CAZyme Information: TREMEDRAFT_72306-t26_1-p1

Basic Information

• Species: Tremella mesenterica
• Lineage: Basidiomycota; Tremellomycetes; ; Tremellaceae; Tremella; Tremella mesenterica
• CAZyme ID: TREMEDRAFT_72306-t26_1-p1
• CAZy Family: GT69
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
937		105401.66	5.7937

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmesentericaDSM1558	8309	578456	1	8308

• Gene Location: location=JH711539:884929-890591(+)

Full Sequence      

MSLTQDNVAKLPSAPQVRRTPSGHSVHSGQSGSRTPSLHQPQSLSRRSSMSAGQRLNIGP
THNVNVGEIGVPVVTPRKERPSHQRSLTGSYFPSQPGVVSMEGEWPIGDEDTWKTALKAE
EMEPNDVQGVANRVVRHVNTTLARQAFNVDELAAYQATALSVRDQLLTRWNETTGHHTLR
APKRIYYLSIEWLIGRSLDNAVLNLGLRNTYEEATRKLGFNFEDLLDQERDAGLGNGGLG
RLAACYIDSMATLCLPGWGYGLRYNYGIFKQLISSSGEQLEAPDPWLDRENPWEIARLDV
SYPIRFFGNVETIPNTDRARWTGGMECMAVAYDTPIPGFATKNCANIRLWKATPISGFDL
NSFNAGNYEASVSASSSVENITRVLYPNDNMYQGKLLRLQQQYLWTSASLQDILRRYTKL
DLSWSKLPEYVCIQMNDTHPTIAIPELMRILIDEEELSYEQAWKITTKVFAYTNHTVLPE
ALEKWELSLFEQLLPRHLQIIYKINYDFLNQVAKRWPNDVDRLARMSIIQEGSPKYVRMA
NLAIVGSFKVNGVAELHSQLLQATIFRDFVEFKGRDFFTNVTNGITPRRWLLQCNPELAA
LVTHTLGSEEWLLNAKLLTNLLPMGDNAEFRSAFKAIKQSNKGRLADVLESELGIDINVN
SIFACQIKRLHEYKRQTITIFSMIYRYLKIKTATREEKKKMQPWTMIFAGKAAPGYYIAK
LVIRLIVNVGKVVNNDPDVGDLLRICFIPDYSVSIAEVLVPAADVSVQVSTAGTEASGTS
NMKLALNGALLLGTVDGANVEIAEDAGEDQCFMFGHLADQVAQVRFNNSYNALPLEQRSP
ELAEVFKMIESGTFGDGHIYEALLQTVYEHDYYLVSNDFGSYLEAQRLVDDLFKNDPEEW
TKKAILTAFAMGDFSSDRSVQDYADGIWSVEPCRVPE

Enzyme Prediction     

EC	2.4.1.1:158

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	215	931	1.6e-262	0.9970326409495549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223136	GlgP	0.0	131	932	10	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
237881	PRK14985	0.0	155	928	35	794	maltodextrin phosphorylase; Provisional
273967	P_ylase	0.0	134	930	1	794	glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
340853	GT35_Glycogen_Phosphorylase	0.0	131	930	1	795	glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
395272	Phosphorylase	0.0	216	930	2	661	Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAW44124.1|GT35	0.0	3	937	4	924
AUB25813.1|GT35	0.0	3	937	4	923
AFR95951.2|GT35	0.0	3	937	4	923
KGB76066.3|GT35	0.0	3	937	4	923
ADV22853.1|GT35	0.0	3	937	4	923

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YGP_A	1.28e-292	81	932	1	877	Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae],1YGP_B Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae]
1C8L_A	1.09e-254	106	934	3	831	Synergistic Inhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug And Caffeine [Oryctolagus cuniculus],1LWN_A Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution [Oryctolagus cuniculus],1LWO_A Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution [Oryctolagus cuniculus],2GPA_A Allosteric Inhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug [Oryctolagus cuniculus],3AMV_A Allosteric Inhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug [Oryctolagus cuniculus]
2GJ4_A	1.20e-254	136	934	22	820	Structure of rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	1.24e-254	136	934	22	820	Structure of rabbit muscle glycogen phosphorylase in complex with thienopyrrole [Oryctolagus cuniculus],5MCB_A Glycogen phosphorylase in complex with chlorogenic acid. [Oryctolagus cuniculus],7ONF_A Chain A, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1AXR_A	1.54e-254	106	934	3	831	Cooperativity Between Hydrogen-Bonding And Charge-Dipole Interactions In The Inhibition Of Beta-Glycosidases By Azolopyridines: Evidence From A Study With Glycogen Phosphorylase B [Oryctolagus cuniculus],1E1Y_A Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site [Oryctolagus cuniculus],1GPY_A CRYSTALLOGRAPHIC BINDING STUDIES ON THE ALLOSTERIC INHIBITOR GLUCOSE-6-PHOSPHATE TO T STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],1PYG_A Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_B Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_C Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_D Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1UZU_A Glycogen Phosphorylase b in complex with indirubin-5'-sulphonate [Oryctolagus cuniculus],1XC7_A Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies [Oryctolagus cuniculus],1XKX_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL0_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL1_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1Z62_A Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor and the allosteric site. Broad specificities of the two sites [Oryctolagus cuniculus],2AMV_A The Structure Of Glycogen Phosphorylase B With An Alkyl- Dihydropyridine-Dicarboxylic Acid [Oryctolagus cuniculus],2F3P_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)oxamic acid complex [Oryctolagus cuniculus],2F3Q_A Crystal structure of the glycogen phosphorylase B / methyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3S_A Crystal Structure of the glycogen phosphorylase B / ethyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3U_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)-N'-cyclopropyl oxalamide complex [Oryctolagus cuniculus],2FET_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],2FF5_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],3BD7_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) thymine [Oryctolagus cuniculus],3BD8_A Glucogen Phosphorylase complex with 1(-D-glucopyranosyl) cytosine [Oryctolagus cuniculus],3BDA_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) cyanuric acid [Oryctolagus cuniculus],5LRC_A Crystal structure of Glycogen Phosphorylase in complex with KS114 [Oryctolagus cuniculus],5LRE_A Crystal structure of Glycogen Phosphorylase b in complex with KS382 [Oryctolagus cuniculus],5LRF_A Crystal structure of Glycogen Phosphorylase b in complex with KS389 [Oryctolagus cuniculus],5O50_A Glycogen Phosphorylase b in complex with 33a [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06738|PHSG_YEAST	1.79e-292	81	932	24	900	Glycogen phosphorylase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GPH1 PE=1 SV=4
sp|Q00766|PHS1_DICDI	6.15e-291	116	935	31	845	Glycogen phosphorylase 1 OS=Dictyostelium discoideum OX=44689 GN=glpV PE=1 SV=3
sp|P34114|PHS2_DICDI	1.92e-269	124	936	108	913	Glycogen phosphorylase 2 OS=Dictyostelium discoideum OX=44689 GN=glpD PE=1 SV=2
sp|P32811|PHSH_SOLTU	8.87e-263	126	936	22	838	Alpha-glucan phosphorylase, H isozyme OS=Solanum tuberosum OX=4113 PE=1 SV=1
sp|P79334|PYGM_BOVIN	1.54e-256	136	934	34	832	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000000

TMHMM  Annotations     

There is no transmembrane helices in TREMEDRAFT_72306-t26_1-p1.