CAZyme Information: MGYG000003682_02615

Basic Information

• Species: Ruthenibacterium lactatiformans
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruthenibacterium; Ruthenibacterium lactatiformans
• CAZyme ID: MGYG000003682_02615
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
379	MGYG000003682_17|CGC1	42729.43	7.6536

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003682	3961825	Isolate	China	Asia

• Gene Location: Start: 13924; End: 15063 Strand: +

Full Sequence      

MYGLAQVPVTERAMLEKDEALKPANMATGRLGGRYVGRNRKWQGIPSLTRTRGGRLYVCF
YSGGEGEGAENYVLLKKSDDDGKTWSEPVLAIDPAGNVRAFDPCLWTAPDGRVFLFWAQS
YGGFDGRAGCWYATCEAPDVRRPEWSAPSRIGDGVMLNKPTVLHTGEWLLPVSLWKAIPS
EYNPSRPNRLANVYLSSDQGRHFRYLSGVDMPDRFYDEHMLVEKQDGTLWMLLRLKTGIG
EAFSSDGGKTWREVRKSGIWGPNARFFIRRLRSGRLLLVNHAQEEGGGASSGRRNRLAAF
LSEDDGKTWSKPLILDCREDVSYPDGVEREDGLIYIIYDRSRFEQKEILMAKFREKDVLA
QQMVSVDGELQILVDKAGE

Enzyme Prediction     

No EC number prediction in MGYG000003682_02615.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	45	350	1.5e-32	0.9210526315789473

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	7.11e-50	45	354	16	339	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	1.38e-24	54	336	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam04616	Glyco_hydro_43	7.25e-04	37	119	63	133	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.
COG3507	XynB2	0.001	60	127	111	168	Beta-xylosidase [Carbohydrate transport and metabolism].
cd18617	GH43_XynB-like	0.004	43	131	66	148	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDT91705.1	8.16e-124	16	377	29	388
QDU15387.1	1.64e-123	11	377	24	388
QEG17440.1	6.60e-123	16	377	25	388
QDT79764.1	2.66e-122	16	377	25	388
QGQ32653.1	1.08e-121	42	377	2	336

PDB Hits     

has no PDB hit.

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
1.000048	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003682_02615.