CAZyme Information: MGYG000004082_01821

Basic Information

• Species: AM51-8 sp900761925
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; AM51-8; AM51-8 sp900761925
• CAZyme ID: MGYG000004082_01821
• CAZy Family: GH151
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
644		73062.14	5.4556

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004082	2757417	MAG	United Kingdom	Europe

• Gene Location: Start: 11498; End: 13432 Strand: -

Full Sequence      

MEDMDAKAYVARLKELGATVTLLNAAGIVANYDTKLDFQPKNPYLRGNTLEEMVEECHRA
GIRVFCRTDFSRIRRDIYEKHPDWAFRTAEGKIVDWEGYVSTCLNGDYQRIYMHEVLREV
LTKIPFDGIFFNMGGFMVTDYDVKYYGACHCENCRRMYRERFGEEMPEQMKPGDPSMLRY
MAFKDQCEREHRERVVKTIREISPQIAIHGVDYIRSESGSDAVRPPWPYSASSNARRGSG
PARMRLADNNAVDFMGFRYRHTSVSPELMELRQWQNLANSGNVSVFIMGDISTHPDRTWY
APTKKVFDFHREHEELYTRMVSDAKVALAVSHGVETNKETQGWVRALTQSHIPFDEIYTD
EMDHPDRLEGKEVLILGDVAVLSDGEAEIIDRFAEKGGTVLVTGKAGMMREDYTPRRGFA
LRCLGVTVTGKPQSLKSSLFEIGKDEEEIFPRSALAHYIAPGDTLMTVRPKEGAKGWLSM
IGEHPYGPPEICYIDDSDRTDAPGIIEMAYGKGKSVYIPFAVGNFYAKEGHKNSLSLMQD
VLFGICGIEEIAPDLSPMVELVLCRTEKEKIIQLINESGCMEKHYMAPLPVYDLSVRIPD
RLADGSRITNCNTLRGGKVSLERDGDDLVLHLNQLCDYEAIVVS

Enzyme Prediction     

No EC number prediction in MGYG000004082_01821.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH151	5	133	6.3e-21	0.9923664122137404

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14871	GHL6	2.19e-38	5	133	1	135	Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
cd03143	A4_beta-galactosidase_middle_domain	1.16e-07	333	421	21	104	A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.
cd14791	GH36	0.002	50	187	67	215	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
cd11335	AmyAc_MTase_N	0.004	34	84	126	182	Alpha amylase catalytic domain found in maltosyltransferase. Maltosyltransferase (MTase), a maltodextrin glycosyltransferase, acts on starch and maltooligosaccharides. It catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or maltooligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose. MTase is a homodimer. The catalytic core domain has the (beta/alpha) 8 barrel fold with the active-site cleft formed at the C-terminal end of the barrel. Substrate binding experiments have led to the location of two distinct maltose-binding sites: one lies in the active-site cleft and the other is located in a pocket adjacent to the active-site cleft. It is a member of the alpha-amylase family, but unlike typical alpha-amylases, MTase does not require calcium for activity and lacks two histidine residues which are predicted to be critical for binding the glucose residue adjacent to the scissile bond in the substrates. The common reaction chemistry of the alpha-amylase family of enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. 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.
pfam14258	DUF4350	0.004	363	402	26	67	Domain of unknown function (DUF4350). This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEN09439.1	3.53e-145	1	625	22	660
QIP16996.1	2.58e-96	4	597	64	669
QHV99491.1	5.63e-94	4	597	64	669
QOT11970.1	4.42e-88	3	641	24	687
QGH35953.1	2.89e-84	3	644	22	665

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000008	0.000030	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004082_01821.