CAZyme Information: MGYG000000030_01566

Basic Information

• Species: CAG-603 sp900066105
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-603; CAG-603 sp900066105
• CAZyme ID: MGYG000000030_01566
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1285		141670.51	5.551

Genome Property

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

• Gene Location: Start: 76864; End: 80721 Strand: +

Full Sequence      

MKKLKNLTLKCASFMMATVMVGTGFLDSLTLSSKRITGNISNGIVAEAAETGTVNADTFS
WDNASVYFLLTDRFRNGDTSNDHSYNRGLDKNGNVINVSDDRGTFHGGDFKGVTQSIKEG
YFNNLGVNAIWISAPYEQIHGYIVGGDGSPSFAHYSYHGYYVLDYTNSDANFGTMDEFKE
LVDTAHEHGIRVVMDIVLNHAGYNSLYDMNEYGFGSVKSGWEDYYYSMTNVNNKDYHSYI
DYEADAVAWGKWWGSDWVRAGLPGYTAGGGDSYTMSLAGLPDFRTESTATVGIPAFLEKK
WKSEGRYDSEVAELKSYLSSHGYDMTVTNCISYWLSTWVREYGVDGFRCDTAKHVEFASW
KRLNDMCTEALKTWKANNPDKKLDDLDFWMTGECWDHGVDNDAYYSKGGFDSMINFETTG
GGMLAEGRIESVYARYATAINDTPDFNVLSYMSSHDSTLARGNMVYLGSALLLLPGGIQI
YYGDETNRGLVDSIPFDGNGGAGHSLRSDMNWDSIDETVLSHWQKVGTFRNSHIAVGAGQ
NTTITTSSGHAFTRTYESGNIKDRVAFCIAAAANTEVTMDVSNVWKDGDRVVNYYDSSSA
VVTDGKVTFNSGANGTVLVQDPDGKPLVTINGEAKFKGTQKVTVSLKDTKQAVISVDGAK
KFIVKDGDSFTIGATAYEGDTVTVSYTAENEKGVVNGKATFYKAYGNEDVGGGGEEEKED
NIIRIKMANGSAPYLYAWTGASTALTDAWPGTKLTEKDSDGYYTFEFAKDISTYNVIIND
GGSGQTSDITGLKGKVTVNVASDFTTKINGGSVEVVENTVTIHIKPYSDVAPFLYVWDNS
GSYNGGFPGKQLSNPDADGWYTFVKEGVSSLNCIVGDGGSSNRTGDITGITSEAWITIKS
ADNTKYDIEKTPVIESKYTLLRKEARAVKNLTVSDYTQASYKKLYSYIAQADKLVALGEK
EADITEVETTYNNIINAKKALVLATPSISSASAGSKAITGKAAYGSKVTVKLNNKTYTAV
TDEITGVWKVNVATALKSTDVLYVSANRDDLKSGELTYKMSGGDVITVGWKEIDSEWYYF
DASGVMQTSKWINGTYYVQADGTMAKSQLVDNNKYYVDANGKWVKTTKWLKINNKWYYNV
SGNIQKSKWVKINSKWYHFDASGVMETSKWINGTYYVQADGTMAKSKLVDNNKYYVDANG
KWVKTTKWLKINNKWYYNVSGNIQKSKWVKINSKWYYFDASGAMQTSKWINGTYYVQADG
TMAVSKWVDGGKYYVGADGKWVKNK

Enzyme Prediction     

No EC number prediction in MGYG000000030_01566.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	108	486	9.6e-148	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	41	565	168	675	alpha-amylase; Reviewed
cd11338	AmyAc_CMD	5.13e-43	72	535	10	383	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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	2.08e-42	64	555	1	438	Glycosidase [Carbohydrate transport and metabolism].
cd11339	AmyAc_bac_CMD_like_2	8.17e-41	65	533	4	344	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
NF033838	PspC_subgroup_1	1.66e-38	1069	1282	487	683	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
BCN30960.1	0.0	41	1066	40	1060
QCT06045.1	5.07e-260	55	887	51	883
QCT06087.1	2.14e-208	17	658	16	705
QMV42547.1	9.19e-201	48	783	28	744
CDM67955.1	1.35e-199	50	785	60	805

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.98e-26	60	580	5	409	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.45e-26	60	580	39	443	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	2.30e-25	60	551	6	383	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1V3J_A	4.37e-20	48	200	1	140	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3J_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_A Chain A, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1V3L_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
1UKS_A	4.37e-20	48	200	1	140	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1UKS_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.28e-129	41	554	167	661	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	2.30e-21	61	355	744	946	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P16950	1.72e-20	55	621	376	921	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P09121	1.92e-19	45	200	25	167	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P05618	1.93e-19	45	200	25	167	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt 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
0.562093	0.433072	0.002759	0.000536	0.000516	0.001019

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000030_01566.