CAZyme Information: MGYG000000217_01158

Basic Information

• Species: Acetatifactor sp900066565
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900066565
• CAZyme ID: MGYG000000217_01158
• CAZy Family: CBM34
• CAZyme Description: Cyclomaltodextrinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
175		21343.64	5.6297

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000217	3653823	Isolate	China	Asia

• Gene Location: Start: 103907; End: 104434 Strand: -

Full Sequence      

MEYSAIFHDMDKRFCYAIDKDLFVIRVQVKKDDIKEIMLHYEDKYIPLEWRDTRKTIPMK
KVATSQFHDYYEAQLQMHLICLRYYFEFTDMQGEKVYYGNYEFSRECITNRDRMFDCPQN
LREEEMFEVPEWAANKVVYQIFPSRFAASQPIDKELCIKHPLHLRIICMAISEEL

Enzyme Prediction     

No EC number prediction in MGYG000000217_01158.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM34	6	119	6.7e-30	0.9416666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02857	E_set_CDase_PDE_N	3.85e-25	6	118	1	108	N-terminal Early set domain associated with the catalytic domain of cyclomaltodextrinase and pullulan-degrading enzymes. E or "early" set domains are associated with the catalytic domain of the cyclomaltodextrinase (CDase) and pullulan-degrading enzymes at the N-terminal end. Members of this subgroup include CDase, maltogenic amylase, and neopullulanase, all of which are capable of hydrolyzing all or two of the following three types of substrates: 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. The N-terminal domain of the CDase and pullulan-degrading enzymes may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
pfam02903	Alpha-amylase_N	1.01e-24	1	106	1	104	Alpha amylase, N-terminal ig-like domain.
PRK10785	PRK10785	4.79e-06	130	163	116	146	maltodextrin glucosidase; Provisional
cd09563	SAM_liprin-beta1,2_repeat1	0.007	147	171	38	62	SAM domain of liprin-beta1,2 proteins repeat 1. SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM02562.1	2.30e-108	1	162	1	162
CBK89717.1	5.96e-103	1	162	1	162
CBK93414.1	5.96e-103	1	162	1	162
ACR77021.1	2.38e-102	1	162	1	162
CBL13402.1	5.33e-99	1	162	5	166

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SMA_A	1.54e-18	1	151	1	150	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1GVI_A	1.54e-18	1	151	1	150	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
1EA9_C	2.84e-18	4	147	4	142	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
1J0H_A	2.46e-17	1	151	1	150	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1J0J_A	2.46e-17	1	151	1	150	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A7U9P668	8.41e-18	1	151	1	150	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
Q08341	1.56e-17	4	151	5	149	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
Q59226	9.74e-17	4	147	4	142	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P38940	1.34e-16	1	151	1	150	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08751	2.49e-16	4	151	4	146	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII 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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000217_01158.