ID A0A0L0GCF3_9EUKA Unreviewed; 834 AA.
AC A0A0L0GCF3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SARC_01297 {ECO:0000313|EMBL:KNC86574.1};
OS Sphaeroforma arctica JP610.
OC Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC86574.1, ECO:0000313|Proteomes:UP000054560};
RN [1] {ECO:0000313|EMBL:KNC86574.1, ECO:0000313|Proteomes:UP000054560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP610 {ECO:0000313|EMBL:KNC86574.1,
RC ECO:0000313|Proteomes:UP000054560};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Sphaeroforma arctica JP610.";
RL Submitted (FEB-2011) 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; KQ241646; KNC86574.1; -; Genomic_DNA.
DR RefSeq; XP_014160476.1; XM_014305001.1.
DR AlphaFoldDB; A0A0L0GCF3; -.
DR STRING; 667725.A0A0L0GCF3; -.
DR EnsemblProtists; KNC86574; KNC86574; SARC_01297.
DR GeneID; 25901801; -.
DR eggNOG; KOG2099; Eukaryota.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000054560; 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:0005975; P:carbohydrate 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 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:UP000054560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 682
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 834 AA; 95890 MW; 88FADDF130E58C69 CRC64;
MAENKVQQAR GMVRRPSLRK GISLRGMPEL ENVEEVKASF NRHLHFTVGK DRNVATNIDF
MQAISMAVRD QLIGKWMRTQ QNYHETDPKR VYYLSLEWYM GRTLGNAMLN LGIQGSTEEA
LNQLGLAIDE LEEYEEDAGL GNGGLGRLAA CFIDSMSTVG LPAHGYGIRY EYGIFKQEFV
DGWQRELPDN WLRYGNPWEI QRPESTQNIR MYGHVSNGKW VDTKQVLAVP YDTPVPGYKN
DVVNTLRLWS ASAPVEFQLD SFNRGDYMGA VIENNVAEDI SRVLYPNDNF FEGKELRLKQ
QYFLVAASLA DIIRRHKTEP SWKERGWACF PDKAAIQLND THPSLAVPEL MRILIDEEGK
DWDESWKITT STLSYTNHTV LPEALERWPV SLFEKLLPRH LQLVYEINHR HMEAVKAKYP
GDNDRLSRMS IIEEGGGKRI HMGYLAIVGT HAVNGVAALH SELIKKTIFK DFYEMYPERF
QNKTNGITPR RWLIKANPAL TNLIDEKLPG EKWATDLYEL AKLKKFADDK DFMRSIQNAK
RENKLSVCRL VAEEYGIELD VDSMFDCHVK RIHEYKRQLL NVLHMITRYN EIKANPDKEF
TPRTVMFGGK CAPGYEMAKR IIKLINNVAD KCNNDPAVSK YLKVVYFENY RVSLAEKIIP
AVDLSEQIST AGTEASGTGN MKFMLNGSLT IGTMDGANVE MAEEMGLENI FIFGMDVDEV
HALGAKGYNP HEFYDNNATL RECLDQIRDG FWSPEDPSMF SMIWDTLMTR GDQYMLLADY
QSYIDKQREV DEVYRDQKKW LKMAIHNIAS IGKFNSDRTI REYAEEIWGA QCRN
//
