CAZyme Information: EDK44753.1

Basic Information

• Species: Lodderomyces elongisporus
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
• CAZyme ID: EDK44753.1
• CAZy Family: GT15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
535	CH981526|CGC7	59164.57	6.3934

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=CH981526:1685459-1687066(+)

Full Sequence      

MTWKKVTLTLSRPLVAGLTGAVIASTIAYKVGQQRTIHNPPQNAFPKTSTTKLTDLSSPQ
YCTNISKVIPEFTKLGIEVVNSKPEIEHHTGNDFTTHKPLPGQVPQYIIYPKTTEEVSQV
LQICNRELIPVVPFSGGTSLEGHFHSTRLGVVLDTSKMNKILAVHDDDLDVVVQAGVNWQ
HLNQELEPYGLMFGTDCGPQGQISGMIATNASGINASRYGAMSANVISVTAVLADGTIVK
TKQRPRKSSAGYNLTNLFIGSEGTLGVVTEAVCKVYPKPKSETVVVVQYPTILDATKSVA
QVFRSGMQPTAIELLDNDMMHCLNYSGYTTRPWLEVPTIFFKIGGINDAVVEENVKVLNK
ITKANNAESFTYAQSKEEQEELFSARKNAFYAMYNWGKNEIDEDVRIWVTDIAVPLSRLS
PVLDKVHEMIKASPFKSIILAHAGDGNFHADIFYQHEQRREVEKLVDLMIELGLANEGTA
TGEHGIGNAKRNFLELELGQDTIDMMRKIKLSLDPNRILNPDKVFKIDPEDKGEY

Enzyme Prediction     

No EC number prediction in EDK44753.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	98	304	1.3e-23	0.425764192139738

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
178402	PLN02805	1.93e-119	92	524	125	548	D-lactate dehydrogenase [cytochrome]
223354	GlcD	2.63e-106	75	525	6	456	FAD/FMN-containing dehydrogenase [Energy production and conversion].
397178	FAD-oxidase_C	8.03e-55	278	524	1	248	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
183043	PRK11230	1.30e-51	104	523	55	470	glycolate oxidase subunit GlcD; Provisional
396238	FAD_binding_4	2.43e-39	105	241	1	138	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSZ31245.1|GT31	1.26e-79	104	481	547	905
BCS28313.1|AA4	1.85e-08	26	241	44	254
UPK94077.1|AA4	5.45e-08	103	312	83	304
QGA13141.1|AA4	1.25e-07	103	312	84	305
QGA20504.1|AA4	2.25e-07	104	353	107	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LPN_A	4.84e-41	108	523	57	469	Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPN_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens]
3PM9_A	4.86e-35	92	524	46	475	Chain A, Putative oxidoreductase [Rhodopseudomonas palustris],3PM9_B Chain B, Putative oxidoreductase [Rhodopseudomonas palustris],3PM9_C Chain C, Putative oxidoreductase [Rhodopseudomonas palustris],3PM9_D Chain D, Putative oxidoreductase [Rhodopseudomonas palustris],3PM9_E Chain E, Putative oxidoreductase [Rhodopseudomonas palustris],3PM9_F Chain F, Putative oxidoreductase [Rhodopseudomonas palustris]
4BBY_A	7.42e-25	103	340	204	440	Mammalian Alkyldihydroxyacetonephosphate Synthase: Wild-Type [Cavia porcellus],4BBY_B Mammalian Alkyldihydroxyacetonephosphate Synthase: Wild-Type [Cavia porcellus],4BBY_C Mammalian Alkyldihydroxyacetonephosphate Synthase: Wild-Type [Cavia porcellus],4BBY_D Mammalian Alkyldihydroxyacetonephosphate Synthase: Wild-Type [Cavia porcellus],4BC9_A MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: WILD-TYPE, ADDUCT WITH CYANOETHYL [Cavia porcellus],4BC9_B MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: WILD-TYPE, ADDUCT WITH CYANOETHYL [Cavia porcellus],4BC9_C MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: WILD-TYPE, ADDUCT WITH CYANOETHYL [Cavia porcellus],4BC9_D MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: WILD-TYPE, ADDUCT WITH CYANOETHYL [Cavia porcellus],5ADZ_A Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1a [Cavia porcellus],5ADZ_B Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1a [Cavia porcellus],5ADZ_C Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1a [Cavia porcellus],5ADZ_D Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1a [Cavia porcellus],5AE1_A Ether Lipid-Generating Enzyme AGPS in complex with inhibitor ZINC69435460 [Cavia porcellus],5AE1_B Ether Lipid-Generating Enzyme AGPS in complex with inhibitor ZINC69435460 [Cavia porcellus],5AE1_C Ether Lipid-Generating Enzyme AGPS in complex with inhibitor ZINC69435460 [Cavia porcellus],5AE1_D Ether Lipid-Generating Enzyme AGPS in complex with inhibitor ZINC69435460 [Cavia porcellus],5AE2_A Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1e [Cavia porcellus],5AE2_B Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1e [Cavia porcellus],5AE2_C Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1e [Cavia porcellus],5AE2_D Ether Lipid-Generating Enzyme AGPS in complex with inhibitor 1e [Cavia porcellus],5AE3_A Ether Lipid-Generating Enzyme AGPS in complex with antimycin A [Cavia porcellus],5AE3_B Ether Lipid-Generating Enzyme AGPS in complex with antimycin A [Cavia porcellus],5AE3_C Ether Lipid-Generating Enzyme AGPS in complex with antimycin A [Cavia porcellus],5AE3_D Ether Lipid-Generating Enzyme AGPS in complex with antimycin A [Cavia porcellus],6GOU_A Development of Alkyl Glycerone Phosphate Synthase Inhibitors: Complex with Inhibitor 2I [Cavia porcellus],6GOU_B Development of Alkyl Glycerone Phosphate Synthase Inhibitors: Complex with Inhibitor 2I [Cavia porcellus],6GOU_C Development of Alkyl Glycerone Phosphate Synthase Inhibitors: Complex with Inhibitor 2I [Cavia porcellus],6GOU_D Development of Alkyl Glycerone Phosphate Synthase Inhibitors: Complex with Inhibitor 2I [Cavia porcellus]
4BC7_A	7.42e-25	103	340	204	440	MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Arg419His mutant [Cavia porcellus],4BC7_B MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Arg419His mutant [Cavia porcellus],4BC7_C MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Arg419His mutant [Cavia porcellus],4BC7_D MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Arg419His mutant [Cavia porcellus]
4BCA_A	7.42e-25	103	340	204	440	MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant [Cavia porcellus],4BCA_B MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant [Cavia porcellus],4BCA_C MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant [Cavia porcellus],4BCA_D MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant [Cavia porcellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12627|DLD1_KLULA	2.27e-153	11	531	47	573	D-lactate dehydrogenase [cytochrome], mitochondrial OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=DLD1 PE=3 SV=2
sp|P32891|DLD1_YEAST	1.20e-147	46	531	85	581	D-lactate dehydrogenase [cytochrome] 1, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DLD1 PE=1 SV=2
sp|Q94AX4|DLD_ARATH	4.71e-105	104	524	145	560	D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1
sp|F1QXM5|LDHD_DANRE	5.78e-93	65	527	32	490	Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
sp|Q7TNG8|LDHD_MOUSE	3.79e-86	75	524	39	483	Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.973191	0.026826

TMHMM  Annotations     

There is no transmembrane helices in EDK44753.1.