CAZyme Information: MGYG000000315_01054

Basic Information

• Species: UMGS951 sp900547585
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; UMGS951; UMGS951 sp900547585
• CAZyme ID: MGYG000000315_01054
• CAZy Family: GH57
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
747		88036.01	5.0179

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000315	1984931	MAG	Sweden	Europe

• Gene Location: Start: 9105; End: 11348 Strand: +

Full Sequence      

MKKKLSIAFIWHMHQPAYRTGPEEIYLMPWVRLHAVKDYLDMLVMMDKFPGLKLNFNLVP
VLVDAIYNYGFRGAHDIYSKLTITPVEELGKEEKTFILNHFFDANYQNMVFHHAAYKKLY
DKRFSRDDIGIEDFTPQEYSDIMAWFNLSWIDPHWRVYPKINELSEKTEGNFTLQDRIDL
IEQQRRILRRIIPTYKKYQDEGKIEISTSPYYHPILPLLADMEDAQRSNTNITPPKLESD
LYEDAVFQVKSALDMFERTFGKRPAGIWPSEHCVSEKTMGILQDLGVKWTISDEGVLEQS
LKREFSRDFRGYLENPYDLCHSYEYKNGKDPINIIFRDAVFPNLIGFEYPNHDPVKAAND
LYDRIKSIQYKLENSPDKNHLLTIAMDGENCWENYPADGTEFLETLYGLINNDEGLETVT
VSGYLEKIKKPKSIKTIHPGSWINRDFMLWVGEPTKNLAWEYLDKTRQDLKEFEKEITDQ
QLLFELWREIYMAEGSDWFWWYGEPNDSGQDNLFDLLFRSHLKNVYKLAGKPEPDYLDIP
LHDSVYVGSRYPRGEVENFELTGSNNDNWANAGCIEIPTTPTMQEKRFFNKIFFEHDKDN
LYLRFDINSYVIDEELGFKDFHQIYIYFKNTSTANPPVANIRTISKTENVMPLLKERFTD
EVKMTFFRKLDFPAQFAKANYDNLWILQIKHGIEAVYKDFVEIKIPFNDLNIQKGETAEF
FIVKAELGLVDKFYPRDTLLSVTRPVD

Enzyme Prediction     

EC	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH57	8	472	3.6e-83	0.8302872062663186

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10796	GH57N_APU	4.11e-106	7	452	1	313	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.
COG1449	COG1449	1.47e-90	3	543	2	502	Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism].
pfam03065	Glyco_hydro_57	1.99e-39	8	436	1	292	Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
cd01022	GH57N_like	2.83e-28	173	452	62	313	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.
cd10792	GH57N_AmyC_like	9.73e-14	163	442	85	401	N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR38601.1	4.57e-278	3	744	6	740
ABD00907.1	4.36e-156	1	745	1	735
BAW95182.1	1.18e-154	1	745	1	742
BAZ37802.1	2.50e-154	1	745	1	744
BAZ45837.1	1.57e-153	1	745	1	748

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7E1Y_A	1.87e-09	172	500	198	507	ChainA, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_B Chain B, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_C Chain C, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_D Chain D, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_E Chain E, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_F Chain F, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_G Chain G, Glycoside hydrolase, family 57 [Staphylothermus marinus F1],7E1Y_H Chain H, Glycoside hydrolase, family 57 [Staphylothermus marinus F1]

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
1.000062	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000315_01054.