ID V5I1H6_BYSSN Unreviewed; 885 AA.
AC V5I1H6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PVAR5_5208 {ECO:0000313|EMBL:GAD96550.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD96550.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD96550.1}.
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; BAUL01000168; GAD96550.1; -; Genomic_DNA.
DR AlphaFoldDB; V5I1H6; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_2_1_1; -.
DR InParanoid; V5I1H6; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000018001; 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:UP000018001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..44
FT /note="Disordered"
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 885 AA; 100308 MW; 331A02C85045FA4E CRC64;
MSSTTTSSHA HERRPSVGAP ISELQGPVGP GFSRPKHKRT FTGFGPSEIR SVEASIPEPL
REAWKKYSPQ GFTNKDDFEK ELVRHVETTL ARSLFNCDEL AAYSGTALAF RDRLIIEWNK
TQQRQTFTDK KRVYYLSLEF LMGRALDNAM LNVGLKDVAK DGLGELGFRI EDVISQEHDA
ALGNGGLGRL AACLLDSMAT LNYPAWGYGL RYRYGIFKQE IVNGYQVEVP DYWLDFNPWE
FPRHDITVDV QFYGSVRRYQ DDDGKFINEW DGGEIVQAVA YDVPIPGYGT STTNNLRLWS
SKASSGEFDF QKFNSGEYES AVADQQRAET ISAVLYPNDN LDRGKELRLK QQYFWCAASL
YDIVRRFKKT KRAWSEFPEQ VAIQLNDTHP TLAIVELQRL LVDVEGLDWD QAWHIVVNTF
GYTNHTVLPE AHEKWSVPLF QNLLPRHLQI IYDINLFFLQ SVEKKFSTDR ELLARVSVIE
ESHPKMVRMA HLAIIGSHKV NGVAELHSDL IKTTVFKDFV EIYGPDKFTN VTNGITPRRW
LHQANPRLSD LIATKLGGYD FLKDLTLLDK LEAHADDKAF KRDWAAVKYA NKVRLAKHIK
DTTGYSVNPS SLFDIQVKRI HEYKRQQLNI FGVIHRYLTI KSMTPEQRKK LVPRVSIFGG
KAAPGYWMAK TVIHLINNVA SVVNKDPDVG DLLKVIFVED YNVSKAELIV PASDISEHIS
TAGTEASGTS NMKFVLNGGL IIGTCDGANI EITREIGEQN IFLFGNLAED VEELRHKHFY
AGDFKLDPDL VKVFDAIRSG TFGNVDDFSA LLSSIAEHGD YYLVSDDFNS YITAQGIVDE
AFKDQDEWIT KSITSVARMG FFTSDRVINE YADSIWNVEP LDVTD
//
