CAZyme Information: MGYG000000408_00094

Basic Information

• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae
• CAZyme ID: MGYG000000408_00094
• CAZy Family: GH57
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
746	MGYG000000408_1|CGC3	88266.67	5.1384

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000408	1810289	MAG	Sweden	Europe

• Gene Location: Start: 98841; End: 101081 Strand: -

Full Sequence      

MQKKLSIAILWHMHQPLYKSNDDNIYLMPWVRLHAVKDYLDMLKIMDNFPKLKLNFNLVP
VLLDALIDYENENCHDIHSKLTVTPIEDLNYDDKIFILNHFFDANYQNMILNHKYYSELY
EKRISKDEINIDDFTDQEYSDIMTWFNLSWTDPYWINIFPELKYLFDKERNFTFEDRKLL
ISIHRKIIKNIIPEYKKYQDQNRIEISTSPYYHPIIPLLLDMNIAKKSATRYPLPQGKFD
MYEDGYTQTVMALDRLEGLFGKRPKGIWPSEHCISEKTAECFAKAGVKWSLSDEGILSSS
LKKEFIRDHRGCILDPYDLTQIYEYNTTSGSINFVFRNAVIPNFISFEYPLHDLQTSLND
IQERIKILQNKIETSPSENHLLLIAMDGENSWEGFEKDGADFLNGLYKIINDDDSLESVL
LSDYIENNDKKTLKKIYPGSWINRNFQIWVAEPTKNLAWEYLNKTRNDLVEFQKDTSIPK
EKLLQAWKEIYIDEGSDWFWWYGEPNDSGQDHIFDYLFREHLINVYKILEKPYPDYLNIP
LISFIGKPSKVPKKLISPQIDGKNNLLDGWTDAGYIEIPSRPIMEDKKIINKIFFGFDKK
NIYFRFDLNTYIKDENDYFKDFYQIFIYFKNQSNKNKNLSSIRTVNRSDTLFPIIKDKYS
NEIKISFTGKKGLAPQLSYATKDNLWVYKLSNNIKFAYDEIAELSISFDELGVKIGEKVD
FFILTSVNDITEEVFPQDVVLSIERL

Enzyme Prediction     

No EC number prediction in MGYG000000408_00094.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH57	8	467	1.4e-70	0.8198433420365535

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10796	GH57N_APU	1.53e-87	7	450	1	312	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	7.48e-74	3	634	2	581	Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism].
pfam03065	Glyco_hydro_57	1.78e-30	8	426	1	282	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	5.40e-22	175	451	64	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.
cd10797	GH57N_APU_like_1	3.75e-07	210	426	110	296	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR38601.1	1.43e-266	3	746	6	741
ACI20270.1	8.54e-152	5	617	3	606
ANV86099.1	8.32e-148	1	613	1	619
ANV89272.1	8.32e-148	1	613	1	619
ACA98130.1	8.32e-148	1	613	1	619

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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000408_00094.