CAZyme Information: MGYG000004288_00531

Basic Information

• Species: Faecalicoccus pleomorphus
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Faecalicoccus; Faecalicoccus pleomorphus
• CAZyme ID: MGYG000004288_00531
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2461		271918.48	4.4016

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004288	2108901	MAG	China	Asia

• Gene Location: Start: 109041; End: 116426 Strand: -

Full Sequence      

MKRHQKAILASVVTASQAATLLNIPVTVMAQEPDVSRTDRVAKNEALQPKSGYTFIGAPV
AMPEVQNNIVTVRYANGEKAKITFLENNLFRFDMEVDGQDGSFKDYADPNDVSHTGRIVQ
QPDSSDEYTKPTPTVGETQDAYSISNDAIILEVSKTDARMTLKRTDGTVVWQEAAPIQYK
TGSTIQSFVKNEGENFYGGGTQNGRFVHTGESIKIENLNNWVSGGVASPNPFYWSTNGYG
VLRNTFKKGEYDFGKTQADVVSTSHTEKRLDAYYFVGDTPISLLQSYFKVTGNPALFPEE
AFYLGHLNCYNRDEWTEGGGTPLETINDSSKYQETNNGGKIKRGGVLETLNGTNETDYKF
SARGVIDQYDKYDMPLGWFLPNDGYGCGYGQDDTNLDNNIANLKSFTDYANSKGVGTGLW
TQSDLTPNPNQPIHLQRDFEKEVYQGGIRTLKTDVAWVGAGYSFGLNGISKAYDIITKAD
TRNRPTIVTLDGWAGTQRYGGIWTGDQTGGNWEYIRFHIPTYIGQSLSGNPNVSSDVDGI
FGGSSLIQTRDIQWKSFTTMMLDMDGWGSYPKKPYVFGEDTTSINRMYLKLRSQLMPYIY
STAYSSANLGEDGEKGKPQVRAMFLEFPEDANAYGKNVQYQFMLGKNLLVAPVYQNTAAD
GQGNDIRNGIYLPDSNQVWIDYFTGKQYQGGSTLNNFDAPIWKLPLFVKNGAILPMTEAH
NNGFAKSETNTKGVDKSKRVVEFYPAGETDYTLYEDAGNTVDNTNTSEVNYGSAVTTHFT
SKVTGEKAVLKAEASQGSYVGYDANKETQFVVNVSEKPSSIQATVGANDANLTEVHSQKE
FDEATGNVYYYNESPDLNRFATPESDFASVKITTTPKLYVKFAKTDVSANAIELSLEGFK
NDGDLDKNVLNKDLKAPANVRAPEESITPDTIHLQWDAVENATSYEVEADGVIQTGFTEP
EFDHTDLAYHSKHTYRVRARNKDGYSQWSETLEVQSAQDPYRNVPKDIQVTWEYGDAWGK
LANILDFDTGTMFHSTKAVQDGQAMIYDLKKIYDLDRIEYTPRLDNKGNGTVQKMDVYTS
LDGTNWTLAYDSSKNPEWTYSKDMSDPDTKTMDMTGQKARYIKYVVKKSVGGFFSAAELQ
PYKVDGTEGYIVGDTNNDGTVDDNDVVQIDNYVGLEEGDPTWDQVKRSDWNDNKYFDAAD
IAQTTSRLGKGIAKTGGDPKGSLVIEPDKAHYSAGEKVTLSIQGISMENVYALGGKIPYN
SEDLQFVSVSSDIATGDQREFVFDRIAYQNQEHPDKNRNVNFAYSNLGDQPMLSGTNRLA
TVTFTAKKDLDIKASDFNLSDFMFVSNNMNYIDPLKPSEDLPEPETESKIQVLSVEGQDE
SVLQPGMGVDKLIDGAWGSDANRFEFKWGNDEASVPARLPYWIRFNFGEIKKVSDVIIHV
RVDGNRINGGALKDFDLYRIKNGVEQKIGSYVIDKTEDENAYVIHFADPIQAEGFKLNAK
TSQAGQIFKLNIDEVEFRQNAQTPIEDITLDEANPTTLNVGDLKGFKASVAPDTATNKLI
KIESSDPEVLEVIRTTRDDHYEYTLHALKPGTVTLTITSNGQTVQGEAITRQVEITVNEA
VTSKEELESKIEEANAILANENLYTPSSLDVLKNALKLAQNVEDKKDATQTEVNAQVVQL
YKAIQQLEYRGSNTAQPDSENPIVVDPANVTATTSASEGPVENAFDGDQATYWHSGWEQG
TEKLPQSVTVDLADEYDVEQVNYLPRQGSRNGDIIKYQIETSEDGETFKPVVVGTIENDG
SSIVERTQPHKIKFDKTKARYVRITALESLGNQNNLYASAAEFSIFGALHSDAIPATSIE
LDKTELKLDAGNTETVTATILPEDTTDTITWESSDPSIASVEALGRRRVRRDANASSNTS
TVTVTALKAGTVTITAKANDTVSKTLTVTVENPKQEQLAELIEQAKGVKYENAALQDYLT
SEIEKATQALDQDQDTLQNAYYALAGALSEIEEIQKDIDQLNSFSDIDDSRYVPNEQYQM
FKEQLQLAQNLLSDPVQNKELIKTHVDALKKAFAQLEELDREKLSNAIQEAEKVNLQDCV
EDDALSAFKTALENAKAANPQSNEEIDTLVNTLLEAQAGLHFKDENLATDDQKESIQHAL
DVLKNLDLELYSEQDGKTIKAAISDGEDALANKDLTKEEASKVIDDLAKALSLEPKEVTP
EEEPASSSQKEVIAKALDILKGLDLNLYDTKAQDVIQETIEEAQKAADNDQLTKEEAANV
LEHLANALSIQPKEDTPKDEKATSTQKEVIEKALDILKDLDLNKYEAKDADLIKEAIEAT
QKALENKELTYAEATDTIEKIAQALLVTPKETEQPDPSDNENPNTNTPDHGQNNSTDTGS
NGSNTVIVNPTDSSKSKGNTKTGVHSFVGLFAALATSAAATAGTVTLLKNKKIRIRRKGK
K

