CAZyme Information: I317_05056-t43_1-p1

Basic Information

• Species: Kwoniella heveanensis
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella heveanensis
• CAZyme ID: I317_05056-t43_1-p1
• CAZy Family: GH71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1330	KI669534|CGC2	148491.38	5.7955

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KheveanensisCBS569	8002	1296119	131	7871

• Gene Location: location=KI669534:87701-92943(+)

Full Sequence      

MSTRNPILPGFNPDPSICHVNSDYFLATSTFEFFPGVAIYHSTDLVDWVLIGHALTRHSQ
LTIRGTQPGFGVWAPTLRHHKGRFYVATAIAQGWGDQSTTPRGFYVSTDNIWDDTTWTDP
VFFDVLGIDQDLFFDDDGRTYLSVAKTKNDGLPHPTWEAIWGVEIDLASGRNKGSPILLR
RSTTDSGVAEGSHIFKRGGWYYLCVAEGGTEEGHQEWIFRSESPLGPYEEPEAKGFNPIL
YNAPDLPIRCTGHTDFVEATDGQWWAVFLGLRPSSSSGIAHMGRETFIAPVEWDSQGWPV
INGGRPVTSEVRGLPHSKPPGAWTDPFSKSGLTKGWYHSQTPYRKEYNTTEREGWLALYG
NGYMIHDSACPSMLLRKQNSLSGNWSVRIDFTPSNEYEEAGTTVFRSKFGFIALLLRKRR
GAPKQVVLRWTDKETDSYKHTSLKASSTIAIAQISFEHAGVKGFVDTDRPRLSWRFEGDA
RDWQQISYDIKVARSSGSVEEFHVDSSKSNLVPWPSTIPLAPCEIAKISVKANGIGRQDT
DWAHAQVEAALLTGSDWSAQMITAADLSLQSPLTQSAPQRPFYVYREFEIKRLDGIARLY
ATAFGMYDVTINGVPASDQVLKPGWTSYDHRLYYQVEDISSLLKVGRNRVMVAVGEGWYS
GRIGFGGGKRWIYGEKNGVMMEIRVGKEVVISTDETWKWSCGPILASELYDGEVYDARLG
IDDYVSEGSSVQLLDRPTASLILDKAPIKRTKEVPVKEIIISPSGKCILDFGQNLVGWVR
INRGAKGKAPGDRIVLSHVEVLEEGEISTRPLRFAKCQDTIICGSDPHALDAWEPTFTYH
GFRYVQVEGWGDDIDPSHFTAVIIHTDMERTGWFSSSHPMINRLHDNVLWSMRGNFVGLP
TDCPQRDERLGWTGDLQVFCKTASFLFDTTSILSGWLQDLAAEQTQNDNVPPLVVPDTFK
RQFNGEPDPAAIWGDVSVLSPLDLFESSGDSAILERQYSSMYDWLKKGIPRDADGLWGQR
TPMDSQFGDWLDPYAPPDFPGDGRTDPYFVANAYLVYVTRKMAEVCHILGKQEEAAELQA
EWSRSITSFADRYITKAGRTVSDSQTALVLALQFDLLSSPSQREVAVGRLEELVRSNVFK
IGTGFAGTPIILDVLANNDRLHLAYRMLQEKQCPSWLYCVSMGATTIWERWDSMRPDGSI
NPGEMTSFNHYALGAVASFMHSTIGGISPLVPGWKKIRIAPRPGGTVTWADVTHMSPYGL
VRCAWRIENSKLHLSITVPPNTTAVIDVGDLQTAIGSGHRQFEVAYQADTRWPPKPIYKS
MTIPLIDEIA

Enzyme Prediction     

EC	-	-	3.2.1.40:1	3.2.1.40:8	3.1.1.73:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	762	1286	6.1e-164	0.9880952380952381
GH43	4	299	9.5e-117	0.993421052631579
CBM91	325	492	4.8e-22	0.76
CBM67	574	725	3.3e-19	0.8181818181818182

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350129	GH43_XynB-like	4.32e-145	5	301	1	285	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.
407469	Bac_rhamnosid6H	4.55e-132	869	1224	1	340	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
350154	GH43_PcXyl-like	8.86e-94	5	300	1	292	Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). This glycosyl hydrolase family 43 (GH43) subgroup includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a characterized bifunctional enzyme with beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) activities. This subgroup belongs to the GH43_XybB subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_XybB subgroup includes enzymes having beta-1,4-xylosidase and alpha-L-arabinofuranosidase activities. Beta-1,4-xylosidases 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. The GH43_XybB subgroup includes Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. 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.
350114	GH43_SXA-like	4.55e-89	5	301	1	292	Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. 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. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. 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.
350103	GH43_XYL-like	2.15e-77	5	294	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
AAW44459.2|GH78	1.28e-279	470	1330	24	866
AFR96797.2|GH78	4.04e-272	448	1330	2	866
AUB26756.1|GH78	4.04e-272	448	1330	2	866
UOH83198.1|GH78	1.49e-269	448	1330	2	857
UPK95035.1|GH78	1.10e-267	448	1317	2	859

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6GSZ_A	6.67e-247	449	1304	2	865	Crystal structure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
3W5M_A	1.78e-130	503	1286	214	992	Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6I60_A	1.43e-91	442	1291	23	901	Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
5Z5D_A	2.46e-83	1	431	1	420	Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 [Geobacillus thermoleovorans],5Z5F_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose [Geobacillus thermoleovorans],5Z5H_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with D-xylose [Geobacillus thermoleovorans],5Z5I_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose and D-xylose [Geobacillus thermoleovorans]
5JOZ_A	2.50e-74	4	471	6	466	Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus],5JOZ_B Bacteroides ovatus Xyloglucan PUL GH43B [Bacteroides ovatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|T2KNB2|PLH20_FORAG	4.28e-135	463	1288	49	878	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
sp|Q82PP4|RHA78_STRAW	6.86e-130	503	1286	214	992	Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
sp|P9WF03|RHA78_ALTSL	4.75e-114	470	1284	51	874	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
sp|T2KPL4|PLH28_FORAG	3.09e-79	465	1298	46	918	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
sp|A7LXU0|GH43B_BACO1	1.84e-73	4	471	28	488	Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000020	0.000020

TMHMM  Annotations     

There is no transmembrane helices in I317_05056-t43_1-p1.