ID A0A0V0VKZ0_9BILA Unreviewed; 1537 AA.
AC A0A0V0VKZ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=T09_1531 {ECO:0000313|EMBL:KRX64185.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64185.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64185.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64185.1};
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:KRX64185.1}.
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DR EMBL; JYDN01000025; KRX64185.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0VKZ0; -.
DR Proteomes; UP000054681; 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 1.10.418.70; Intraflagellar transport protein 81, N-terminal domain; 1.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR041146; IFT81_CH.
DR InterPro; IPR043016; IFT81_N_sf.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR Pfam; PF18383; IFT81_CH; 1.
DR Pfam; PF00343; Phosphorylase; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT DOMAIN 955..1074
FT /note="IFT81 calponin homology"
FT /evidence="ECO:0000259|Pfam:PF18383"
FT COILED 1086..1144
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1258..1324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1387..1496
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1537 AA; 177178 MW; 77674096F674B1FF CRC64;
MPDFSRNSET AIDCCLRSSW LAETDSLHSN IFGLKIMLTD REKRKQISIR GIAQVENVAN
MKKAFNRHLH FTMMKDRNVA TPRDYFYSLA HTVRDHVTSR WIRTQQHYHD KDPKRVYYLS
LEFYMGRTLS NTMLNLGIQA ACDESLYQLG LDIEELQELE VDAGLGNGGL GRLAACFLDS
MATLGLAAYG YGLRYEYGIF KQVIKNCCQV EEPDDWLRFG NPWEKARPEY MLPVNFYGKV
VHDDKGRAHW VDTQLMFAMP YDTPVPGYQN NVVNTLRLWS AKAENHFNLT FFNDGDYIEA
VLDRNAAENI TRVLYPNDNC FEGRELRLKQ EYFLVAATLQ DIIRRYRASK LAATSAPGKV
FQNFPEKVAI QLNDTHPAMA IPEFMRIMVD LESMTWDEAW DICVRTFAYT NHTVLPEALE
RWSCALLENL LPRHLEIIYE INQKFLDSVL RRWPGDLDRM RRMSLVEEAD QYGEKRINMA
HLCIVGSHAV NGVAAIHSEI LKKSVFHDFY EMWPEKFQNK TNGITPRRWL LLSNPSLADV
IAEKIGEAWI TDLSQLERLK PLVKNVGFLE AIRRVKQARL MNGIFLVFHE NKMRAAQWLA
DTYNLELNPS SMFDIQVKRI HEYKRQLLNV FHVITMYNRI KKDPALKVVP RTVMIGGKAA
PGYYMAKLII QLINCVADVV NHDPIIGNKL KLIFLENYRV TLAEKIIPAA DLSQQISTAG
TEASGTGNMK FMLNGALTIG TLDGANVEMM EEMGKENIFI FGMTEEEVNA LQHAGYNSMT
YIEKNAELKQ CIEQIETGFF SPNNPGLFKD ITNMLKYHDR FYLCADFEAY LKCQEDVNKA
FLDTNRWTQM ALYNIASSGK FSSDRTIKEY AKDIWNVPVS TEKLPAPFAG PQFEENSSKA
DNNNDAAVVD ATKATAAARN AVPTTPTSPK ALRWYDLNWS SSTDSWLLSI QTKMEEMKFV
ISELNRPPYN QTLSLVELDA LEPFQLLQLL SDTLCLLAKE KRVEVKPQTV TEVSLRVLEW
LTLLRYASSM EKDEFHRAIA GGNKETIFKA LAWILRRQNE VEQRLYLSKF LIPIKVPVDF
LQDVEVEQLN KECENLMEEF KELHKEFMKV KTAAEARITV SSDIASMESE KEALLKRLER
AKSKVNNLPD FENLLHVCRE FRQEAERSDA LSKTKKDQSF SLKNVRQQLR HINQQIDKLE
LEADTTSPRE KLNQLEDELR VLQYIAEEKL PQDIELNRKT VGKLSEIIQQ SPFEKADLQE
LDSQVEEVEK EIEKLQNDLK VQKNASENKL EVYRHQADIV ARKKNDALNT LQHLMLQLQQ
AEQGQSKKSN ENVFFVQSNL DQIKNTARND SSSRVDDVIN LRSSFPEMST KDSVDGISDT
EKNDVRNGHS YEELKKLQEA YQNLSDEMQV KKAKYNAVVV EEQSVLLELE KEVNALQQDA
ELSELQVSKL NDQESFLTSR FNDMKQRDDH ELICIMEETA ERMKLAEETY RKVREEEQSI
IRIKDDIMLE NICSLNEAKS LLKLKLLFSK KNEPLSK
//
