CAZyme Information: MGYG000000673_00365

Basic Information

• Species: CAG-873 sp004552485
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp004552485
• CAZyme ID: MGYG000000673_00365
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1141	MGYG000000673_4|CGC3	124872.74	4.9706

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000673	2306526	MAG	Kazakhstan	Asia

• Gene Location: Start: 73925; End: 77350 Strand: -

Full Sequence      

MKQNLTKLFAFLLCLIGATVPGMQALEIDHFANPTINSNAPDPSVMRAPDGMFYLSSGSA
IWKSPNLTDWTWARWAFEGEGTQEPGDGHLGIKGDVWASDINYINGKYVMYFAISVWGGE
WDCGICVATSDKPEGPYTWQKKLFNSREIGVQNSIDPFYIEDNGKKYLFWGSFSGIFGVE
LSDDGLSVVGEKKQIAGKGFPDGIEATCIYKRNGYYYLIGSRGSCCEGLNSTYNLCVARA
TSLFGTYTNKWGSHAMYNYYEPLLQSNDSVKGPGHCSEMIEDDHGQTWLYYHGYESSHPD
DGRLGYLGKVDWVDDWPVMGTYPATGGVKPYIRRFESNDIRERWSYCDARGTRHKPGFDA
GKVTSIAYRDGKLYCVYDHSSIKVLDAQSGQYLRDLPAGDVVRGGERVLSSVREYQGGII
ACNMAVPGQELRIYYWSGDFAAPRLLMSTTDLKNCSRLGENMDVGSGWGDTWIAFANDNG
SESALVEFHDNNGTWTSNRERITSNGSDNCRIGDNARAWMCGGTWWFGGNNMGAGYFGRG
NGTINPNLWVPGLGNWGSEHKELFYGLHKYALNFVFDGKSNGRIRFLCDDSGNYNSTSSV
GTWPASGLGGQENTTGECELCVNSDGKSYIEIWACSANQGLMYLTHNNPPEISTEPSVTA
NPARLDLNAHINDIAEGKITFSGRNLDNKELYLTLRDDNACVFTLSQNVLQPATGNNTVT
VSYNTSKAGSHNASIEVRVDDVVRCTVPVSGKCTVYTPSYAIDKMEELWSYSVNKGNLGQ
TGWFDNNGITRDMCAVGTNLYVLNYNSSSITILDGKTGQTKGNLSAAGISGGKIALAAIK
SLGDKVIGCNMAEANDELRVYIWDNDNATPRLLFSTTDHGGVEVGRSMATYGDMNNGIIA
LGYGQAPKNQNIQKVVYFTVENGNVNTTANVRDLSANYTGGNSSNQHVMFDSDMSFWLSN
KDTYPMHFGNDGTLIEKVESGLDGQRFGVGNDLFTYAGHKYLAITTTLGSSSQAAWGNAT
LELLDISNGLGGATHRGRYPYDGLGPDNWGTVGNTAICHSISDLGNELYLWIMVPKQGIA
AYYNSDGYRPNGAENISVDDADADAPAVYYNLQGVRMNAENLTPGLYIRRQGSVTTKVLV
K

Enzyme Prediction     

No EC number prediction in MGYG000000673_00365.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	31	317	2.4e-79	0.9966555183946488

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	1.90e-103	33	312	1	291	Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
cd08998	GH43_Arb43a-like	3.98e-54	42	312	3	277	Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
cd08999	GH43_ABN-like	5.17e-52	33	318	1	284	Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
cd08988	GH43_ABN	2.62e-48	41	295	1	261	Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
pfam04616	Glyco_hydro_43	2.82e-47	31	317	1	281	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. 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
SCM57950.1	2.07e-96	31	341	39	345
CEA16128.1	1.00e-94	27	330	30	331
BBD45555.1	1.11e-94	3	330	8	333
QCQ48881.1	3.91e-92	31	333	23	323
QRM69386.1	3.91e-92	31	333	23	323

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3D60_A	4.88e-24	45	319	47	312	ChainA, Intracellular arabinanase [Geobacillus stearothermophilus]
3CU9_A	4.88e-24	45	319	47	312	Highresolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus [Geobacillus stearothermophilus]
3D5Y_A	2.97e-23	45	319	47	312	ChainA, Intracellular arabinanase [Geobacillus stearothermophilus],3D5Z_A Chain A, Intracellular arabinanase [Geobacillus stearothermophilus]
6F1G_A	3.02e-23	45	319	48	313	Thestructure of AbnB-E201A, an intracellular 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus]
1WL7_A	5.22e-23	45	319	47	312	Structureof the thermostable arabinanase [Geobacillus thermodenitrificans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B3EYM8	2.72e-23	45	319	48	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
Q93HT9	2.91e-22	45	319	48	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
P94522	1.56e-21	97	317	104	321	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
A5AAG2	1.03e-18	40	319	28	317	Probable arabinan endo-1,5-alpha-L-arabinosidase C OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=abnC PE=3 SV=1
A2QT85	1.08e-18	18	319	8	321	Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=abnA PE=3 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
0.000279	0.999067	0.000170	0.000164	0.000144	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000673_00365.