CAZyme Information: MGYG000003238_01178

Basic Information

• Species: UBA1375 sp002305795
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1375; UBA1375 sp002305795
• CAZyme ID: MGYG000003238_01178
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1534		166897.56	3.8575

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003238	1468351	MAG	United States	North America

• Gene Location: Start: 4166; End: 8770 Strand: -

Full Sequence      

MKKRSILAWILSFAMLCSCFSAGMLPASAQEVDGVEFPESLAPGNDANIHDPSIFYDQAS
GYYYVYSTGMGGDVLTVVRTQDPNMRSWERLEFDTSGLITDEILAVTPVYNIWAPDMVKV
GEEYRLYYSCSTGGSGNSCIAMATSDRPDGGFVFQGIVVQSSQSSWGTTGNAIDPCIVTE
ESTGDRYMTWGSFGAGIFIQKMTEDGFLDQSSPAVNIAYRPQPQNGVEGPYIRYNADTGY
YYLFVSYGNLNNNYNVRVARSRSITGPYLDDMGNDMAADSNGSLDSDIGYKLTSGFQYPG
GDNDFGAAWMGLGHCSVLEQNGTWILYSHARMNAGGGEYGGLWMQCHQLVWSEEGWPLMV
SAFYDGEEEQQVSPGAMVGTFLRIDLSKDDSDLTRTSTEMTFAADGTFTTEAYGDGRWDF
TGENTVYCFYDSGRIDQLKVLPGWDQENGRGCYGITGDDQDTHLQVWGKKVSDNYNVAEE
VSFTPGWLVQPSQDDLLAHYPLQYDLSDATRSYADGVITGAGYSMDSGVLHLEGGAKATG
NYLQLPTGMLDGQDTMTISFWAENENDSGNYAAFFVGSTEANPLNYLLLNPANPSGYVKL
AFTDSVSANNAPWETEVGFAASNNATGNSVEKVDGLALYTIVVEGNTLMLYVNGQPAGNA
VTLSRTISDLGENLAVYLAASSYGDDLMAGSFRDLQIYDTALNRIQVQQIYGQKEAILAQ
WALDSIDLEESDALRHSLTLPTQSLGYEITWSTSNPQAISQSGEVFRPAAGSQPATVTLT
ASATAGNQVLTKDFTFTVLPQQEDINVDAQYYLSLIDLPEYLYTDLALPATTGNQDSIIW
SSSEEGVLGSDGSLNTDSTRPQTVTLTATLTYGAGSAQKEFSLTVTGGYPYGVFGYMTGT
TDLDGSLHLAEVNPEGQVTQLNSGNGVLYADLSGVAANNNAYKSADTGLYFTSAALARQP
ESGYLLAVSRSMEQDTVWFYTTSDLVQYDSGTPLTLQEGTNVAKIHSLVYSDSQIQVSWT
SDTGESYTTLVAADFSRVLSGQEAQPVTVYAPYALPEGALAETTGVLYLTQEEYTALTNR
LSDPTNNGMEEIPEIHTSAGVIPQMPQSVTATYTDGSTQEFGVQWDLEGLDFTQPGRYTV
TGTVEQTQYENPFILYRADPYIVQAEDGSYYFTASYADENYSSYDRVTLRHADTIEGLAE
AADVTLWTGNLLWAPEIHYINGQWVMYYATGIKACTRICREGGDPMNPADWGAEIPFDTI
PNYNSTSSLDMTYFEVNGTGYVIWAQMGAGNAIQRSTLYMAQLDPNDPSRITGDTITLTT
PQYAWEMVNYMVNEGPSVLQKDGKIYVSFSASGTGVEYCMGLLTADADSDLMDPASWSKT
GYPVLTSQNVPGEYGPGHNSFTYDEDGNAIFVYHARSESSNSGDTLADSGRHARIKRVHW
AADGTPILSMSYEEELAVENRTVTVTIVVEEEPLAQDDLNQDDQVDVLDVMTLAQAAVGS
FTLPEGVDGDQNQDGALNVLDVMIFAQRLVSRNR

Enzyme Prediction     

No EC number prediction in MGYG000003238_01178.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	1157	1446	1.7e-79	0.9966555183946488
GH43	48	357	3e-70	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18819	GH43_LbAraf43-like	1.42e-113	1158	1416	1	277	Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). 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. 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.
cd18818	GH43_GbtXyl43B-like	1.40e-89	1158	1416	1	273	Glycosyl hydrolase family 43 such as Geobacillus thermoleovorans IT-08 beta-xylosidase/exo-xylanase (GbtXyl43B). This glycosyl hydrolase family 43 (GH43) subgroup includes the characterized enzymes Geobacillus thermoleovorans IT-08 beta-xylosidase (EC 3.2.1.37) / exo-xylanase (GbtXyl43B), and Paenibacillus sp. strain E18 alpha-L-arabinofuranosidase (EC 3.2.1.55) Abf43B. 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. 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.
cd18817	GH43f_LbAraf43-like	1.50e-86	1158	1416	1	262	Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. 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.
COG3940	COG3940	2.57e-85	1148	1446	4	308	Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
cd08998	GH43_Arb43a-like	2.20e-75	49	352	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBF42300.1	7.53e-176	506	1476	58	1067
CAD6011226.1	2.55e-152	491	1469	22	1023
QNF28727.1	3.26e-145	492	1471	36	1017
AZZ51743.1	4.46e-131	494	1470	35	1037
AIQ31573.1	1.70e-97	915	1469	651	1230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AKF_A	3.25e-68	1149	1446	11	310	Crystalstructure of exo-1,5-alpha-L-arabinofuranosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKG_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKH_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranotriose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKI_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido [Streptomyces avermitilis MA-4680 = NBRC 14893]
3K1U_A	1.05e-66	1145	1459	5	325	Beta-xylosidase,family 43 glycosyl hydrolase from Clostridium acetobutylicum [Clostridium acetobutylicum]
5M8B_A	2.71e-63	1144	1446	22	335	ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
5M8E_A	6.44e-61	1142	1447	18	334	Crystalstructure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria],5M8E_B Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria]
4KC7_A	1.33e-34	47	419	31	419	CrystalStructure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC8_A Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q82P90	2.49e-67	1149	1446	37	336	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=Araf43A PE=1 SV=1
P82594	4.81e-57	1149	1424	50	327	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
G4MMH2	5.60e-57	1149	1446	41	342	Alpha-L-arabinofuranosidase B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=abfB PE=1 SV=1
A5IKD4	6.93e-34	47	419	28	416	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
P42293	1.22e-33	46	426	33	427	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2

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
0.000530	0.544685	0.453893	0.000374	0.000276	0.000217

TMHMM  Annotations     

start	end
5	27