ID A5DAT5_PICGU Unreviewed; 871 AA.
AC A5DAT5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PGUG_00390 {ECO:0000313|EMBL:EDK36292.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36292.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK36292.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408155; EDK36292.2; -; Genomic_DNA.
DR RefSeq; XP_001487013.1; XM_001486963.1.
DR AlphaFoldDB; A5DAT5; -.
DR STRING; 294746.A5DAT5; -.
DR GeneID; 5129181; -.
DR KEGG; pgu:PGUG_00390; -.
DR VEuPathDB; FungiDB:PGUG_00390; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; A5DAT5; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000001997; 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:UP000001997};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 736
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 871 AA; 99360 MW; FB7BB180EF99185E CRC64;
MGDYLTPAEL PHPKLKRTNT GFTPNQIIAL DAAIPEAAKK TWNKYSLLKP LGGRNHNEEE
PGVFNAEEKF EEYFVRHVET TLARNMYNCD TLAAYQATSN TIRDGLLVDW ANTQQKQTIH
DGKRVYYLSL EFLMGRALDN ALINLNARNN TTTSLEHLGF NLEDVLDQEP DAALGNGGLG
RLAACFVDSL SSRNYSGWGY GLNYQYGIFK QKIIDGYQVE TPDYWLKYSN PWEIDRNEIQ
IPVDFYGYVY ENYDTNTGEA KKVWAGGERV LAVAADFPIP GYNTSTTNNL RLWNARPTTE
FDFGKFNAGD YQQSVAAQQR AESITSVLYP NDNFESGKEL RLKQQYFWVA ASLHDIIRRF
KKTHKSNWDK FADQVAIQLN DTHPTLAIVE LQRVFVDVEG LDWDKAWSIV RKVFAYTNHT
VMTEALEKWP VTVLSRLLPR HMEIIYDINF FFLKDVERKF PHERDILSRV SVIEESEPKQ
VRMAYLAIIG SHKVNGVAEL HSELIKTTIF KDFVRVFGPD KFTNVTNGIT PRRWLRQANP
KLAALIAEAL NDPNYEYLTN LGMLKKLEPL VDDDTFLKKW DAIKFDNKRR LAGLIKSETG
IEVDPSVMFD VQVKRIHEYK RQQLNIFAVI YRYLHIKKLI REGKSVDDIK KNYYIPKCSI
FGGKAAPGYY MAKTIIHLIN EVASVVNHDT EIENLLKVVF IPDYNVSKAE VITPASDLSN
HISTAGTEAS GTSNMKFALN GGLIIGTVDG ANVEITREIG EENIFLFGNL AESVDELRHK
HVYEGVKVPE SLQEVFSAIE SGLFGNADEF KSLVESIKYH GDYYLVTDDF DLFLEAHRKL
EKVYGHDGSG HLHNWVKKSL LNVAQYGLFQ F
//
