CAZyme Information: MGYG000003463_00094

Basic Information

• Species: Succinivibrio sp900767695
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; Succinivibrio; Succinivibrio sp900767695
• CAZyme ID: MGYG000003463_00094
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
565	MGYG000003463_10|CGC1	61253.37	5.376

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003463	2187524	MAG	Fiji	Oceania

• Gene Location: Start: 1461; End: 3158 Strand: +

Full Sequence      

MSAILKGDLKARPDGVAQGGSARAEIFTIVPSRKVPAPASEWIAGDGLGPLPSSRIYAEG
FQMLSVQEGTVENRIFQGRCPDDALPYRHNPRQGSVREAYGVVAFENAAGGFTLLGFTTC
NSAQGRFLIDASSCSITLSLMVSDGQGRIADDALKGEGFCQIAAPALEEALALYASLAGS
GRGAGSKPPMGWCSWYSRYEKVTEDYVKDSLEVLKSFPELECVLIDDGYQEHMGDWLSFS
GKFPRGLDGICSDIHSASRIPGIWLAPMIASGASRLAHEHPEWLARGPNGEIANASDLTY
GGWRDLPWHTLDYGKAEVRQWMRDTVHELRHKYGIRLFKLDSLYWGAYEGLSFSTPMTGV
MNLRLALKAIRDGAGDDSFILGCNAPLWACNGLVDGMRVSDDAARSATVFAANSRACALR
SWMNRKLWINDPDCLLLCDLGDQRASEGEYAFHLGSILASDGIFMSGDDLTAMSKERLDL
LHRASAVAAAPRQVRWSGDFSRAEILLENTGRAMTVAINRGRESMDFDLPSGTDFMSLRK
IGGTISIPPLCGVVSEHSAKGAIEQ

Enzyme Prediction     

No EC number prediction in MGYG000003463_00094.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH36	167	504	3.8e-52	0.48691860465116277

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14791	GH36	1.95e-62	187	484	1	293	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.
COG3345	GalA	1.01e-46	50	453	147	582	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14790	GH_D	3.46e-12	188	468	1	235	Glycoside hydrolases, clan D. This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families 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. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
pfam02065	Melibiase	9.85e-10	199	341	48	190	Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
cd11313	AmyAc_arch_bac_AmyA	2.28e-08	274	341	105	161	Alpha amylase catalytic domain found in archaeal and 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, bacteroidetes, and proteobacteria. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYO71082.1	3.99e-104	54	474	57	480
AEA78704.1	1.11e-103	54	481	57	490
AYC05146.1	1.57e-103	54	481	57	490
QHQ90134.1	2.21e-103	54	481	57	490
SPM18452.1	2.21e-103	54	481	57	490

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M0X_A	2.17e-44	174	481	190	504	Structureof apo structure of GH36 alpha-galactosidase from Thermotoga maritima [Thermotoga maritima],5M12_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with intact cyclopropyl-carbasugar. [Thermotoga maritima],5M16_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with a hydrolysed cyclopropyl carbasugar. [Thermotoga maritima],5M1I_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar. [Thermotoga maritima],6GVD_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8],6GWG_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose covalently linked to the nucleophile [Thermotoga maritima MSB8],6GX8_A Alpha-galactosidase from Thermotoga maritima in complex with hydrolysed cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8]
6GTA_A	2.70e-43	174	481	190	504	Alpha-galactosidasemutant D378A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 3,5 difluorophenyl leaving group [Thermotoga maritima MSB8],6GWF_A Alpha-galactosidase mutant D387A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 2,4-dinitro leaving group [Thermotoga maritima MSB8]
1ZY9_A	2.11e-42	174	481	179	493	Crystalstructure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution [Thermotoga maritima]
6LCJ_A	4.99e-31	168	432	141	375	TtGalA,alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_B TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_C TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_D TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_E TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_F TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCK_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_B TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCL_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_E TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8]
4FNR_A	5.08e-09	194	341	335	478	Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
G4FEF4	8.55e-44	174	481	167	481	Alpha-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=galA PE=1 SV=1
Q9ALJ4	2.78e-08	194	341	335	478	Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA 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
1.000064	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003463_00094.