CAZyme Information: I302_06222-t42_1-p1

Basic Information

• Species: Kwoniella bestiolae
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella bestiolae
• CAZyme ID: I302_06222-t42_1-p1
• CAZy Family: GH5
• CAZyme Description: phosphatidylinositol glycan, class A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
728		80561.38	9.1614

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KbestiolaeCBS10118	9270	1296100	137	9133

• Gene Location: location=KI894022:1839474-1842619(-)

Full Sequence      

MANITFQLRQALYTILLLLVSLFALVIGLVCTLTGQRLNTNYYVARTFYHVAGPILGWKF
EVEGEEYLWKLDGEGGGQAGKKGRRMVMVGNHQSMVDILYLGRIFPKRAAIMAKKSIKWI
PGLGWWMMMSGTVFINRSNNKSAVASMTQAGDDMKRKGISLWIFPEGTRHMSAESDLLPF
KKGAFYLAVQSGVPVVPVVCENYHRLFDGKTRFKRGTLKIKVLPPIPTTGLTASDVPALM
EKTREMMLETLKSISSPSPSASTSISELNSPAPLLAHQEDSRSSYFATHAADEQAVENAV
GEEEADSGKSIKSVKTKETSKVSVRDEEDNGSTKSGKKKDKKKLSIAMISDFFLPVVGGV
EGHIYSLSVEMMKRGHKVIVITHSHPRRVGIRHLSPGLKIYYLPILPIASSATLPNYLLF
LPYFRSIMIAERITLIHGHGSLSSLAHEALFHKDLFDPPIKGVFTDHSLFGFGDAVGVLT
NKLLVGALRCADGVVCVSNTGRENTVLRAQLDPELVSVIPNALIPEDFTPDPSKADPNYI
TIVVISRLFYRKGIDLLIASCPHICALFPEVRFVVGGDGPKMVELEQMREKYQLQDRVEL
LGRVRPGDVRDVLNRGQIYLNNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPEDMIE
FARADEEDVIRALTHAIHTIKSGKHDPLKAHERVKGMYTWEEVAERTEKVYERAMETPSR
STAERLSR

Enzyme Prediction     

EC	2.4.1.198:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	537	677	3e-31	0.8875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340827	GT4_PIG-A-like	0.0	345	728	1	382	phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
340831	GT4_PimA-like	9.16e-57	346	712	2	366	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in certain bacteria and archaea.
153251	LPLAT_AGPAT-like	4.66e-51	55	244	7	184	Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.
223515	RfaB	3.12e-46	346	716	3	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
223282	PlsC	3.28e-41	26	251	18	227	1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADV21782.1|GT4	0.0	1	728	1	735
AFR95039.2|GT4	0.0	1	728	1	727
AUB24781.1|GT4	0.0	1	728	1	727
AAW43127.1|GT4	0.0	1	728	1	727
UOH80933.1|GT4	0.0	1	667	1	656

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KYM_A	2.83e-23	82	235	74	224	Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima [Thermotoga maritima MSB8],5KYM_B Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima [Thermotoga maritima MSB8]
6TVP_A	7.65e-14	344	711	15	396	Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155]
4N9W_A	2.02e-09	344	712	5	365	Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155]
2GEJ_A	2.15e-09	344	712	21	381	Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155]
6N1X_A	3.37e-09	355	681	13	338	Chain A, Glycosyltransferase [Staphylococcus aureus subsp. aureus CN1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P87172|GPI3_SCHPO	1.18e-137	348	712	1	363	Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gpi3 PE=3 SV=1
sp|Q64323|PIGA_MOUSE	1.40e-125	345	728	34	416	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Mus musculus OX=10090 GN=Piga PE=2 SV=1
sp|P37287|PIGA_HUMAN	1.91e-125	345	713	34	400	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Homo sapiens OX=9606 GN=PIGA PE=1 SV=1
sp|Q94BX4|PIGA_ARATH	3.59e-124	343	728	6	387	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Arabidopsis thaliana OX=3702 GN=PIGA PE=2 SV=1
sp|B3LKQ3|GPI3_YEAS1	3.54e-108	344	719	3	383	Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit OS=Saccharomyces cerevisiae (strain RM11-1a) OX=285006 GN=SPT14 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000001

TMHMM  Annotations     

Start	End
12	34