Enzyme Prediction     

No EC number prediction in MGYG000004288_00531.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	467	714	2.6e-58	0.5339578454332553
CBM32	1712	1844	1.7e-26	0.9112903225806451
CBM32	1016	1139	1.4e-16	0.8709677419354839

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06596	GH31_CPE1046	1.85e-171	290	685	1	334	Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
COG1501	YicI	2.17e-68	137	786	99	735	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055	Glyco_hydro_31	1.04e-60	273	714	1	442	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06603	GH31_GANC_GANAB_alpha	1.66e-39	484	716	213	428	neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
cd06589	GH31	9.52e-38	351	589	15	265	glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK23937.1	0.0	2	2228	4	2209
QJA02122.1	0.0	1	2215	1	2224
BCT46261.1	0.0	56	2076	43	2115
QIK85989.1	0.0	50	2289	41	2257
QBJ76643.1	0.0	51	2211	52	2204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6M76_A	6.55e-266	54	1002	35	963	GH31alpha-N-acetylgalactosaminidase from Enterococcus faecalis [Enterococcus faecalis ATCC 10100],6M77_A GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine [Enterococcus faecalis ATCC 10100]
7F7R_A	3.48e-265	54	1002	35	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7Q_A	9.47e-265	54	1002	35	963	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
4LKS_A	1.07e-30	1712	1847	31	166	Structureof CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with galactose [Clostridium perfringens ATCC 13124],4LKS_C Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with galactose [Clostridium perfringens ATCC 13124],4LQR_A Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens ATCC 13124],4P5Y_A Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with N-acetylgalactosamine [Clostridium perfringens ATCC 13124]
6JR8_A	1.51e-30	130	865	90	828	Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F234	4.34e-31	112	760	69	713	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999	2.92e-29	143	762	56	662	Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q9FN05	2.40e-27	270	762	332	822	Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
B9F676	9.70e-25	270	762	330	820	Probable glucan 1,3-alpha-glucosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os03g0216600 PE=3 SV=1
Q9BE70	1.25e-24	469	716	405	636	Neutral alpha-glucosidase C (Fragment) OS=Macaca fascicularis OX=9541 GN=GANC PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000670	0.998413	0.000259	0.000283	0.000198	0.000167

TMHMM  Annotations     

start	end
2426	2448