ID H6C1T2_EXODN Unreviewed; 896 AA.
AC H6C1T2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HMPREF1120_05835 {ECO:0000313|EMBL:EHY57811.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57811.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY57811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57811.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-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; JH226134; EHY57811.1; -; Genomic_DNA.
DR RefSeq; XP_009158272.1; XM_009160024.1.
DR AlphaFoldDB; H6C1T2; -.
DR STRING; 858893.H6C1T2; -.
DR GeneID; 20310474; -.
DR VEuPathDB; FungiDB:HMPREF1120_05835; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; H6C1T2; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000007304; 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:UP000007304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 733
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 896 AA; 101798 MW; BF1FE2D2AB900987 CRC64;
MSAGTPTSAP RERKLSTGAP ISTLQGPVGP GFSRPKHKRT ATGFAAQDIK AVESSIPEHM
REAWRKHSPQ GFKTKDEFEA ECVRHVETTL ARSLYNCDEL AAYSGTALAF RDRLIIDWNK
TQQRQTFADQ KRIYYLSLEF LMGRTLDNAM LNVGLKNVAK EGLEELGFRI EDVINQEHDA
ALGNGGLGRL AACFLDSLAS LNYPAWGYGL RYRYGIFKQE IENGYQVEIP DYWLDFNPWE
FARHDVTVDV QFYGWVNKYT NDEGKQVVAW QDGEIVKAVA YDVPIPGYGT STVNNLRLWS
SKASSGEFDF SKFNSGDYES AVADQQRAET ISAVLYPNDN LERGKELRLK QQYFWCAASL
HDIVRRFKKT QRKWSEFPDQ VAIQLNDTHP TLAIVELQRI LVDKEGLEWD VAWDIVTKTF
GYTNHTVLPE ALEKWSVPLL QNLLPRHLSI IYDINLFFLQ SVERRFPKDR ELLARVSIIE
ESQPKMVRMA YLAIVGSHKV NGVAELHSDL IKTTIFKDFV KIYGPDKFTN VTNGITPRRW
LHQANPRLSE LIASKLGSYE FLKDLTLLNK LEPFVDDKDF KKEWAEIKYA NKVRLAQHIL
KTTGVSVNPK SLFDVQVKRI HEYKRQQLNI FGVIHRYLAI KAMTAEERKK LLPRVSIFGG
KAAPGYWMAK TIIHLINKVG EVVNNDPEVG DLLKVIFIED YNVSKAEIII PASDISEHIS
TAGTEASGTS NMKFVLNGGL IIGTLDGANI EITREIGEQN VFLFGNLAED VEDLRHNHFY
GNYQVDPELV KVFDCIKAGT FGDESAFGAL IGAIAEHGDY YLVSDDFHSY CQTQQLIDEA
YRNQDEWLSK SILSVARMGF FTSDRCINEY ADSIWNIEPL QVKDEAEVRA RTGLDN
//
