CAZyme Information: MGYG000001732_01028

Basic Information

• Species: HGM11530 sp900751685
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11530; HGM11530 sp900751685
• CAZyme ID: MGYG000001732_01028
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1777	MGYG000001732_26|CGC1	198718.56	4.4133

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001732	3073889	MAG	Sweden	Europe

• Gene Location: Start: 3335; End: 8668 Strand: +

Full Sequence      

MSFNRKFKKILITFLTLSILAGTQIQLPLSASAGTENTGAWGDLGNGYYNNPVLPADYSD
PDIIRVGSDYFLITSTFVQSPGITVLHSVDLINWEIIGGAVKDITQINPKHDYTVMNTYG
RGIWAPCISYNPSNQRFYIHFGDPDFGMYMVYTDDIYGEWSDVQEVVLPNGTGFGSGWDD
CGILWDEDGQGYFAATNFADGYKDYIFKISQDGYHLEDTGALVHQSDDGLYPDGERSPEA
LKMFKKDGMYYFFHNGINGGKRKAFIMRSTSIYGKLKNGDAGTFESPGKYEHIPYPIVEG
TREPNQGNLIDIQADNGSTKWFFWTHQGSTDMDGRPNSLIPVTWNSDGWPVAGTEDIHSA
GKMVWENIEKPIKDSEIKRPQTSDEFSLEKMGVQWMWNYQPRNEFWTLSERPGFLRLKAF
KPLKTDTLNKAGNSLIQRMYRTDGNVVTTKMDVSSMADGQFAGLLYMMGGTAAGIGVYRE
NGANYIKFKGNTDITGEVIPDSISNVYFKAEWENDMLTRSYYSIDGITYRQFGEEYQIVK
SNYRGGHIGFFCYNDLSESGSVDFDYLHYEMDVNEKAPVIMGVDDGGMYDLPVTLRYSRG
NATLNGKPIQSGTRVSGEGTYTIRVEDRGIAAEKTFTLTEDAVEPGIRVPFSMNVGGGKT
EGFTKDQQYRSGYWGALNGTIYEQDGEGIYKTARKAETLSFQFDGIPFGYYKVKLHFIEC
DVSSVGQRVFDVVLQNQLKDQVDVFKEAGEGVPLVKEYDGIEIDGSLTMELEGVSGEALL
CGIELVAGNEPIKTPRPQLEIDEVLLGKQEGNNILPETFDNYIISPDEWDGILTDMVITE
STAVTPNCGVAPVSGKAISFQKTAEAMRKFKEPIKNGQVIFSGDYAQATRIKSMSLVDSS
GKQVVKIGYDLDSTSATDNNILFINGQSVLKTYMLTSRTEQMSVKDMVIDVDEGTISYTV
SYSKREGKENKWVTEKNTVENVRIKDIAGLLISGEGASYAGFADNIVLYSKVPGQEPQPT
LTPTPEPSKDVNVLIDPLKKGVGINRDMIGLFFEDINFAADGGLYAEMIKNRSFEFYGAD
GSANPEGADLSMESWTVSKTKGCTAEYQVKDELPLHSNNTKYLTVDISVPGSGVELQNTG
FGGIDLKKGEAYKFSIFARGADYKGEYTVSVVKDGKTYAQAVSNEPFTNEWKKQELLFTA
DDNVDNGMFVLTLKGTGKIDLDMISLFPHNTYQNRENGLRADLVEVLKDINPGFLRFPGG
CIVEGYDLENRYNWKDTVGPVEERKINWSRWQNTIRGHYFSDYFQSNGLGFYEYFLLCED
LGCEPVPVVNCGMSCQYQSPKEVVPLDQMNGYVQDALDLIEFANGAIDTPWGALRASMGH
PEPFDLKYVGIGNEQWGPDYFDRYEIFQQAFAEKYPEIKLITTSGPDPDGSKFDQAWNLF
KTKDQTYAYAVDEHYYKTPEWFFDNVDRYDNYDRNGLKVFAGEFAAHDKSTQPRSNSIYT
ALAEAAFMTGLEKNADIVQMASYAPLFAKEDCWQWTPDMIWFNNSSICLTPNYYVQKMYS
NNMGDYTVSNEITGSEPDIASTLYTTVSYDEVNDDIIIKAVNSASKKIKATFDINSSVKV
SNIGKISLLAAEDPEAVNTMENPDLIKEVDFMYDGFANKFTYELEENSFTIFRIPVDQGK
DYNVIAKLKADDFSKGSKAAAEVSIRNNTGAEKTATLYLAMYSENGELLQVKRVDKKLEQ
MEAVDTSVEAEMPENTFKVALFVWEGMMPVHMESKTA

Enzyme Prediction     

EC	3.2.1.55

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	1213	1759	1.9e-118	0.8174603174603174
GH43	50	350	8e-62	0.996309963099631
CBM57	653	783	6.1e-17	0.9727891156462585

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09001	GH43_FsAxh1-like	1.36e-77	49	353	2	270	Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
COG3534	AbfA	3.92e-57	1221	1677	33	501	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964	Alpha-L-AF_C	3.30e-45	1482	1668	1	192	Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
COG3507	XynB2	1.27e-44	43	570	15	547	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08989	GH43_XYL-like	1.86e-44	51	344	1	271	Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYR23081.1	1.96e-192	39	570	19	550
AMP97575.1	1.75e-187	1029	1676	22	658
AHW58581.1	4.92e-183	1032	1676	22	644
QIA07679.1	1.87e-182	1032	1678	22	646
QDH78970.1	1.61e-179	1039	1678	35	659

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZPS_AAA	6.44e-81	1048	1677	17	627	ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]
6MLY_A	3.12e-41	51	575	23	516	ChainA, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_B Chain B, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_C Chain C, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_D Chain D, Bifunctional GH43-CE protein [Bacteroides eggerthii]
6MS3_A	1.36e-32	45	465	26	419	Crystalstructure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6MS3_B Crystal structure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS2_A	1.82e-32	45	465	26	419	Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
1YRZ_A	5.31e-31	51	465	7	403	ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P82593	4.62e-128	1019	1592	23	577	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
Q9SG80	9.78e-89	1041	1680	52	661	Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1
Q8VZR2	4.05e-88	1044	1697	54	672	Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1
Q8NK90	4.64e-70	1048	1664	42	617	Alpha-L-arabinofuranosidase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=abfA PE=1 SV=2
U6A629	4.95e-70	1033	1545	18	505	Alpha-L-arabinofuranosidase A OS=Penicillium canescens OX=5083 GN=abfA PE=1 SV=1

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
0.000623	0.997166	0.001552	0.000250	0.000199	0.000180

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001732_01028.