CAZyme Information: MGYG000001639_03177

Basic Information

• Species: Haloferax massiliensis
• Lineage: Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Haloferax; Haloferax massiliensis
• CAZyme ID: MGYG000001639_03177
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
502	MGYG000001639_4|CGC2	54084.41	3.7524

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001639	3991467	Isolate	not provided	not provided

• Gene Location: Start: 88748; End: 90256 Strand: +

Full Sequence      

MLEDMTKRHGSNNIDRRTVLKSLGAGAVATVGGLGLSGTVSADESSTHYHNPVGPIGFGD
VSIIEDNGTYYAYGTETPQDIIPIAESTDMYNWSYIAPALTETPGWHPTESDPGCWAPDI
RYHDGQYHLYYSLSVWGSDNAGIGLATSDTPDGPFTDQGPVIESGDLDLTNCIDADTVIV
DGQPWLVWGSYEGIYAVQMNGAMDDIVPGTEFQMAGQMIEGPVMLQDNGYWYLFYSSGQC
CEGYDSTYRLECGRATSFTGPYYNQNGTDLRDLTETHQGVPILEGNSEFTGPGHNDVFRG
PDGDWWCFYHVEATADDETRYMMQDRIEWDNNDWPVIACNGVPSSEAPVPGEPSGCESGP
ISDGTYAITNVNSGKLLEVANAGTADGDNVRQYADTGSACQDWDVTANGDGTYAITNVNS
GLWLEVASAGTAEGDNIQQYSNTTHPTQAWTIEDAGGGEYRLVNANSGLLAEVANAGTAD
GDNVQQWSDNGGSHQRWTFTSV

Enzyme Prediction     

No EC number prediction in MGYG000001639_03177.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	49	335	2e-88	0.9966555183946488
CBM13	364	501	1.4e-28	0.6914893617021277

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	1.55e-125	51	329	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	3.22e-80	63	330	7	278	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	1.21e-59	60	329	2	277	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.
cd18830	GH43_CjArb43A-like	2.32e-59	50	330	2	291	Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes the bifunctional Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). It 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	9.07e-55	51	336	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKU09509.1	8.32e-295	28	409	1	382
QIB79924.1	4.80e-294	28	409	1	382
QLH81511.1	1.05e-279	5	409	1	412
QLC35059.1	4.92e-185	14	409	10	403
ADB63307.1	6.28e-180	5	405	1	405

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B7K_A	2.04e-48	60	336	23	300	GH43Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_B GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_C GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_D GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
3CU9_A	1.18e-40	60	338	26	313	Highresolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus [Geobacillus stearothermophilus]
3D60_A	1.64e-40	63	338	29	313	ChainA, Intracellular arabinanase [Geobacillus stearothermophilus]
3D5Y_A	8.46e-40	60	338	26	313	ChainA, Intracellular arabinanase [Geobacillus stearothermophilus],3D5Z_A Chain A, Intracellular arabinanase [Geobacillus stearothermophilus]
6F1G_A	8.67e-40	60	338	27	314	Thestructure of AbnB-E201A, an intracellular 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B3EYM8	6.64e-40	60	338	27	314	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
Q93HT9	2.32e-38	60	337	27	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
P94522	7.63e-37	60	300	44	291	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
P95470	2.47e-36	36	337	23	333	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
P42256	1.97e-30	65	337	41	321	Arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus niger OX=5061 GN=abnA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	0.000000	0.999932	0.000067	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001639_03177.