CAZyme Information: CKF44_06666-t42_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CKF44_06666-t42_1-p1
• CAZy Family: GT39
• CAZyme Description: starch phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
927	CP022327.1|CGC8	104418.50	5.5162

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansKN99	6967	N/A	0	6967

• Gene Location: location=CP022327.1:421034-425445(+)

Full Sequence      

MAELTKENLDKVPASPGSSHSSRTPSLHQPEMSRRSSLSAGHPHSFKQVDPTQIGVPIVT
PRKERPGHQRSLTGSYFPSQKGGIVDMPGEWPVGDEKTWREGKKAMTIDQENPQDVANTI
VRHVNTSLGRQVYNVDEVAAYQATALSVRDQLLDRWNQTAAYHTAKAPKRVYYLSIEWLV
GRSLDNAVLNLGMRNVYEEANRKLGFNFEDLLNEERDAGLGNGGLGRLAACYIDSMATLN
LPGWGYGLRYNYGIFKQLISNSGEQLEAPDPWLDRENPWEIARLDVTYPIRFYGRVDPIP
NTDRAVWSGGMECLAVAYDTPIPGYGTKNCANIRLWSAKPVQGFDLNSFNAGNYEASVAA
SSEVENITRVLYPNDNMYAGKKLRVMQQYLWVSASLQDMLRRFTKLDLPWTELPDYVCIQ
MNDTHPTLAIPELMRILIDEEKLDYNTAWKITQKVFAYTNHTVLPEALERWQLDLFEELL
PRHLQIIYRINFDFLGLVAKRWPGDMDRIRRMSIIEEGSPKYVRMAYLAIVSSFKINGVA
ELHSQLLQATIFRDFVEFKGRDAFTNVTNGITPRRWLLQCNPELAALITHTLGSDDWATN
LKLLKNLLPMADNADFRKAFTNIKMDNKCRLASLIEAELGITLNVNSVFMTQIKRLHEYK
RQTLNLFGVIYRYLRIKQASPEERKKITKHTAIFAGKAAPGYYVAKLVIRLINNVARVVN
DDPDVGDLLKVVFIPDYSVSIAEVLVPASDVSVQISTAGTEASGTSNMKLALNGALLLGT
VDGANVEIAEDAGEDQSFLFGHLAEQVDEVRYANTYQPTPLEQRSPELAQTFKAIEAGTF
GDGAIYAPLLKTVYEHDYYLVSNDFGSYLSAEKLMDECYDSDKTEWTRKSIITAFNMGDF
SSDRSVQDYADGIWSVEPCEVPEGFSI

Enzyme Prediction     

EC	2.4.1.1:158

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	202	917	2.2e-266	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
184948	PRK14986	0.0	143	918	44	812	glycogen phosphorylase; Provisional
223136	GlgP	0.0	110	918	3	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
237881	PRK14985	0.0	141	914	35	794	maltodextrin phosphorylase; Provisional
273967	P_ylase	0.0	120	916	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	117	916	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUB25813.1|GT35	0.0	1	927	1	927
AFR95951.2|GT35	0.0	1	927	1	927
AAW44124.1|GT35	0.0	1	927	1	928
UOH82088.1|GT35	0.0	11	927	529	1439
ADV22853.1|GT35	0.0	1	927	1	927

