CAZyme Information: MGYG000000544_00785

Basic Information

• Species: Zag1 sp900769355
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1; Zag1 sp900769355
• CAZyme ID: MGYG000000544_00785
• CAZy Family: GH57
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
833	MGYG000000544_35|CGC1	96854.22	5.88

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000544	1985493	MAG	Fiji	Oceania

• Gene Location: Start: 1333; End: 3834 Strand: -

Full Sequence      

MSDKKNEVFLTIHGHFYQPPRENPWLEAIELQDSALPFHDWNERICKECYNPNSVSKIVD
SRNRILDVVNNYEHMSFNFGPTLLSWLEHFAPLTYERIIKADIESVAEHSGHGNAMAQVY
NHIIMPLANENDKRTQILWGIRDFVYRFGRKPEGMWLAETAVDDETLRLLEENGIKFTVL
SPYQALKFRKKGDKDWQDVSWGNIDPARSYRYYIKSAPGKYIDLFFYDGAISRSVAFDEL
LKDGNKFIKRLKEGISDCRDYPQLVNIATDGESYGHHTKFGDMALSYVLKIKAKDEGFTI
TNYAEYLDKYRSDCEVDIKQASSWSCFHGVGRWKEDCGCSTGGHPGWNQKWRKPLRNALD
YLRDELVAVFEEEGQKYFDDCWKVRNEYINVILDRSEMNVKKFQQDNFKPDLSDEDKVRA
MELLEIQRQTLLMYTSCGWFFSEISGIETVQIMKYAARAMQLAAKFTDKNLEENFTNILA
EAKSNIADFGTGKDIFERFVKPSIITPKQIACLWALSSLYEDFEDEEDVYCYTINRLAYK
KAQKGSATFVVGHIEVQSRITLQKSNLVLALMQYAGGDFHCAIKEYSDDAEYNKMKNDLI
KTFTAYSLTEIIRALDEYFGKEYFTLKDIFIEERRKILQILLKGKLEKFSQTYQDMYDEG
KGSIYHLQGLGLKIPDEFKISASYALSHKFNDIVVHSTGFMDEEIIQQAVDINFEAKKID
IQLDKTPSNKVFGKKILQNINRLVHSFEIQQADVVLEIFENIRKLELQVDIAEAQNTYFA
KIYHRIGDIIESDAFKAKKNSIKRFVEMLLEIGENLNINTEFYRKKLDKALLK

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH57	56	326	1.6e-56	0.6971279373368147

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10797	GH57N_APU_like_1	0.0	9	339	1	327	N-terminal putative catalytic domain of mainly uncharacterized prokaryotic proteins similar to archaeal thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). This subfamily of mainly uncharacterized bacterial proteins, shows high sequence homology to GH57 archaeal thermoactive amylopullulanases (APU, E.C 3.2.1.1/41). Thermoactive APUs are type II pullulanases with both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity.
pfam12055	DUF3536	3.27e-134	347	630	1	284	Domain of unknown function (DUF3536). This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea. This domain is typically between 274 to 285 amino acids in length. This domain is found associated with pfam03065.
cd01022	GH57N_like	4.77e-50	12	334	4	312	N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
cd10796	GH57N_APU	1.38e-17	74	324	47	303	N-terminal catalytic domain of thermoactive amylopullulanases; glycoside hydrolase family 57 (GH57). Pullulanases (EC 3.2.1.41) are capable of hydrolyzing the alpha-1,6 glucosidic bonds of pullulan, producing maltotriose. Amylopullulanases (APU, E.C 3.2.1.1/41) are type II pullulanases which can also degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch, producing oligosaccharides. This subfamily includes GH57 archaeal thermoactive APUs, which show both pullulanolytic and amylolytic activities. They have an acid pH optimum and the presence of Ca2+ might increase their activity, thermostability, and substrate affinity. Besides GH57 thermoactive APUs, all mesophilic and some thermoactive APUs belong to glycoside hydrolase family 13 with catalytic features distinct from GH57. This subfamily also includes many uncharacterized proteins found in bacteria and archaea.
cd10793	GH57N_TLGT_like	3.49e-11	40	312	16	259	N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57). 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR38251.1	0.0	1	832	1	832
BCS53554.1	2.03e-242	5	819	4	811
ACM19576.1	3.43e-238	7	819	2	805
AFM25144.1	8.81e-235	7	818	2	805
AEG16364.1	4.14e-233	7	789	2	779

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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000544_00785.