CAZyme Information: MGYG000004802_00453

Basic Information

• Species: UMGS1384 sp900551265
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; UMGS1384; UMGS1384 sp900551265
• CAZyme ID: MGYG000004802_00453
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
944	MGYG000004802_16|CGC1	107500.05	5.4387

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004802	2084927	MAG	Spain	Europe

• Gene Location: Start: 16521; End: 19355 Strand: +

Full Sequence      

MLIYHHSQDLNYRRPFGAAEVSSRVSIALDATDTAAVTLRLWRDGVGETRVPMKPEGTRF
TAEIETPPEGCLLWYYFLITGTDGREYRYGAPRDGLGGEGCLYEHEPPSYQITVYRPAPV
PAWYKDALVYQIFPDRFHRGADWRQRVCDAAHPQDWRGPRRVIQEDWDDTPYYTRDSTGA
VTRWPFFGGTLEGVREKLPYLRSLGVTAIYFNPIFRAASNHRYDTADYCAIDPMLGDEAS
FQTLCQEARDMGISVILDGVFSHTGADSVYFDKFGNYGGHGAYLDETSPYRKWYRFKSDG
EPGYECWWGVTDLPNVEETEPSYREFICGKNGVVRRWMAAGAAGWRLDVADELPDSFIEE
VRRAVKAENPNGVLIGEVWEDASRKVSYGEHRRYLMGDELDAAMNYPFREMMLDFIMGRC
NAESLCRRMMSLMENYPPENFFGAFNLIDGHDRIRALTQLGGAPENLSDVQRERYRLPEK
LYQLAVRRLKLLSVLQYASPGVPCVYYGDEAGVQGFEDPYNRGTYPWGREDAGLLQHYRM
LGLIYHEHPVLKNGTYRPFAAGGSVYGFWRENEEERILVVANRSVTDQAAYTAAVPDGTW
ALELLSSQELEIKDGTLALSLSPSSAALVLVRRMPPERVKLSRAAGVICHVSSLPAAGQW
GTLGRHARAFVDFLQRAGMKIWQILPLNPTGLGDSPYLSPAVFAGNPNFIDPDTPVDPAG
FDAFCAENRYWLDDYALYTALKEKFNGAPWQEWPVDARDRTDLSKYRRSLSRRVKTIQMQ
QYRFFAQWDALHTYARERGISIVGDLPIYVAPDSADTWAHRDMFLLDAHGRLRARAGVPP
DYFTPDGQDWGNPLYDWAAMRRDGYRWWIERLRTCALRYDYVRLDHFRSFAAYYAIPAGV
SAREGEWQPGEGLRFFDAVRRELGGIGIIAEDLGVLDVGVYNLL

Enzyme Prediction     

No EC number prediction in MGYG000004802_00453.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	189	519	4.4e-126	0.9936708860759493
GH77	719	943	1.7e-84	0.4493927125506073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14510	PRK14510	0.0	1	944	1	1088	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11338	AmyAc_CMD	0.0	126	556	1	389	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.
PRK14508	PRK14508	8.46e-142	641	937	3	350	4-alpha-glucanotransferase; Provisional
pfam02446	Glyco_hydro_77	1.52e-123	650	944	2	339	4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
PRK10785	PRK10785	1.92e-108	1	620	2	597	maltodextrin glucosidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUC03509.1	8.45e-299	1	944	1	962
QJW48918.1	1.16e-298	3	943	6	1006
QJW48913.1	1.16e-298	3	943	6	1006
SDS02076.1	6.45e-297	5	944	7	975
QOY60572.1	1.34e-296	5	944	5	958

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JF6_A	1.48e-77	75	623	82	575	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1BVZ_A	2.04e-77	75	623	82	575	Alpha-amylaseIi (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1BVZ_B Alpha-amylase Ii (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1JI2_A Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],1JI2_B Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],3A6O_A Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris],3A6O_B Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris]
1JF5_A	5.40e-77	75	623	82	575	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZM_A	5.40e-77	75	623	82	575	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1JIB_A	1.03e-76	75	623	82	575	ChainA, NEOPULLULANASE [Thermoactinomyces vulgaris],1JIB_B Chain B, NEOPULLULANASE [Thermoactinomyces vulgaris],1JL8_A Chain A, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1JL8_B Chain B, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1VB9_A Chain A, alpha-amylase II [Thermoactinomyces vulgaris],1VB9_B Chain B, alpha-amylase II [Thermoactinomyces vulgaris],2D2O_A Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],2D2O_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38939	4.55e-109	5	630	255	918	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950	2.60e-107	5	630	255	919	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P36905	1.05e-102	5	630	258	921	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	6.53e-99	5	630	258	920	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P0A3Q0	8.30e-82	643	943	4	354	4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 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
1.000022	0.000014	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004802_00453.