ID A0A075AHF4_9TREM Unreviewed; 884 AA.
AC A0A075AHF4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, 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};
GN ORFNames=T265_03696 {ECO:0000313|EMBL:KER29789.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER29789.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER29789.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) 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; KL596672; KER29789.1; -; Genomic_DNA.
DR RefSeq; XP_009166502.1; XM_009168238.1.
DR AlphaFoldDB; A0A075AHF4; -.
DR STRING; 6198.A0A075AHF4; -.
DR GeneID; 20317883; -.
DR KEGG; ovi:T265_03696; -.
DR CTD; 20317883; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000054324; 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 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 Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
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:UP000054324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 841..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 685
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 884 AA; 102041 MW; F3A94A05ADDDE7E2 CRC64;
MGEQGSRFES FMRRTNRGIS ISSVQISDKT SNIKEDLNRH LHTTLSKDFY VANIKDYYLA
LAHTVWERLS TRWLRTHQQQ YLSDPKRVYY LSLEFYMGRS LANAMMNLGI SDSVTQALYD
FGLSLEELEE YESDAGLGNG GLGRLAACFL DSMVNLNLAA TGYGIRYDYG VFEQRIVNGW
QVEEPDDWLR YGNPWEIARL ELSQSVNFYG HVEIDSFGRR HWVDCQTLHA VPYDTPVPGY
LTNTCNSLRL WAARAPRNFD FSIFNTGDYI NAVCDRNVAE NVSRVLYPND NCFEGKELRL
KQEYMLVSAT LQDILRRFQL IDDNGPQRMD YNRLPDKVAI QLNDTHPSLA IPELMRILVD
IAGLDWYKSW DIVVRIFAYT NHTILPEALE RWPVEMMKKL LPRHMEIIYK VNYDFLEMVS
KRYPKDLERL RRMSIIEEEP VKAVNTALLC VIGSHAINGV SAIHSDIIRN ETFKDFAELW
PHKFQNKTNG ITPRRWLMLC NRKLADLISS KLDEDWITEL SKLAQLKGQA DSKDFLEKAM
QVKMFNKRRL ATHIKEEYGI EVDVNSIFDV QVKRIHEYKR QLLNCLHIIT MYNTLRNHPG
ADIHPRTIMI GGKAAPGYYM AKLIIKLINN VAKVVNSNPI VSKKLKVIFL ENYRVSLAEI
VIPAADLSQQ ISTAGTEASG TGNMKFMLNG AITIGTMDGA NVEMCEEVGQ ENMFIFGLRV
NEVNKLRKSG YYPQNYIYKI PELKEALEQI RDGHFSPDQP NLFKDIYNSI AFDDRYLLCA
DFEDYMRAQR EVNAVYRDKM RWAKMSVLNI MSSGKFSSDR AIAEYAYDIW GVKPERHIAL
PPSIPRTSEH MPPGHKRTSM RRKSLGAEPS GRPTTESFFE YNYD
//
