CAZyme Information: MGYG000000067_02224

Basic Information

• Species: Lachnoclostridium_B sp900066765
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium_B; Lachnoclostridium_B sp900066765
• CAZyme ID: MGYG000000067_02224
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1875	MGYG000000067_13|CGC2	205520.34	4.2488

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000067	3710135	Isolate	United Kingdom	Europe

• Gene Location: Start: 79058; End: 84685 Strand: -

Full Sequence      

MKKGKKAVKHFSRVILALLLAVSMIPLPAAASASSDNGDGTYNNPVIYADVPDVDVIRVG
DTYYMSSTTMHLSPGVPIMKSKDLVNWEIVNYVYDVMDDGDAMSLRNGQSAYANGSWASS
LRYYDGKYYVSFMSYTTGKTYFYTTDDIENGVWTHTEVKGGYHDMGLFFDDDGKIYMAYG
GGTIKICEMEIVENGLQIKPGTEKVLISDAWKGTALEGTGGLAEGTHVQKINGKYYVFMI
TWPAENADAGTKGMRTELCFRADSIEDFVNGNWERKIVLQDKGAAQGGIIDTVDGDWYGM
VFRDMGPVGRCPVLVPVTWTDGWPMMGNEKGEVDDTAVMPLESWGEKSVVTSDEFYNGEE
RAAYTKQYEMYGATGVPTAADVDEEIEALEVYDGDELIENGSFDDGTEHWTVNDPADIEV
VEEDGNKILKVTNRTTTGSGPRQDITGDVVEGGTYKITAKIKYDHPNSPATKNFNMCIYN
GKSYVNGDSIQIMGSGTITKGEWGTVSGTFTVKEGTDISASAIFLETSWAANPTADNDLM
DFYVDDVSVIAESIPKEEGDNLIKNGGFEDELSRWTGRENCTLTLDTTEKVSGNSSVKVT
DRKVTGSGPQQDVSGLLEAGDIIDVSYNIKYTTGPDTRNFILTAFYDGTYKNIVGGNVKK
GEWTKISSSYTVPEDMNTDNLVFFLETSWTPEQDPENDRMDYYVDDLVVTKRVIEQPTMD
ERSYNGSNLKLEWQWNHNPNNACWSLTDRAGYLRMTTGSTCKTLTEARNTLTQRTYAPQC
SGNVALEVGNMKNGDVAGLAAFAAKYGYVGVKMDGGKKYLVMVGTKENGSDNFEPYEADS
VELTQDRVYLKIDFDFNSNKAYFYYSLDGKSWTKIGDELPMVYSLAHFMGYRFGLFNYAT
KSTGGYVDFDYFRIEDGNSGTEGTKDAGTAKMENVQAAGVANAEVEIPVKMTSLPEGNYK
SISASFGIPSQLKVTDVVFNEKNVTGTATYSYSNGQLLLTVNGEGVGYTATEEDDVFATI
KLKAADYVTADIDATVQADYIQTTGDKVSYDVSGAKSVVTLKYVDMGALAKKPGDSNPLV
DHKFGADPYAMEYDGRVYIYMTNDSQEYEAQNNGSVDNTYGNINTINVISSADMVNWTDH
GSIPVAGKNNPDGAAKWATCSWAPAAAHKTIDGKEKFFLYFADGGGGIGVLEADSPIGPF
VDPIGQALVPPGSAHADGVIWLFDPAVLVDDDGTGYLYYGGGVPDNDANNPKTSRVVKLT
DDMVHLDGDAQVIDAPAIFEDSGIHKYGEKYYYSYCSNFSQHAAGYPGQGIICYMESDSP
MGPFEYKGEILDNPAKFFGVGGNNHHAIFEFGGEYYITYHAQTLGKALGKANGYRSTHIN
KVNISKDGTIEPITADMKGISLLKTVDPYARLEGEMFAWNSGIKTAVSKQEGSMVKTLNM
EVTDIQNGDWTAIAGLDFGVSGAKKLTANIAAKEGGKVEIRLDSADGTLAGTLEVPAGDG
NYKKVECELEGVTGEHNVFFVFTGADGKDLMTVDYWQFEETEVKVDKTDLKEAIDKATAV
DITKYTEETVEKLQEALAKANEVFKDDNATQQEVDDAAKALTDAQEALKEIEKPEPVVTD
KKALEAAVKAAVADTEKAKYTEESWAAYEEALKKAEEVLAKEDATQQEIDDAVAALDKAA
KALQAKGLPYEDVVESDWFYDEVAYNYYEEIMTGMDPTHFGPYVILPRAQFATILHRIEG
KPAAEYTNRFPDVPDGQFYSTAVLWAADAEVITGYTDSGYFGTNDPITREQMVTMMYRYA
EYKKYESKEPTDISAFTDADEVTEFAEKAMKWAVANGIIAGKENEDGSYRLDPQGGTSRA
ECAIIIQRFMEKFEK

Enzyme Prediction     

No EC number prediction in MGYG000000067_02224.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	1076	1390	2.7e-136	0.9967845659163987
GH43	43	324	8.9e-96	0.996309963099631
CBM22	561	687	1.3e-27	0.9847328244274809
CBM22	397	527	7.9e-27	0.9770992366412213
CBM6	1414	1539	2.5e-25	0.855072463768116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09003	GH43_XynD-like	5.64e-163	1077	1393	1	315	Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd09001	GH43_FsAxh1-like	1.35e-136	41	327	1	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.
cd08990	GH43_AXH_like	3.69e-64	1086	1392	1	269	Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd18618	GH43_Xsa43E-like	3.74e-54	1084	1392	1	275	Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd08989	GH43_XYL-like	3.59e-50	44	320	1	272	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
ANY68648.1	0.0	39	1544	30	1373
AZT91394.1	0.0	5	1538	10	1345
ABP67988.1	0.0	4	1538	2	1345
AAB87371.1	0.0	4	1538	2	1345
BCS82265.1	0.0	43	1538	57	1347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3C7E_A	4.64e-163	1069	1540	6	486	Crystalstructure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis. [Bacillus subtilis],3C7F_A Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus subtilis in complex with xylotriose. [Bacillus subtilis],3C7H_A Crystal structure of glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with AXOS-4-0.5. [Bacillus subtilis],3C7O_A Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with cellotetraose. [Bacillus subtilis]
3C7G_A	4.80e-163	1069	1540	7	487	Crystalstructure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with xylotetraose. [Bacillus subtilis]
6MLY_A	1.15e-115	44	916	23	512	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]
5A8C_A	1.40e-63	1078	1400	30	324	ChainA, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus],5A8D_A Chain A, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus]
3ZXJ_A	6.57e-39	41	324	7	288	Engineeringthe active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXJ_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45796	1.93e-164	1069	1538	31	507	Arabinoxylan arabinofuranohydrolase OS=Paenibacillus polymyxa OX=1406 GN=xynD PE=1 SV=1
Q45071	6.19e-162	1069	1540	32	512	Arabinoxylan arabinofuranohydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynD PE=1 SV=2
T2KN85	2.40e-36	29	355	38	382	Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22160 PE=1 SV=1
Q9WXE8	9.29e-28	36	354	35	331	Putative beta-xylosidase OS=Prevotella ruminicola OX=839 PE=3 SV=2
A7LXT8	3.05e-21	42	333	23	306	Non-reducing end alpha-L-arabinofuranosidase BoGH43A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02654 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
0.000284	0.998988	0.000227	0.000177	0.000161	0.000142

TMHMM  Annotations     

start	end
12	34