dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001024_01586

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Basic Information help

Species

HGM11521 sp900751885

Lineage

Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11521; HGM11521 sp900751885

CAZyme ID

MGYG000001024_01586

CAZy Family

GH146

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
940		106569.93	5.0114

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001024	2614111	MAG	Sweden	Europe

Gene Location

Start: 5445; End: 8267 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001024_01586.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH146	26	574	1.6e-157	0.9980119284294234

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07944	Glyco_hydro_127	6.42e-112	26	574	1	503	Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
COG3533	COG3533	3.68e-75	27	654	12	572	Uncharacterized conserved protein, DUF1680 family [Function unknown].
pfam12733	Cadherin-like	2.86e-05	854	934	5	87	Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJW37681.1	6.78e-247	19	936	369	1293
QDP74899.1	7.48e-246	19	936	369	1293
ARU52215.1	4.16e-245	19	936	369	1293
ARK06383.1	4.16e-245	19	936	369	1293
QUB98427.1	1.64e-244	19	936	369	1293

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YQH_AAA	1.96e-91	12	802	18	780	ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]
5OPJ_A	3.21e-86	12	802	18	780	Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron]

Swiss-Prot Hits help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000036	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001024_01586.