CAZyme Information: MGYG000004529_00533

Basic Information

• Species: UMGS1477 sp900761525
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; UMGS1477; UMGS1477 sp900761525
• CAZyme ID: MGYG000004529_00533
• CAZy Family: GH57
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
759	MGYG000004529_13|CGC1	89184.73	4.7348

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004529	1929683	MAG	Israel	Asia

• Gene Location: Start: 19104; End: 21383 Strand: +

Full Sequence      

MHQPLYKDINENGIYYMPWVRLHAVKDYLDMLLIADKYDKIKLNFNFVPVLLDALIDYTD
NNTHDIHSKLTVTDVGELTFDDKVYILNNFFDANYRHMIKHHAYYETLYKKRLTIEDTNV
ECFSDQEYSDIMALFNISWMDPYWKEVYPEIKMLTEKEKNYTLEDRQRIIEIQRDIIRNI
IPQYKAHQQKGKIELQTSPYYHPILPLLLNMKDAKASATRYPLPKGDFNMKDDAYKQTVN
ALDRMEELFGKRPKGIWPSEHCISKDTLDCLIKAGVSWTLSDEGVLSSSIKKEFIRDHRG
SIIDPYDMTQVYNYKNTKGDINLVFRNSVIPNLISFEYPLHDTKDSLNDIYDRIKTIQGK
LENSPSDNHLLLIAMDGENSWESFDNDGIDFLNGLYSKINEDNSLDCVLLSDYIENNKKT
QLNKITPGSWINHNFQLWVAEPTKNLAWEYLNNTCNDLYKFERQGVFSQAQLKQAREELQ
IAQGSDWFWWYGEPNDSGQDNIFDYLFRQHLMNVYRALYMDYPEYLNTSLISSIGKPSRN
QKSLITPNIYDTNDENVWQNAGFIEIPSRPIMEDKRILNKIFFGCDNDKMYFKFDLNNFL
LSECGNNFSLSNQFKIFIYYKKEAELLTDNVLNQSSVRTLISHDDIYPTLKEKYTNEVQI
TFKDKNCVSIQLSQALSNNLWAYSLSNNVEYNFDNNLYISIPFDDLNITKGEKVEFCFIT
SICDKTEEVCPQDLLLSLIRPDSNKFIIDELNYDESLSV

Enzyme Prediction     

No EC number prediction in MGYG000004529_00533.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH57	1	456	1.3e-72	0.8067885117493473

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10796	GH57N_APU	9.59e-88	1	439	7	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	3.25e-58	1	527	12	497	Alpha-amylase/alpha-mannosidase, GH57 family [Carbohydrate transport and metabolism].
pfam03065	Glyco_hydro_57	5.20e-30	1	425	6	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	6.47e-18	162	440	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	6.54e-10	154	430	86	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	3.10e-251	1	740	16	740
AFZ48786.1	9.27e-131	2	741	14	750
BAQ62420.1	2.65e-130	2	741	14	751
QDZ40903.1	1.81e-129	2	709	14	702
AFZ54829.1	1.94e-129	2	596	14	621

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 MGYG000004529_00533.