ID G4UI92_NEUT9 Unreviewed; 887 AA.
AC G4UI92;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=NEUTE2DRAFT_109031 {ECO:0000313|EMBL:EGZ73925.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73925.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73925.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891217; EGZ73925.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UI92; -.
DR STRING; 510952.G4UI92; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OMA; WLKQANP; -.
DR Proteomes; UP000008513; 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:UP000008513};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 735
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 887 AA; 100768 MW; 1F88729B26A2273A CRC64;
MASNTTQRVP LRERRPSVGA PLVDIQGGVA PAGVSRPKHK RTLTGFGPGE IKNVEASIPE
PQRKAWLAHQ TSGFKDKDGF ETEVVRHVET TLARSMYNCD EQAAYSACSL AFRDRLILEW
NRTQQRQTFA DSKRVYYLSL EFLMGRALDN AMLNIGQKDV AKAGLAELGF RIEDVIEQEH
DAALGNGGLG RLAACFLDSL ASLNYSAWGY GLRYRYGIFK QEIIDGYQVE VPDYWLDFNP
WEFPRHDVTV DIQFYGHVTK RTDDNGKTIA TWEGGEIVKA VAYDVPIPGY ATPSTNNLRL
WSSKAASGEF DFQKFNSGDY ENSVADQQRA ETISAVLYPN DNLDRGKELR LKQQYFWVAA
SLYDIVRRFK KSRRAWKEFP DQVAIQLNDT HPTLAVVELQ RILVDLEGLD WEEAWNIVTN
TFGYTNHTVL PEALEKWSVP LFQHLLPRHL QLIYDINLFF LQSVERKFPK DREMLARVSI
IEESQPKMVR MAHLAIVGSH KVNGVAELHS DLIKTTIFKD FVEVFGPDKF TNVTNGITPR
RWLHQANPRL SELISSKTGS QNFLKDLTEL AKIEHYKDDK AFRKEWAEIK YANKVRLAKH
IKKTTGVDVN PSALFDVQVK RIHEYKRQQM NIFGVIHRYL TLKSLSPEER KKFQPRVSIF
GGKAAPGYWM AKQIIHLINA VGAVVNNDKD IGDLLKVIFL EDYNVSKAEM IIPASDLSEH
ISTAGTEASG TSNMKFVLNG GLIIGTCDGA NIEITREIGE QNIFLFGNLA EDVEDIRHNH
TYGSYTVDPD LVKVFEAIEK GTFGEPNDFM GMISAVRDHG DFYLVSDDFH SYIETQELVD
KAYRDQEGWI TKSIESVARM GFFSSDRCIN EYAEGIWNIE PLAVKDQ
//
