ID A0A1E4TXJ2_PACTA Unreviewed; 870 AA.
AC A0A1E4TXJ2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PACTADRAFT_67995 {ECO:0000313|EMBL:ODV96470.1};
OS Pachysolen tannophilus NRRL Y-2460.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV96470.1, ECO:0000313|Proteomes:UP000094236};
RN [1] {ECO:0000313|Proteomes:UP000094236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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; KV454013; ODV96470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TXJ2; -.
DR STRING; 669874.A0A1E4TXJ2; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000094236; 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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000094236};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 717
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 870 AA; 99459 MW; CC2D3EB7BB4164FD CRC64;
MSDLVPQSPE SLPRPRLHKR TLTGFTSTEI KVIDSIIPSE SRELWKKFGS KEFNTVEEFQ
ASFISHVEKT LARSMYNCDN LAAYQAASSA VRDKLILHWN KTQQLHTAKD IKRVYYFSFE
FLMGRAMDNA LINLDIKDLT KEGVNKLGFN LEDLLEIEPD AGLGNGGLGR LAACFVDSLS
TQNYAGWGYG VRYQYGIFAQ KIIDGYQVET PDYWLRFSNP WELPRLEIQI PVDYYGFTQT
VKDLKTGKSK KQWFGSERVL AVAYDFPVPG YDTANVNNLR MWSAQPTTEF DFNKFNQGDY
QNSVAEQQKA ESITAVLYPN DNFYQGKELR LKQQYFWVAA SLHDIIRRFI KTKRNWSEFP
DQVAIQLNDT HPTVAVVELQ RVLVDIEGLD WDTAWQIVIK TFSYTNHTVM QEALEKWPLD
LFGNLLPRHL EIIYDINLKF LQQVEKKFPG DNDLLSKVSI IEESSPKNIR MANLAIIGSH
RVNGVAELHS ELLRTTLFKD FVKVFGVEKF TNVTNGITPR RWLREANPEL SELIASKLGG
FGYLTNLTEL KKLESFINDS SFKKRWAEIK VNNKKRLSLL VKNLTGIDIN PDSLFDIQVK
RIHEYKRQQL NIFGVIHRYL QLKKCKNNEE RVKLYTPKVS IIGGKAAPGY YMAKTIIKLI
NSVGDVINKD PDIGDLLKVV FVPDYNVSKA QIITSASDVS EHISTAGTEG SGTSNMKFVL
NGGLIIGTVD GANVEITREI GEENIFLFGN LAENVEQLRH NHKFNSLENN IVPSSLQEVF
DAIESNTFGD SSEYKSLIDS IKIHGDYYLV TDDFDSYLQT QKLVDDEFRN HRDEWIVKCI
SSVANMGFFS SDRCIQEYAE NIWNVEPVQE
//
