CAZyme Information: MGYG000002857_00301

Basic Information

• Species: Hydrogeniiclostridium sp900550095
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Hydrogeniiclostridium; Hydrogeniiclostridium sp900550095
• CAZyme ID: MGYG000002857_00301
• CAZy Family: GH93
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
363		41247	4.6703

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002857	2686801	MAG	United States	North America

• Gene Location: Start: 11162; End: 12253 Strand: -

Full Sequence      

MMANETEKTVHVRWEEPIQIHDYPVFQDTNRDARVVSPGTYGSEYVRMLELKDGSWLSVY
TFYDNNGYRLEAGGGTKLGFSLSRDQGKTWEQISTLSHPSRDMDNGQLAFAENGDILLSC
RSVRWQESYYLPLYRSADGGRNWEFSSMIDETSGHPGALGNPDKGLYEPHLYRLEDGRLA
VMYANEKHVKRAPHFSQIISMKVSDDDGETWGDEIWVAWDPERPELRPGMPVWMRLKNGL
YMVVFEVGDPSVKPEATFYIYYKTSKNGVDWEPGIGTLIPEQWGGPYLEQLEDGRLLVSS
NAGVISVGNEEGAQWKTLEPPAFPSFTWSSLKALEGNRFAVFNSCSREEGGHNIQLRFGE
LEK

Enzyme Prediction     

No EC number prediction in MGYG000002857_00301.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH93	43	340	8.1e-69	0.9804560260586319

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	4.11e-12	14	258	125	335	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.
cd15482	Sialidase_non-viral	1.96e-09	14	213	59	239	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.
cd15482	Sialidase_non-viral	1.90e-08	35	357	3	336	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.
pfam13088	BNR_2	1.27e-06	37	225	103	264	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd08996	GH32_FFase	0.002	174	308	70	207	Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYQ73077.1	9.56e-160	9	363	378	734
AYQ75607.1	4.35e-127	20	361	36	372
QIP14490.1	2.88e-126	12	363	24	374
QHV93795.1	4.70e-125	12	361	24	372
AYQ71526.1	3.53e-120	18	361	34	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A71_A	1.76e-13	83	353	57	342	Highresolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000034	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002857_00301.