGIFKQTIVD GWQVEEPDNW
     LRYDNPWEKS RPEYMLPVNF YGRVEKDQNG KANWVDTQIV FAMPYDTPIP GYHNNVVNTL
     RLWSAKAENH FHLKFFNDGD YLQAVLDRNI SENITRVLYP NDNMFSGKEL RLKQQYFLVA
     ATLQDIIRRF KSSKYGCRDA VRADFSTFPD KVAIQLNDTH PSIGIPEFIR LLVDVEGLKM
     QQAWDVCVKT FAYTNHTLLP EALERWPVSL MSNLLPRHLE IIYEINQKFM DEVAQKYPGD
     FDRMRRMSIV EEADSMGEKR INMAHLCIVS SHAINGVAAL HSDLLKSQTF KDFYEFYPDR
     FQNKTNGITP RRWLLMSNPS LSEVISEKIG DGWITNLDEL QKLKEFSDDP TFLNDIMRVK
     QENKQKVAEW LKIEYGIKVN PESLFDVHVK RIHEYKRQLL NALHVITLYN RIKANPNGKY
     VPRTVMYGGK AAPGYHMAKQ IIKLINSVAA IVNNDPIVGD KLKVIFLENY RVSMAEKIIP
     AADLSEQIST AGTEASGTGN MKFMVNGALT IGTLDGANVE MAEEMGKENM FIFGMTVEEV
     EELQRKGYNS MDFINKNSEL KQIVDQIDGG FFTPDEPRLL QDLANSLKYH DRFLVCADYE
     SYIKCQDKVN TTYDDKEKWS QMALFNIASS GKFSTDRTIS EYAREIWNIT PGEIDLPAPY
     ERKPSS
//