CAZyme Information: MGYG000000284_00107

Basic Information

• Species: Parabacteroides sp900540715
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900540715
• CAZyme ID: MGYG000000284_00107
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	MGYG000000284_1|CGC5	65545.29	4.8767

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000284	5935659	MAG	Sweden	Europe

• Gene Location: Start: 164047; End: 165783 Strand: -

Full Sequence      

MKKLLLTLLAVPLWVSCQDSHQIEAKIAQSPKTFCNPVNLNLQTMKIDGGEGIREAADPV
VVTFKEKHYLCASKSSGYWYSDDFTNWKHVFITDSVLPIEDYAPGLFIHNDYLYYVGSTH
GKGMLYRSSAPEKGEWEPVKEIWSFWDPAFYVEGDNLYMYYGCSPVDPIYMQVLDLNTLE
AKTEVITCFNSDKENHGWERTGELNELPRRPYIEGAWMTAHQGKYYLQYAAPGTEWKSYA
DGAYVSASPTGPFTYMENSPVSYKPTGFIGGAGHGCMFTVGNENYWKAATNSISVRHMFE
RRVSFFPAGFDKDGYLYTNTYLGDYPMYLPGGKEQTAGSYQPGWMLLSYKKPVTVSSSLD
GYPAENTVDEDSRTAWVAASNKADEWLQVDLQNLSSIQAIQVNFDEYGANQRGFVPDVYQ
SYLISASANGKDWYPVVDYSTKKTDTPHDYIEFEAPFKARYIKLQNKEYTVSSNLSVRDL
RIFGNGLGSKPRAVNDFTVKRDLTDPCRVRLSWNEVPHTQGYIVRYGVAEDKLYNNFQVM
GDTTLEIGSLNQGVTYYFTIDTYNENGVTQTSQVEVCQ

Enzyme Prediction     

No EC number prediction in MGYG000000284_00107.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	56	314	1.1e-95	0.9961832061068703
CBM32	356	470	2.5e-22	0.8145161290322581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08982	GH43-like	1.95e-164	54	357	3	308	Glycosyl hydrolase family 43 protein; uncharacterized. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08978	GH_F	7.14e-22	57	286	1	245	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08991	GH43_HoAraf43-like	2.96e-19	57	305	1	272	Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam00754	F5_F8_type_C	2.37e-18	352	478	1	124	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam04616	Glyco_hydro_43	4.77e-14	57	285	11	249	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT49472.1	4.43e-199	248	578	15	345
QIA09145.1	8.33e-168	34	574	35	575
BBE16007.1	5.50e-167	29	574	26	570
ADQ81046.1	7.53e-167	1	570	1	565
ALM50367.1	3.25e-163	33	574	29	570

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QQS_A	2.85e-09	33	274	4	256	Crystalstructure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168],4QQS_B Crystal structure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168]
3BN6_A	3.52e-06	333	465	15	141	CrystalStructure of the C2 Domain of Bovine Lactadherin at 1.67 Angstrom Resolution [Bos taurus]
2PQS_A	3.58e-06	333	465	16	142	CrystalStructure of the Bovine Lactadherin C2 Domain [Bos taurus],2PQS_B Crystal Structure of the Bovine Lactadherin C2 Domain [Bos taurus],2PQS_C Crystal Structure of the Bovine Lactadherin C2 Domain [Bos taurus],2PQS_D Crystal Structure of the Bovine Lactadherin C2 Domain [Bos taurus]
2L9L_A	7.86e-06	362	464	40	144	NMRStructure of the Mouse MFG-E8 C2 Domain [Mus musculus]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000310	0.182849	0.816633	0.000083	0.000085	0.000072

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000284_00107.