CAZyme Information: MGYG000000484_01646

Basic Information

• Species: Butyrivibrio_A sp000431815
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Butyrivibrio_A; Butyrivibrio_A sp000431815
• CAZyme ID: MGYG000000484_01646
• CAZy Family: CBM61
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
909	MGYG000000484_10|CGC1	97066.47	3.9964

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000484	2428908	MAG	Fiji	Oceania

• Gene Location: Start: 36581; End: 39310 Strand: +

Full Sequence      

MKSIVRKATAVGLAVAMAIGSMALSPVKGSQNVMLGNGDFETGTADEWNLSWDSATVSVD
QYASNNTTFTLTLPWYEADTEVSASYTTGTLDAGTYKVSLDISGAEMNSGLKLSVKAADG
TQLYTSDAITTTGWDAWQTVTSDEIILDAQSTVTVTLGGTETATYWGNIDNLVIEKTDGD
TEEADTTVDADIFVKKVKGLSDDFITGMDVSSYISEIESGVVYYDWDGNALDKQGFFNLL
ADSGVNWIRVRVWNNPYDTNGNGYGGGDNDLDKAIEIGKLATNAGMKVLVDFHYSDFWAD
PAKQKAPKAWSSMSLTEKETALYNYTYDSLTAIKAAGVDVGMVQVGNETNNGMCGETDMT
SKCALYNKGSEAVRAVDANILIALHFTNPENAGSYASIAEKLAANNVDYDVFASSYYTYW
HGTMSNLTSVLKNIADTYGKKVMVAETSYAYTMQDGDGHENTIKNSATDLVSGYSATVQG
QANVVRDVIQAVADIGSAGIGMLYWEPAWIPVKYAYENGEVSHDILTSNKTIWESKGSGW
ASGYAVEYDPDDAGVWYGGSAWDNQAMFDFAGKPLASLNVYKYVRTGAKTTVKVDSAEAL
NVEINAGDALTLPDRVIIYYNDGTTGEGNVTWDTNGTDVSTLEEGTYVFYGTIQGCDIKA
VLNVNVKSHNYVVNPSFEDSDRSMWVITGDADATDYQNKSADAASGDYSLHFWKGSDYAF
DVSQTITGLKPGTYRFTVSAQGGDAAGAVNAIYAVSSGVRQDASFELVGWTTWQNPVIEE
IVVGEDGTVTIGAALSLPSGAWGTLDDFTLTLVKASDEDNDKPSDEEDDKPSGDNDTPSG
DNSGNGSGDNSGDNGGDNGGGNNKLEEKDPDVGAGDGRLFKLVIMLGAAVVTVMITGSKI
YKKAVKNSN

Enzyme Prediction     

EC	3.2.1.89

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH53	205	580	5.3e-127	0.9941520467836257
CBM61	670	810	3.2e-38	0.9858156028368794
CBM61	35	172	6.3e-17	0.9574468085106383

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3867	GanB	9.46e-151	184	593	19	403	Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
pfam07745	Glyco_hydro_53	2.78e-132	205	581	1	333	Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
pfam07532	Big_4	5.70e-09	600	655	4	58	Bacterial Ig-like domain (group 4). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
cd04079	CBM6_agarase-like	0.001	84	176	45	134	Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 alpha- and beta agarases. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family 16 agarases. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the activity of alpha- and beta-agarase catalytic modules which are involved in the hydrolysis of 1,4-beta-D-galactosidic linkages. These CBM6s bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide, and directing the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. This family includes three tandem CBM6s from the Saccharophagus degradans agarase Aga86E, and three tandem CBM6s from Vibrio sp. strain PO-303 AgaA; in both these proteins these are appended to a GH16 domain. Vibrio AgaA also contains a Big-2-like protein-protein interaction domain. This family also includes two tandem CBM6s from an endo-type beta-agarase from a deep-sea Microbulbifer-like isolate, which are appended to a GH16 domain, and two of three CBM6s of Alteromonas agarilytica AgaA alpha-agarase, which are appended to a GH96 domain.
cd04080	CBM6_cellulase-like	0.002	93	149	68	122	Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase). This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKS46422.1	6.21e-251	82	811	139	853
SQI62631.1	8.52e-248	37	819	39	815
AYA74678.1	1.43e-241	13	817	12	815
AET58154.1	3.78e-239	22	820	14	812
QSF47646.1	2.00e-237	91	823	84	799

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R8L_A	8.35e-179	187	587	7	394	Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis]
2GFT_A	6.66e-178	187	587	7	394	ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
7OSK_A	2.81e-84	192	593	38	403	ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1HJS_A	2.04e-41	207	510	6	301	Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]
4BF7_A	2.00e-38	207	510	23	318	Emericillanidulans endo-beta-1,4-galactanase [Aspergillus nidulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q65CX5	1.11e-177	187	587	32	419	Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1
O07013	1.19e-169	191	587	40	423	Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
P48843	1.16e-61	204	537	6	337	Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
P48841	7.88e-46	199	523	20	343	Arabinogalactan endo-beta-1,4-galactanase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=ganB PE=1 SV=1
P83692	1.12e-40	207	510	6	301	Arabinogalactan endo-beta-1,4-galactanase OS=Thermothelomyces thermophilus OX=78579 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000408	0.998853	0.000249	0.000173	0.000153	0.000136

TMHMM  Annotations     

start	end
882	901