CAZyme Information: MGYG000000030_00441

Basic Information

• Species: CAG-603 sp900066105
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-603; CAG-603 sp900066105
• CAZyme ID: MGYG000000030_00441
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
947		104889.18	5.863

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000030	3025033	Isolate	United Kingdom	Europe

• Gene Location: Start: 82045; End: 84888 Strand: +

Full Sequence      

MQKKFFSGLKKTVASVLSTVMVLSTFSGLTIIRAKQEIAYASNGYELVDDIQDSAILHCW
NWSYSTIEDHLELIAQCGYSAIQTSPAQQPKDYAWEGVVGMDVGFPSCGGTGNWWKLYQP
VTFSVCNNGITWLGTKAELESLCAKAETYGIKVIVDVVANHMGNITGWKNNLSDVSKQVG
EYWNPDMLTDETFWHINTRFVHDDDSRISFTMGCMGMPDLNTADSRVQTYVKNYLNELID
CGVDGFRFDAAKHIETPDDDPSYASDFWPNVLNSAKSYYKSKTGKDLYVYGEILNTVGDN
FDISGYTKYMSVTDNNAGNKTLEGVRGNTPSTPALKYPANKSVLWAESHDTYMNESSRYA
SDRAIIRAWAAVENVDNAAALFYVRPYYSTETLVNDMDNQFISNPQKNLEKRLMGVCNTY
TWATKEVAAINHFNNRFYNCSDSQGTSDNITYIKRGNGIILVNFNGSGEISTDAHGLASG
TYTDEVSGNTFTVSDGTISGNITSEYGIAVIYQNVMSNPTTKHPAQIATNLGNGSVFYTN
GLDVDVTVMNATSASYTASTGESGTLTGEKTVTIGKGLKDGQTVTLTVKATSSYGTVTKK
FTYTKQSKAVEISTSKKDGSGFYTDGFTLTMEALYATNATYTTSDGQSGSFATTKDITIG
TGLKVGEKVTVTIKANNDLGSVTKTFTYIKKEGSNAIYFKNTNNWSDVTAYAWKNETVKN
AAWPGAPMECIDAENQIFMVELDPDAGYTKIIFSNNGASQTADLDIPELGYIYTGSGWEE
YEETKTGWQQAGKYWYYYDSNGKMVTGWQKISGKWYYFNDSGIMQTGWIKLDGKWYHLKG
SGEMQKGWIKLSGKWYYLKGSGVMQTGWIKLDGKWYHLKGSGEMQKGWQKISGKWYYLNA
SGVMQTGWIKLNGKWYYLKSSGEMISGEKVTIGGKSYTFNSNGVWIK

Enzyme Prediction     

No EC number prediction in MGYG000000030_00441.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	62	356	7.1e-72	0.9924812030075187
CBM26	697	764	2.6e-16	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	4.97e-99	53	437	1	345	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.
NF033930	pneumo_PspA	4.58e-59	785	947	442	607	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	5.15e-57	786	946	483	660	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033838	PspC_subgroup_1	1.52e-52	785	927	485	627	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
NF033838	PspC_subgroup_1	1.94e-51	786	943	506	663	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM70432.1	7.83e-97	17	781	11	742
QCT06294.1	2.17e-94	38	786	43	684
QLY40627.1	7.82e-81	43	611	75	599
CDM67953.1	2.58e-77	9	779	4	664
QDY86356.1	1.87e-75	41	606	42	559

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	9.09e-58	51	512	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
3DC0_A	3.20e-57	51	512	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	1.21e-56	51	512	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1XGZ_A	1.86e-15	54	371	11	318	ChainA, Alpha-amylase, pancreatic [Homo sapiens],1XH0_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH1_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],1XH2_A Chain A, Alpha-amylase, pancreatic [Homo sapiens],3BAK_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAX_A Chain A, Pancreatic alpha-amylase [Homo sapiens],3BAY_A Chain A, Pancreatic alpha-amylase [Homo sapiens]
1KGW_A	2.46e-15	54	393	11	339	ChainA, ALPHA-AMYLASE, PANCREATIC [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.99e-63	51	775	47	646	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	5.35e-48	40	519	40	467	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	1.13e-45	23	785	117	912	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P41131	1.43e-20	53	369	25	317	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA PE=3 SV=1
O18345	3.79e-19	54	489	29	454	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 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
0.303555	0.640508	0.051616	0.002199	0.000800	0.001294

TMHMM  Annotations     

start	end
13	32