ID A0A0D2WXP7_CAPO3 Unreviewed; 829 AA.
AC A0A0D2WXP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CAOG_007395 {ECO:0000313|EMBL:KJE97558.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE97558.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE346374; KJE97558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2WXP7; -.
DR STRING; 595528.A0A0D2WXP7; -.
DR EnsemblProtists; KJE97558; KJE97558; CAOG_007395.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; A0A0D2WXP7; -.
DR PhylomeDB; A0A0D2WXP7; -.
DR Proteomes; UP000008743; 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; 3.
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; 2.
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:UP000008743};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 674
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 829 AA; 94570 MW; F8292D44AF518A01 CRC64;
MATTPTKTEA PPLRPTLGSK QISLRGIPKL ENVDEIKATF IRHVHADLAK DRNVATTNDY
YLALAHTVRD HVVSKWIRTQ QTYYNTDPKR VYYLSLEYYM GRSLCNTMVN LGIATESEEA
MYQLGLNIEE MEESEEDAGL GNGGLGRLAA CFLDSMATLN LPAYGYGIRY EYGIFKQQIR
DGYQVELPDS WLKRGNPWEI ARPEYMLPVQ FYGRSELGPD GKHKWVGTQT VMALPYDSPI
PGYKTNTVNT MRLWSARSPN DFDLSYFNHG DYIKAVIDRN LAENISRVLY PNDNFFEGKE
LRLKQEYFMV SATLQDIVRR YKAATFGSRE LSRKSFDLFP EKVAIQLNDT HPSLAIPELM
RILVDLEGCT WEYAWKICTA TFGYTNHTVL PEALERWHGV ALRFPGDHDR LRRMSLIEED
GDKRVNMANL SIVNMANLSI VGSHAINGVA RIHTEIIKNS IFRDFFEFTP EKFQNKTNGI
TPRRWLLVSN AALADLITER IGEKWSLDLR HLHKLEQYAD DPDLQRAFFD VKQSNKQRLA
TLIKEQYKIE INVDSIFDCH VKRIHEYKRQ LLNALHIITL YNRIKENPSG DFVPRTVFIG
GKAAPGYYMA KMIIKLICSI AEVVNNDPIV GNRLKVVFLE NYRVSLAERV IPATDLSEQI
STAGTEASGT GNMKFMLNGA LTIGTMDGAN VEMSEEVGAE NMFIFGLNVD EVEALAKAGY
DPNKYYHANR ELKHALDQIG NGYFSATNRD LFVHVVDSLL KHGDRYMLLA DYASYVETQD
RVAVEFRNRK LWMRKCILNV AASGKFSSDR TIQEYAADIW KAEPVNVVL
//
