CAZyme Information: EDK47365.1

Basic Information

• Species: Lodderomyces elongisporus
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
• CAZyme ID: EDK47365.1
• CAZy Family: GT91
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
598		68750.82	6.8296

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LelongisporusNRRLYB-4239	5908	379508	109	5799

• Gene Location: location=CH981533:294009-295805(+)

Full Sequence      

MSKDYLTPSTLPQPKLKRTNTGFTPNQIIALDAAIPESAKHIWFKYSQLDLLEKKSRGAN
HEPNIHNIVDNPQKFEEEFVRHVETNLGRSMYNCDDLAAYQAAAKTVRDALIIDWANTQQ
RQTIQDGKRVYYLSLEFLMGRAMDNALINLKCEKNTRNSLNELGFNLEDVLNQEPDAALG
NGGLGRLAACFVDSLSSKNYSGWGYGLNYQYGIFKQKIIDGYQIETPDYWLKYTNPWVLD
RHEIQIPVDFYGYVYEESDPNTGKISKNWSGGERVLAVAADFPIPGYNTNNTNNLRLWNA
KPTNEFDFTKFNAGDYQLSVASQQKAESITAVLYPNDNFEEGKELRLKQQYFWVAASLHD
IVRRFKKNHHLNWQKFPEQIAIQLNDTHPTLAIVELQRILVDLEGLDWDEAWSIVTKVFA
YTNHTVMVEALEKWPVGLVGRLLPRHLEIIYDINYFFLKQVEKNFPDQRDLQSKVSIIEE
GNPKSVRMAYLAIVGSHKVNGVAELHSELIKTTIFKDFVKVFGPDKFTNVTNGITPRRWL
RQANPKLAALIAKKLNDPNYEYLTNLGRLKDLERFIDDEKSSRNGTLSNLTISADWRY

Enzyme Prediction     

EC	2.4.1.1:158

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	160	579	6.2e-161	0.56973293768546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
273967	P_ylase	0.0	79	579	1	494	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	77	580	2	496	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	160	580	1	363	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.
184948	PRK14986	2.37e-176	102	577	44	508	glycogen phosphorylase; Provisional
223136	GlgP	3.64e-173	71	580	5	455	Glucan phosphorylase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG25253.1|GT35	0.0	1	583	1	584
CCE41151.1|GT35	0.0	1	583	1	584
CAX40640.1|GT35	0.0	1	578	1	578
AOW30468.1|GT35	0.0	1	578	1	578
BAE44621.1|GT35	0.0	4	578	2	576

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YGP_A	3.16e-264	14	580	1	562	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]
2GJ4_A	3.02e-169	69	584	10	522	Structure of rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
4EJ2_A	3.10e-169	69	584	10	522	Crystal structure of GPb in complex with DK10 [Oryctolagus cuniculus],4EKE_A Crystal structure of GPb in complex with DK11 [Oryctolagus cuniculus],4EKY_A Crystal structure of GPb in complex with DK15 [Oryctolagus cuniculus],4EL0_A Crystal structure of GPb in complex with DK16 [Oryctolagus cuniculus],4EL5_A Crystal structure of GPb in complex with DK12 [Oryctolagus cuniculus],4MHO_A Crystal structure of Gpb in complex with S3, SUGAR (N-[(BIPHENYL-4-YLOXY)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MHS_A Crystal structure of Gpb in complex with SUGAR (N-[(2E)-3-(BIPHENYL-4-YL)PROP-2-ENOYL]-BETA-D-GLUCOPYRANOSYLAMINE [Oryctolagus cuniculus],4MI3_A Crystal structure of Gpb in complex with SUGAR (N-{(2R)-2-METHYL-3-[4-(PROPAN-2-YL)PHENYL]PROPANOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S21) [Oryctolagus cuniculus],4MI6_A Crystal structure of Gpb in complex with SUGAR (N-[4-(5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MI9_A Crystal structure of Gpb in complex with SUGAR (N-[(3R)-3-(4-ETHYLPHENYL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) (S20) [Oryctolagus cuniculus],4MIC_A Crystal structure of Gpb in complex with SUGAR (N-{(2E)-3-[4-(PROPAN-2-YL)PHENYL]PROP-2-ENOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S6) [Oryctolagus cuniculus],4MRA_A Crystal structure of Gpb in complex with QUERCETIN [Oryctolagus cuniculus]
2GM9_A	3.10e-169	69	584	10	522	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]
2FFR_A	4.38e-169	69	584	10	522	Crystallographic studies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06738|PHSG_YEAST	1.63e-266	14	580	24	585	Glycogen phosphorylase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GPH1 PE=1 SV=4
sp|Q00766|PHS1_DICDI	8.53e-196	76	598	45	550	Glycogen phosphorylase 1 OS=Dictyostelium discoideum OX=44689 GN=glpV PE=1 SV=3
sp|P34114|PHS2_DICDI	1.00e-171	76	578	115	612	Glycogen phosphorylase 2 OS=Dictyostelium discoideum OX=44689 GN=glpD PE=1 SV=2
sp|P00489|PYGM_RABIT	2.69e-168	69	584	22	534	Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
sp|Q9WUB3|PYGM_MOUSE	5.20e-168	69	584	22	534	Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EDK47365.1.