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YGP_A	6.55e-298	114	918	42	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]
4BQE_A	3.52e-256	102	922	39	874	Arabidopsis thaliana Cytosolic Alpha-1,4-glucan Phosphorylase (PHS2) [Arabidopsis thaliana],4BQE_B Arabidopsis thaliana Cytosolic Alpha-1,4-glucan Phosphorylase (PHS2) [Arabidopsis thaliana],4BQF_A Arabidopsis thaliana cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with acarbose [Arabidopsis thaliana],4BQF_B Arabidopsis thaliana cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with acarbose [Arabidopsis thaliana],4BQI_A ARABIDOPSIS THALIANA cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with maltotriose [Arabidopsis thaliana],4BQI_B ARABIDOPSIS THALIANA cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with maltotriose [Arabidopsis thaliana]
1AXR_A	3.90e-255	92	918	3	829	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]
3ZCQ_A	4.04e-255	92	918	4	830	Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution [Oryctolagus cuniculus],3ZCR_A Rabbit muscle glycogen phosphorylase b in complex with N-(4-tert- butyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2.07 A resolution [Oryctolagus cuniculus],3ZCT_A Rabbit muscle glycogen phosphorylase b in complex with N-(2-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.0 A resolution [Oryctolagus cuniculus],3ZCU_A Rabbit muscle glycogen phosphorylase b in complex with N-(pyridyl-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 2.05 A resolution [Oryctolagus cuniculus],3ZCV_A Rabbit muscle glycogen phosphorylase b in complex with N-(indol-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 1.8 A resolution [Oryctolagus cuniculus],4CTM_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTN_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTO_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4YI3_A Crystal structure of Gpb in complex with 4a [Oryctolagus cuniculus],4YI5_A Crystal structure of Gpb in complex with 4b [Oryctolagus cuniculus],4YUA_A Glycogen phosphorylase in complex with ellagic acid [Oryctolagus cuniculus],5JTT_A Crystal structure of GPb in complex with 8a [Oryctolagus cuniculus],5JTU_A Crystal structure of GPb in complex with 8b [Oryctolagus cuniculus],5LRD_A Crystal structure of Glycogen Phosphorylase b in complex with KS242 [Oryctolagus cuniculus],5MEM_A A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe. [Oryctolagus cuniculus],5O52_A Glycogen Phosphorylase b in complex with 33b [Oryctolagus cuniculus],5O54_A Glycogen Phosphorylase b in complex with 29a [Oryctolagus cuniculus],5O56_A Glycogen Phosphorylase b in complex with 29b [Oryctolagus cuniculus],5OWY_A Glycogen Phosphorylase in complex with KS252 [Oryctolagus cuniculus],5OWZ_A Glycogen Phosphorylase in complex with KS172 [Oryctolagus cuniculus],5OX1_A Glycogen Phosphorylase in complex with JLH270 [Oryctolagus cuniculus],5OX3_A Glycogen Phosphorylase in complex with SzB102v [Oryctolagus cuniculus],5OX4_A Glycogen Phosphorylase in complex with CK900 [Oryctolagus cuniculus],6F3J_A The crystal structure of Glycogen Phosphorylase in complex with 10a [Oryctolagus cuniculus],6F3L_A The crystal structure of Glycogen Phosphorylase in complex with 10b [Oryctolagus cuniculus],6F3R_A The crystal structure of Glycogen Phosphorylase in complex with 10c [Oryctolagus cuniculus],6F3S_A The crystal structure of Glycogen Phosphorylase in complex with 10d [Oryctolagus cuniculus],6F3U_A The crystal structure of Glycogen Phosphorylase in complex with 10h [Oryctolagus cuniculus],6QA6_A Glycogen Phosphorylase b in complex with 30 [Oryctolagus cuniculus],6QA7_A Glycogen Phosphorylase b in complex with 29 [Oryctolagus cuniculus],6QA8_A Glycogen Phosphorylase b in complex with 28 [Oryctolagus cuniculus],6R0H_A Glycogen Phosphorylase b in complex with 3 [Oryctolagus cuniculus],6R0I_A Glycogen Phosphorylase b in complex with 4 [Oryctolagus cuniculus],6S4H_A The crystal structure of glycogen phosphorylase in complex with 8 [Oryctolagus cuniculus],6S4K_A The crystal structure of glycogen phosphorylase in complex with 12 [Oryctolagus cuniculus],6S4O_A The crystal structure of glycogen phosphorylase in complex with 9 [Oryctolagus cuniculus],6S4P_A The crystal structure of glycogen phosphorylase in complex with 13 [Oryctolagus cuniculus],6S4R_A The crystal structure of glycogen phosphorylase in complex with 11 [Oryctolagus cuniculus],6S51_A The crystal structure of glycogen phosphorylase in complex with 10 [Oryctolagus cuniculus],6S52_A The crystal structure of glycogen phosphorylase in complex with 14 [Oryctolagus cuniculus],6YVE_AAA Chain AAA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
5OX0_A	4.04e-255	92	918	4	830	Glycogen Phosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q00766|PHS1_DICDI	2.41e-298	100	921	24	845	Glycogen phosphorylase 1 OS=Dictyostelium discoideum OX=44689 GN=glpV PE=1 SV=3
sp|P06738|PHSG_YEAST	1.30e-297	66	918	24	900	Glycogen phosphorylase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GPH1 PE=1 SV=4
sp|P34114|PHS2_DICDI	3.88e-280	111	922	109	913	Glycogen phosphorylase 2 OS=Dictyostelium discoideum OX=44689 GN=glpD PE=1 SV=2
sp|P32811|PHSH_SOLTU	5.08e-262	111	922	21	838	Alpha-glucan phosphorylase, H isozyme OS=Solanum tuberosum OX=4113 PE=1 SV=1
sp|O84250|PHSG_CHLTR	3.78e-258	112	916	9	809	Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000000

TMHMM  Annotations     

There is no transmembrane helices in CKF44_06666-t42_1-p1.