dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Parabacteroides goldsteinii

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii

CAZyme ID

MGYG000001489_01368

CAZy Family

GH33

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
704	MGYG000001489_1\|CGC32	78852.96	4.9327

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001489	6453137	Isolate	not provided	not provided

Gene Location

Start: 1770478; End: 1772592 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000001489_01368.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH33	394	604	2.6e-19	0.5584795321637427

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	1.71e-22	359	693	17	333	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
COG1957	URH1	3.39e-16	38	212	3	174	Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism].
cd02651	nuc_hydro_IU_UC_XIUA	2.40e-15	40	324	2	298	nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, xanthosine-inosine-uridine-adenosine-preferring and, uridine-cytidine preferring nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains proteins similar to nucleoside hydrolases which hydrolyze both pyrimidine and purine ribonucleosides: the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the inosine-uridine-xanthosine preferring nucleoside hydrolase RihC from Escherichia coli and the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium. This group also contains proteins similar to the pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases URH1 from Saccharomyces cerevisiae, E. coli RihA and E. coli RihB. E. coli RihA is equally efficient with uridine and cytidine, E. coli RihB prefers cytidine over uridine. S. cerevisiae URH1 prefers uridine over cytidine.
cd00455	nuc_hydro	7.77e-15	40	302	1	261	nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment.
pfam01156	IU_nuc_hydro	4.25e-14	38	322	1	255	Inosine-uridine preferring nucleoside hydrolase.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SCM58084.1	3.26e-188	341	698	37	393
BBD46309.1	3.44e-185	340	701	35	395
ACT93133.1	2.23e-171	320	700	12	398
SOE23805.1	2.19e-170	340	700	25	382
QGY48039.1	1.67e-167	342	700	27	384

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HX0_A	9.46e-170	320	700	15	401	ChainA, Uncharacterized protein Dfer_1899 [Dyadobacter fermentans DSM 18053],5HX0_B Chain B, Uncharacterized protein Dfer_1899 [Dyadobacter fermentans DSM 18053]
4KPN_A	3.46e-10	38	222	30	215	Plantnucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_B Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_C Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_D Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_E Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_F Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_G Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens],4KPN_H Plant nucleoside hydrolase - PpNRh1 enzyme [Physcomitrium patens]
6BA1_A	2.13e-06	37	216	4	184	Purine-PreferringRibonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_B Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_C Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_D Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_E Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_F Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_G Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_H Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_I Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_J Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_K Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_L Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_M Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_N Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_O Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_P Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_Q Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA1_R Purine-Preferring Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A]
6BA0_A	2.75e-06	40	254	7	213	Pyrimidine-specificRibonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA0_B Pyrimidine-specific Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA0_C Pyrimidine-specific Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A],6BA0_D Pyrimidine-specific Ribonucleoside Hydrolase from Gardnerella vaginalis [Gardnerella vaginalis 315-A]
3G5I_A	4.80e-06	40	253	6	210	CrystalStructure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor [Escherichia coli K-12],3G5I_B Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor [Escherichia coli K-12],3G5I_C Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor [Escherichia coli K-12],3G5I_D Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor [Escherichia coli K-12]