CAZyme Information: MGYG000004899_00447

Basic Information

• Species: Bacteroides sp900555635
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635
• CAZyme ID: MGYG000004899_00447
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
887	MGYG000004899_2|CGC2	100311.19	5.0939

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004899	5396709	MAG	China	Asia

• Gene Location: Start: 105091; End: 107754 Strand: -

Full Sequence      

MKNRIICVLAILLSLHAHSREHVDIGTMVTASVTKNGNLSAGGIAVASSSKGSRSAAKAI
DNDRSSYWQSSKSEGWFVVDLKAPYQLTSIRQEFLQSSVWRFKIEGSVDNENWLLLIDRT
KGIAGDIFAESVSGVYRYVKLTVMGSADGFLPSSRELFITGANADKNIALGKQCTNVLLQ
EDHCPMDALDGNMSTYWMAENDRFPQEMTVDLGEICNLSGVQQIFKDYDQWKYIIEGSND
ELQWQVLVDNSAGISGFDFKSPASGKFRYVRLSVLGSSKGYWAHSCEFRVFGSETQDGFS
NNQGLRNLAYDALASTSSFCDNAHEQKKAFDSDNETFWYANDGTYPQWLCADLGLPCNIR
SIEQRFAEKDVWSFIIEGSNDTKRWDVLADCRSGVAGSEYSKDLNGVYRYIKLTVLGAKY
GSRASSRSLVISGLGSPRNTAWWEESSGMTRYYPKYYRQTLKSIKDSLDILQGQGYRSIE
LSAIYEGDPSVWGGLGATDNYAIDPSIGTMEDFEELLREIHARDMRLTFFGNVGYCWYKA
PFFEKACDDQRNNVDSKERSWFHFSDKKISDNWFWSERAQAYYYSFWGNSDGAEGRIPSY
NFNNKEWQEECRNYLEYWANKGVDGLLLDAPEAYDGINDNIINESIVRVLNRRGILTNAE
GSWDVNKWIGRFGFRLIQGFDMYGWGGGKKSEALNARRNQNPAELNDKLKNYRDRAVALG
GTTITPPMWEIPATNEERLFELAYLVSMGTLVINHYGDHHQEYIAQSILAKWPAKDQERF
YDLIRLQNSYNGLAPLGQRTCIPTNDDTKYTVFKRSNKDGKVSALVIMNFQNSAETISFN
LKNTGIMLEQSPINLLDKNDLLPVLSENYQVTLPAYGYLILGVQNAE

Enzyme Prediction     

No EC number prediction in MGYG000004899_00447.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	461	633	5.1e-23	0.5382165605095541
CBM32	48	145	9.4e-16	0.7983870967741935

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	6.59e-21	461	630	22	185	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
cd11359	AmyAc_SLC3A1	8.44e-19	442	630	2	199	Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins. SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
COG0366	AmyA	1.47e-18	460	631	27	200	Glycosidase [Carbohydrate transport and metabolism].
cd11334	AmyAc_TreS	3.86e-18	460	630	25	197	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
pfam00128	Alpha-amylase	8.39e-18	460	630	2	173	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQA30230.1	0.0	1	887	1	892
QUT61733.1	0.0	1	887	3	894
ATB27203.1	3.82e-234	17	883	151	992
QNK56434.1	4.78e-52	76	415	618	947
SDU79006.1	3.02e-30	437	883	50	501

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Y9T_A	1.98e-14	416	630	1	219	FamilyGH13_31 enzyme [Lactobacillus acidophilus NCFM],6Y9T_B Family GH13_31 enzyme [Lactobacillus acidophilus NCFM]
6YUP_A	2.41e-14	436	630	111	315	ChainA, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUP_C Chain C, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUZ_A Chain A, Neutral and basic amino acid transport protein rBAT [Homo sapiens],6YUZ_C Chain C, Neutral and basic amino acid transport protein rBAT [Homo sapiens]
6LI9_A	2.46e-14	436	630	125	329	Heteromericamino acid transporter b0,+AT-rBAT complex bound with Arginine [Homo sapiens],6LI9_C Heteromeric amino acid transporter b0,+AT-rBAT complex bound with Arginine [Homo sapiens],6LID_A Heteromeric amino acid transporter b0,+AT-rBAT complex [Homo sapiens],6LID_C Heteromeric amino acid transporter b0,+AT-rBAT complex [Homo sapiens]
2ZE0_A	2.32e-13	442	630	5	200	Alpha-glucosidaseGSJ [Geobacillus sp. HTA-462]
4AIE_A	1.21e-12	439	645	3	216	Structureof glucan-1,6-alpha-glucosidase from Lactobacillus acidophilus NCFM [Lactobacillus acidophilus NCFM]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	5.58e-16	461	641	56	226	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q07837	1.32e-13	436	630	111	315	Neutral and basic amino acid transport protein rBAT OS=Homo sapiens OX=9606 GN=SLC3A1 PE=1 SV=2
Q64319	6.88e-13	436	645	108	331	Neutral and basic amino acid transport protein rBAT OS=Rattus norvegicus OX=10116 GN=Slc3a1 PE=1 SV=1
Q9P6J3	1.01e-12	442	630	13	213	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
O05242	2.21e-12	441	630	4	200	Probable oligo-1,6-glucosidase 3 OS=Bacillus subtilis (strain 168) OX=224308 GN=yugT PE=3 SV=2

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
0.000266	0.999055	0.000217	0.000152	0.000149	0.000138

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004899_00447.