CAZyme Information: SPRG_09957-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_09957-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
404		44379.02	7.5874

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

• Gene Location: location=KK583257:54577-55898(+)

Full Sequence      

MALLALPSAKATRPTSRTLCFGVTSWPMDGQKRLWLRLIASLRAHPTIDYSFHIFLLEPK
PVHPTDVFTAHGLNVTHVPMMVSREDIARYDITHEKMRVALADFADADDRTTFPSYVHSL
WASLVAAFAPCKGGVLSYPNSRNHDDRVWAGLGRAAGAAGVVLELSSVRPTPHTVDLLIG
PSQYTLAHPSVINGMRADMRSVIPPGVDPTIFAPRARSHTNRCVVVGYLGRLTLEKSLGL
LARAVELLTQTNMTSSCVTFRWVGDGADAKYYKRYPITFLGSIDDEAALIHELQTWDVAV
QPGLQETFCIANLEVMAVGLPLVTFGVAGVAEYVRHEENAWVVDEISPRALAAAIALLAD
DPILRRQLGHGARRTVETRYTWAHTVAAYDEAYGRLIGSAMYKP

Enzyme Prediction     

No EC number prediction in SPRG_09957-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	225	368	3.4e-21	0.91875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223515	RfaB	6.26e-30	50	398	22	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831	GT4_PimA-like	1.13e-27	19	393	4	365	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.
340842	GT4-like	1.56e-21	202	384	170	355	glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.
340837	GT4_CapM-like	6.90e-20	206	389	172	357	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
395425	Glycos_transf_1	4.30e-19	225	374	4	157	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55764.1|GT4	1.73e-120	3	385	127	503
QTE29023.1|GT4	5.22e-17	196	397	148	356
QKS48987.1|GT4	1.25e-16	201	391	181	376
QIA27462.1|GT4	4.45e-16	50	398	33	392
UNK46420.1|GT4	4.85e-16	50	393	40	397

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3C4Q_A	1.89e-08	198	399	188	408	Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A	1.94e-08	198	399	208	428	Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D3Q051|MSHA_STANL	7.97e-10	198	404	210	435	D-inositol 3-phosphate glycosyltransferase OS=Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 / LLR-40K-21) OX=446470 GN=mshA PE=3 SV=1
sp|P0CF99|PIMC_MYCTO	3.71e-09	203	396	172	368	GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol dimannoside mannosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=pimC PE=1 SV=1
sp|A5U3B9|PIMC_MYCTA	3.71e-09	203	396	172	368	GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol dimannoside mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=pimC PE=3 SV=1
sp|Q8NTA6|MSHA_CORGL	9.55e-08	198	399	188	408	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1
sp|A4QB40|MSHA_CORGB	9.55e-08	198	399	188	408	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain R) OX=340322 GN=mshA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000001

TMHMM  Annotations     

There is no transmembrane helices in SPRG_09957-t26_1-p1.