CAZyme Information: MGYG000000250_02533

Basic Information

• Species: TF01-11 sp001414325
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp001414325
• CAZyme ID: MGYG000000250_02533
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
850		93347.59	8.716

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000250	3613289	Isolate	China	Asia

• Gene Location: Start: 62272; End: 64824 Strand: -

Full Sequence      

MRLKKITTVLMAAAMCISGLTAVPADANAAASSSAASSTTRISVHDPSIFYDSSTGSYNI
YGSHMAQASSKDLRNWSAMRTQGYTNKSLYASENVEGIYYIKNKFSGLYLDIENGSAQDG
ANIRQWSYNGSDAQKFKFVSTGDGYYYILTGATSYKKCVDVDGGSSKDGTNIMQWSYWGG
EMQKYRIVQNADGTYAILTKASDCKSGLDVYDWSKSAGGNINEWNYWGGDCQKWELVTAV
KNSGSTKASKNESLEQSLASSFQWAGYNDSDCKGGYGVWAPDVIYNKNYVWKDGSKGAYM
IYYCTSSTAVRSCIGYGVSKSATGPFSYVDTVVYSGFTKGDVNVTTKSNLGTKTVNTNYS
NTNIPKLINNGKVEKVGNWFSSNGAYNSSFYPNAIDPCILFDANGKLWMTYGSWSGGIYI
LELDAATGQPKYPKTTSGNTDGYFGKKIAGGYKKSGEAPYIQYDAESGYYYLYVTYGWLG
ADGGYHMRMYRSKTINGNYVDAAGNSAVFSAGTNQADRGIKVMGNYNFTPIMQGYKSAGH
NSAFIDTDNQRYLVYHTRFDSGNESHEVRVHQQFLNQDNWPVTAVYEYLGSTISKTGYSA
SDMLGEYEFVNHGKDASTKNVGMLTTQKVKLNSNGKITGDVTGSWSYIKGTYYCQMVIDG
VMYKGVFFKQKDETPSHNEVMTFSLIGKNNQTIWGTKNSVKVSKTEGIFYIRNKFSGKYL
DVADGSSADHANIQQWAYNGLASQKYKIVSNGDGYYYILTGASNYTKALDVAMGSAADGT
NIVQYSLNKGTNQLFKLSKQSDGTYAVLSKASSCKSGLDVYDWSRDSGGNINQWNFWGGD
CQKWILAAVK

Enzyme Prediction     

EC	3.2.1.99

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	230	581	7.7e-91	0.9096774193548387
CBM13	95	240	5.9e-23	0.7127659574468085
CBM13	705	847	7.8e-21	0.6968085106382979

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18832	GH43_GsAbnA-like	5.57e-119	230	576	27	332	Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. 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. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). 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. Many of these enzymes 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.
COG3507	XynB2	8.18e-60	264	765	82	516	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08998	GH43_Arb43a-like	5.36e-45	274	572	55	274	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.
cd08988	GH43_ABN	5.44e-38	274	574	56	276	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.
pfam16369	GH43_C	1.08e-30	586	695	2	106	C-terminal of Glycosyl hydrolases family 43. This is the C-terminal of Glycosyl hydrolases family 43. It is around 100 residues in length from various Bacteroides species. The function of this family is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAV13132.1	2.34e-296	40	697	52	708
ADL52282.1	2.34e-296	40	697	52	708
QYR21530.1	7.13e-271	40	697	42	701
QKS43770.1	7.57e-268	41	697	44	701
AIQ51381.1	7.27e-266	31	697	35	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HO9_A	3.33e-144	254	704	101	553	Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
5HO0_A	1.30e-141	254	704	101	553	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]
4KCA_A	2.90e-79	260	697	199	637	CrystalStructure of Endo-1,5-alpha-L-arabinanase from a Bovine Ruminal Metagenomic Library [Bos taurus],4KCA_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from a Bovine Ruminal Metagenomic Library [Bos taurus]
3LV4_A	2.43e-72	256	696	62	441	Crystalstructure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580],3LV4_B Crystal structure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580]
2X8F_A	9.39e-72	256	697	85	469	Nativestructure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis],2X8F_B Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P42293	5.01e-71	256	697	85	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
A5IKD4	3.67e-69	251	697	78	468	Extracellular endo-alpha-(1->5)-L-arabinanase OS=Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) OX=390874 GN=Tpet_0637 PE=1 SV=1
P95470	5.78e-13	393	581	155	331	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
Q93HT9	8.10e-10	393	513	144	257	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B3EYM8	8.24e-10	393	513	144	257	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB 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
0.000230	0.999009	0.000238	0.000199	0.000167	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000250_02533.