CAZyme Information: MGYG000000977_01645

Basic Information

• Species: Clostridium sp900539375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900539375
• CAZyme ID: MGYG000000977_01645
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
965	MGYG000000977_16|CGC2	108380.78	6.3379

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000977	2927434	MAG	Australia	Oceania

• Gene Location: Start: 32365; End: 35262 Strand: -

Full Sequence      

MLKFKKKIISLITSLTVSSSIFIGIPITTEAVTTENSISTEKSLKNYNLPEDVKDGVILH
AWNWSFNQVKEHIEEIAECGYGSVQVSPIQPNKDSPMQNTSQWWKLYQPINFTIGNDLGT
AEEFKAMCDEAHKYGVKIIVDVVSNHLANKTNGYDKSEQIPDYIRNNSNYWHSSSIGKVN
DSSRYQMTQGNIGMPDLNTGNTEIQNMVIKFLNEAQDLGADGFRFDAAKHIELPTDGNIA
SDFWPRVINAIKSKDSNSFVYGEILGTAGTSIENYTKYIKVTDCGMGYDVRKAIYDTNVS
LVQNYTIDKASNAITWVESHDTYANDEHETTYMTDEQIKLGWGLIGARNKSVPLFFVRPT
SMNAALGSYTTLWQNKEIVEVNKFHNYFEGKSEYVRKLNNNSVFAVERGGEGVVLTNLGS
GKAKINTETTLKDGTYIDTVSGASFTVYNGKLSGEISGRKIAVLYNSNTPINKGTVTFKY
IDKETKKEIAEPVIISGGVGTKFSHNLKDIDGYEFNCSISDDKLIFTEEPITITYEYSKY
AKGNVIIKYVNADTKEEIETSKSISGKIGTSYTTEAKDIKGYELVESPNNASGVYTENDI
TVIYLYKEKEFNTLKVHYYNKNNWSNVYLYTYAKVDGVTVKYTGNWPGTKMTNEGNGWWS
FEVTDAEEAYIMFNNNNGSQEPAANQSGYEASGEVWVKDKKVLYKNPDAPETGKVIVKYI
DEETGEILKTIKLEDEIGKDYKTESLSIDGYTLKTIPTNSIGKFTKGDIEVIYKYSKDVL
VPTIESFTPDKASPQLQGTNIKLTVKASGKGTLQYKFIIKDDKGNWYKLRDFSTSNTYVW
KASASGNKKLYVDVKDEFGNVVREELNYKIIASSNLEIQSFTVDKTSPQVKGTNVKLTVK
ASGKGTLQYKFIIKDDKGNWYKLRDFSTSNTYVWKTTVAGSKKLYVDVKDEDGKVVRKEL
NYVVK

Enzyme Prediction     

No EC number prediction in MGYG000000977_01645.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	64	327	7.4e-87	0.9924812030075187
CBM26	615	685	2.4e-20	0.92

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	3.29e-129	55	395	1	352	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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	3.98e-41	56	322	2	238	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
NF033187	internalin_J	4.43e-25	444	813	485	816	class 1 internalin InlJ. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin J (InlJ).
COG0366	AmyA	1.26e-20	64	269	26	244	Glycosidase [Carbohydrate transport and metabolism].
pfam16738	CBM26	1.29e-20	616	685	1	68	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASR47410.1	2.92e-137	46	707	45	656
QDY86356.1	6.21e-136	46	707	45	656
CDM67894.1	1.35e-135	47	953	44	936
QYK62214.1	1.94e-133	46	707	53	664
APB71173.2	5.36e-133	46	707	53	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	2.66e-101	53	465	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	4.25e-100	53	465	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	7.55e-100	53	465	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1VIW_A	8.12e-23	58	475	13	456	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	8.17e-22	58	475	13	456	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	9.73e-108	53	690	47	641	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.36e-92	43	719	41	684	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	3.46e-70	30	726	131	811	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
Q71VU0	4.04e-28	444	780	485	788	Internalin J OS=Listeria monocytogenes serotype 4b (strain F2365) OX=265669 GN=inlJ PE=3 SV=1
P27350	5.88e-28	50	469	31	458	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy 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
0.000680	0.998392	0.000259	0.000257	0.000198	0.000178

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000977_01645.