CAZyme Information: MGYG000001615_01331

Basic Information

• Species: Eisenbergiella sp900548905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900548905
• CAZyme ID: MGYG000001615_01331
• CAZy Family: GH97
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
852	MGYG000001615_6|CGC5	96320.47	4.9227

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001615	6842156	MAG	China	Asia

• Gene Location: Start: 118844; End: 121402 Strand: +

Full Sequence      

MMWTLDSPNKAVKVTVKQREDGSLLYGAARHGKKVIEESAAGICTELGDFTDGLVFEREE
SRSIREEYSIPAGKKEVYTNHAEELALYFHACDSLFIFRLRAFDDGMAFRYEIQHPGRET
FLVKKERTEFRISPNGDKLWLQDWIPTYEGPYNARAWDKSMNGQPFGMPSLFFSEKDGAW
IMLNEANVINSDGSYCSCHLIGNENGCMSIGFAPEEKGKPIKTPLPFRSPWRYAVIAGSL
DELVNSTINYNLNPPSVITDTSWIKPGRALWSWWEDMNGAQLYLESRNYVDMAAAYGFEG
LTLDCGWDACWVKELCEYAHKKNVQIWIWTAMQRLDTREKAEELIPLWAGWGVDGLKIDF
FENDSRHTMWQYNMIADLMIENKLMINFHGSVKPMGEGRTWPNFMTAEGIMGMEHYQWSD
MPNSLHNCTVPFTRNVAGPMDYTPTAFSNLKNRNTTMGHQLALPVVFDSGLTNYALALRF
MEGWKGTDFLRRTKNHYRGVKVLSGYPGDHAAILRYTDSEWLIGVITSPKKKVTLSLDFL
GEGEYEAEIYEDSAKGDMISRTYRKVCAEDTLEMSLLANGGAGIYITGKIEPLPCGICSG
YMSDRCTEYPGKDAKMIQGSEKVVWDEETAGFVLNGAAEFCGKVKETKNYSLRFFYAAEE
PWEMEFCCGDYTETVKMPASNAIRTFVTHEIIVPVKEGDVTFRMKRISGKAPAVWKLKLI
DNDPFMPVAYGIREENLCGGGEITVVDGVAAATGLGWDAQLLFDEVTVPAAGRYVLRIIY
AAGDCRDISIQANDGDVIDTYLHSTSGWEFPTWEYVGEKEVLVNLKEGRNRIRLFNDHGL
ISHIRGIELIAE

Enzyme Prediction     

No EC number prediction in MGYG000001615_01331.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH97	3	585	7.3e-154	0.9746434231378764

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam10566	Glyco_hydro_97	2.81e-68	260	491	1	275	Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
pfam14508	GH97_N	1.18e-49	7	255	1	235	Glycosyl-hydrolase 97 N-terminal. This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
pfam14509	GH97_C	1.72e-19	501	587	5	97	Glycosyl-hydrolase 97 C-terminal, oligomerization. Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
cd04081	CBM35_galactosidase-like	2.55e-12	738	839	23	115	Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.
cd04083	CBM35_Lmo2446-like	2.65e-09	746	839	29	113	Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGQ93835.1	1.87e-314	2	852	1	848
AEC02290.1	1.53e-149	6	839	50	854
AEE97714.1	7.25e-132	2	584	11	588
SDT24292.1	5.41e-128	4	807	44	844
APZ33378.1	1.42e-127	4	834	13	838

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HQ4_A	2.29e-58	4	591	2	663	AGlycoside Hydrolase Family 97 enzyme from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8],5HQA_A A Glycoside Hydrolase Family 97 enzyme in complex with Acarbose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
5HQC_A	2.29e-58	4	591	2	663	AGlycoside Hydrolase Family 97 enzyme R171K variant from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
5XFM_A	5.10e-58	8	581	22	637	Crystalstructure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_B Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_C Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_D Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron]
5HQB_A	5.83e-58	4	591	2	663	AGlycoside Hydrolase Family 97 enzyme (E480Q) in complex with Panose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
3A24_A	1.19e-54	7	586	6	640	Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D7CFN7	1.11e-66	3	581	35	615	Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1
Q8A6L0	7.61e-55	3	586	23	661	Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
G8JZS4	2.00e-41	5	589	25	724	Glucan 1,4-alpha-glucosidase SusB OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susB PE=1 SV=1

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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001615_01331.